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时间：2015-07-20 17:48
PROTEIN BINDING
THE HIGH-RESOLUTION AND NEW FORM CRYSTAL STRUCTURE OF BAMA POTRA4-5
2 FROM E.COLI
MOL_ID: 1;
2 MOLECULE: OUTER MEMBRANE PROTEIN ASSEMBLY COMPLEX, YAET PROTEIN;
3 CHAIN: A;
4 FRAGMENT: POTRA45 DOMAIN (UNP RESIDUES 266-420);
5 ENGINEERED: YES
MOL_ID: 1;
2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
3 ORGANISM_TAXID: 83333;
4 STRAIN: K-12;
5 GENE: ECDH1_3426, YAET;
6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
7 EXPRESSION_SYSTEM_TAXID: 562;
8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
10 EXPRESSION_SYSTEM_PLASMID: PET-28A
POTRA FOLD, INSERTION OF OUTER MEMBRANE PROTEINS, PROTEIN BINDING
X-RAY DIFFRACTION
Z.Q.GAO,H.ZHANG,Y.H.DONG
10-AUG-11 3Q6B
H.ZHANG,Z.Q.GAO,H.F.HOU,J.H.XU,L.F.LI,X.D.SU,Y.H.DONG
HIGH-RESOLUTION STRUCTURE OF A NEW CRYSTAL FORM OF BAMA
TITL 2 POTRA4-5 FROM ESCHERICHIA COLI.
ACTA CRYSTALLOGR.,SECT.F
2 RESOLUTION.
1.50 ANGSTROMS.
3 REFINEMENT.
: PHENIX (PHENIX.REFINE: 1.6.4_486)
: PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
: DAVIS,KRESHNA GOPAL,RALF GROSSE-
: KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
: TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
: MORIARTY,REETAL PAI,RANDY READ,JANE
: RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
: SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
: LAURENT STORONI,TOM TERWILLIGER,PETER
REFINEMENT TARGET : ML
DATA USED IN REFINEMENT.
RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
RESOLUTION RANGE LOW
(ANGSTROMS) : 25.79
MIN(FOBS/SIGMA_FOBS)
COMPLETENESS FOR RANGE
(%) : 92.9
NUMBER OF REFLECTIONS
FIT TO DATA USED IN REFINEMENT.
(WORKING + TEST SET) : 0.149
(WORKING SET) : 0.147
FREE R VALUE
FREE R VALUE TEST SET SIZE
(%) : 5.060
FREE R VALUE TEST SET COUNT
FIT TO DATA USED IN REFINEMENT (IN BINS).
RESOLUTION RANGE
NWORK NFREE
1 25.7975 -
BULK SOLVENT MODELLING.
METHOD USED
: FLAT BULK SOLVENT MODEL
SOLVENT RADIUS
SHRINKAGE RADIUS
ERROR ESTIMATES.
COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)
PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
FROM WILSON PLOT
(A**2) : NULL
MEAN B VALUE
(OVERALL, A**2) : NULL
OVERALL ANISOTROPIC B VALUE.
B11 (A**2) : 0.28620
B22 (A**2) : -1.58070
B33 (A**2) : 1.29450
B12 (A**2) : -0.00000
B13 (A**2) : -0.22290
B23 (A**2) : -0.00000
TWINNING INFORMATION.
FRACTION: NULL
OPERATOR: NULL
DEVIATIONS FROM IDEAL VALUES.
CHIRALITY :
PLANARITY :
TLS DETAILS
NUMBER OF TLS GROUPS
NCS DETAILS
NUMBER OF NCS GROUPS : NULL
OTHER REFINEMENT REMARKS: NULL
4 3Q6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-11.
REMARK 100 THE RCSB ID CODE IS RCSB063248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200
EXPERIMENT TYPE
: X-RAY DIFFRACTION
REMARK 200
DATE OF DATA COLLECTION
: 04-DEC-10
REMARK 200
TEMPERATURE
(KELVIN) : 100
REMARK 200
REMARK 200
NUMBER OF CRYSTALS USED
REMARK 200
REMARK 200
SYNCHROTRON
REMARK 200
RADIATION SOURCE
REMARK 200
REMARK 200
X-RAY GENERATOR MODEL
REMARK 200
MONOCHROMATIC OR LAUE
REMARK 200
WAVELENGTH OR RANGE
(A) : NULL
REMARK 200
MONOCHROMATOR
: DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200
REMARK 200
DETECTOR TYPE
REMARK 200
DETECTOR MANUFACTURER
: MARMOSAIC 225 MM CCD
REMARK 200
INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200
DATA SCALING SOFTWARE
: HKL-2000
REMARK 200
REMARK 200
NUMBER OF UNIQUE REFLECTIONS
REMARK 200
RESOLUTION RANGE HIGH
(A) : 1.500
REMARK 200
RESOLUTION RANGE LOW
(A) : 50.000
REMARK 200
REJECTION CRITERIA
(SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200
COMPLETENESS FOR RANGE
(%) : 95.3
REMARK 200
DATA REDUNDANCY
REMARK 200
(I) : 0.07400
REMARK 200
(I) : 0.07400
REMARK 200
FOR THE DATA SET
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200
HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200
HIGHEST RESOLUTION SHELL, RANGE LOW
(A) : 1.55
REMARK 200
COMPLETENESS FOR SHELL
(%) : 83.1
REMARK 200
DATA REDUNDANCY IN SHELL
REMARK 200
R MERGE FOR SHELL
(I) : 0.33600
REMARK 200
R SYM FOR SHELL
(I) : NULL
REMARK 200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3OG5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS
(%): 38.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1M SODIUM
REMARK 280
CACODYLATE PH 6.5, 30% PEG 8000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280
TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290
REMARK 290
REMARK 290
REMARK 290
REMARK 290
X+1/2,Y+1/2,Z
REMARK 290
-X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290
WHERE NNN -> OPERATOR NUMBER
REMARK 290
MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290
1...000000
REMARK 290
0...000000
REMARK 290
0...000000
REMARK 290
2 -1...000000
REMARK 290
0...000000
REMARK 290
0...000000
REMARK 290
1...000000
REMARK 290
0...000000
REMARK 290
0...000000
REMARK 290
4 -1...000000
REMARK 290
0...000000
REMARK 290
0...000000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.
BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350
1...000000
REMARK 350
0...000000
REMARK 350
0...000000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465
M RES C SSSEQI
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OG5
RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BAMA POTRA45 TANDEM
C9QRL1_ECOD1
SEQADV 3Q6B MET A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B GLU A
EXPRESSION TAG
SEQADV 3Q6B ASN A
EXPRESSION TAG
SEQADV 3Q6B LEU A
EXPRESSION TAG
SEQADV 3Q6B TYR A
EXPRESSION TAG
SEQADV 3Q6B PHE A
EXPRESSION TAG
SEQADV 3Q6B GLU A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B MET A
EXPRESSION TAG
SEQADV 3Q6B ALA A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B MET A
EXPRESSION TAG
SEQADV 3Q6B THR A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B GLN A
EXPRESSION TAG
SEQADV 3Q6B GLN A
EXPRESSION TAG
SEQADV 3Q6B MET A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B ARG A
EXPRESSION TAG
MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
GLU ASN LEU TYR PHE GLU GLY SER HIS MET ALA SER MET
THR GLY GLY GLN GLN MET GLY ARG TYR LYS LEU SER GLY
VAL GLU VAL SER GLY ASN LEU ALA GLY HIS SER ALA GLU
ILE GLU GLN LEU THR LYS ILE GLU PRO GLY GLU LEU TYR
ASN GLY THR LYS VAL THR LYS MET GLU ASP ASP ILE LYS
LYS LEU LEU GLY ARG TYR GLY TYR ALA TYR PRO ARG VAL
GLN SER MET PRO GLU ILE ASN ASP ALA ASP LYS THR VAL
LYS LEU ARG VAL ASN VAL ASP ALA GLY ASN ARG PHE TYR
VAL ARG LYS ILE ARG PHE GLU GLY ASN ASP THR SER LYS
ASP ALA VAL LEU ARG ARG GLU MET ARG GLN MET GLU GLY
ALA TRP LEU GLY SER ASP LEU VAL ASP GLN GLY LYS GLU
ARG LEU ASN ARG LEU GLY PHE PHE GLU THR VAL ASP THR
ASP THR GLN ARG VAL PRO GLY SER PRO ASP GLN VAL ASP
VAL VAL TYR LYS VAL LYS GLU
*141(H2 O)
A 3 LYS A 267
A 3 THR A 334
A 3 ARG A 321
ASN A 329 -1
B 3 TYR A 348
B 3 SER A 408
B 3 THR A 397
VAL A 405 -1
90.00 101.00
90.00 C 1 2 1
1...000000
0...000000
0...000000
0...001413
0...000000
0...031286
1.00 49.14
1.00 45.61
1.00 42.37
1.00 44.15
1.00 47.33
1.00 52.65
CD1 TYR A 266
1.00 53.12
CD1 TYR A 266
CD2 TYR A 266
1.00 54.47
CD2 TYR A 266
CE1 TYR A 266
1.00 55.76
CE1 TYR A 266
CE2 TYR A 266
1.00 56.05
CE2 TYR A 266
1.00 57.32
1.00 63.36
1.00 37.64
1.00 39.31
1.00 39.64
1.00 42.01
1.00 42.05
1.00 47.70
1.00 51.52
1.00 55.23
1.00 56.97
1.00 37.80
1.00 39.58
1.00 43.23
1.00 47.99
1.00 40.16
1.00 40.68
CD1 LEU A 268
1.00 42.94
CD1 LEU A 268
CD2 LEU A 268
1.00 40.27
CD2 LEU A 268
1.00 40.35
1.00 41.44
1.00 44.38
1.00 48.47
1.00 43.20
1.00 43.93
1.00 42.55
1.00 40.28
1.00 37.63
1.00 34.98
1.00 35.59
1.00 34.66
1.00 37.00
1.00 38.63
1.00 34.96
CG1 VAL A 271
1.00 37.00
CG1 VAL A 271
CG2 VAL A 271
1.00 36.61
CG2 VAL A 271
1.00 33.24
1.00 34.46
1.00 34.34
1.00 33.96
1.00 41.61
1.00 51.22
1.00 59.02
OE1 GLU A 272
1.00 60.50
OE1 GLU A 272
OE2 GLU A 272
1.00 63.72
OE2 GLU A 272
1.00 35.27
1.00 33.04
1.00 33.81
1.00 37.68
1.00 35.17
CG1 VAL A 273
1.00 36.37
CG1 VAL A 273
CG2 VAL A 273
1.00 35.13
CG2 VAL A 273
1.00 32.79
1.00 31.78
1.00 27.96
1.00 28.97
1.00 40.09
1.00 44.16
1.00 28.00
1.00 27.41
1.00 30.40
1.00 34.84
1.00 28.55
1.00 27.28
1.00 26.32
1.00 25.73
1.00 31.77
1.00 41.17
OD1 ASN A 276
1.00 44.11
OD1 ASN A 276
ND2 ASN A 276
1.00 42.29
ND2 ASN A 276
1.00 24.63
1.00 23.81
1.00 24.19
1.00 23.73
1.00 26.57
1.00 33.54
CD1 LEU A 277
1.00 38.44
CD1 LEU A 277
CD2 LEU A 277
1.00 36.52
CD2 LEU A 277
1.00 25.33
1.00 24.85
1.00 25.23
1.00 27.09
1.00 24.90
1.00 23.49
1.00 26.07
1.00 26.44
1.00 33.55
1.00 23.97
1.00 24.36
1.00 24.78
1.00 25.65
1.00 25.09
1.00 26.58
ND1 HIS A 280
1.00 30.54
ND1 HIS A 280
CD2 HIS A 280
1.00 30.15
CD2 HIS A 280
CE1 HIS A 280
1.00 30.94
CE1 HIS A 280
NE2 HIS A 280
1.00 29.14
NE2 HIS A 280
1.00 27.93
1.00 28.30
1.00 28.04
1.00 29.39
1.00 34.11
1.00 42.36
1.00 26.22
1.00 26.82
1.00 24.97
1.00 27.55
1.00 30.60
1.00 22.32
CA AGLU A 283
0.44 21.77
CA AGLU A 283
CA BGLU A 283
0.56 20.89
CA BGLU A 283
1.00 21.73
1.00 21.71
CB AGLU A 283
0.44 26.26
CB AGLU A 283
CB BGLU A 283
0.56 24.48
CB BGLU A 283
CG AGLU A 283
0.44 28.74
CG AGLU A 283
CG BGLU A 283
0.56 27.47
CG BGLU A 283
CD AGLU A 283
0.44 29.28
CD AGLU A 283
CD BGLU A 283
0.56 26.90
CD BGLU A 283
OE1AGLU A 283
0.44 32.22
OE1AGLU A 283
OE1BGLU A 283
0.56 32.71
OE1BGLU A 283
OE2AGLU A 283
0.44 26.43
OE2AGLU A 283
OE2BGLU A 283
0.56 24.41
OE2BGLU A 283
1.00 22.32
1.00 22.46
1.00 23.26
1.00 25.89
1.00 22.34
CG1 ILE A 284
1.00 22.97
CG1 ILE A 284
CG2 ILE A 284
1.00 25.07
CG2 ILE A 284
CD1 ILE A 284
1.00 24.24
CD1 ILE A 284
1.00 25.18
1.00 29.37
1.00 27.86
1.00 31.09
1.00 37.57
1.00 49.13
1.00 58.26
OE1 GLU A 285
1.00 62.94
OE1 GLU A 285
OE2 GLU A 285
1.00 59.62
OE2 GLU A 285
1.00 23.13
1.00 21.93
1.00 16.96
1.00 21.26
1.00 20.49
1.00 25.57
1.00 30.51
OE1 GLN A 286
1.00 30.87
OE1 GLN A 286
NE2 GLN A 286
1.00 31.66
NE2 GLN A 286
1.00 18.10
1.00 15.16
1.00 18.22
1.00 20.64
1.00 17.49
1.00 17.59
CD1 LEU A 287
1.00 20.84
CD1 LEU A 287
CD2 LEU A 287
1.00 19.24
CD2 LEU A 287
1.00 22.27
1.00 23.39
1.00 25.87
1.00 29.82
1.00 26.43
OG1 THR A 288
1.00 31.55
OG1 THR A 288
CG2 THR A 288
1.00 29.30
CG2 THR A 288
1.00 26.12
1.00 30.87
1.00 32.23
1.00 33.37
1.00 34.05
1.00 41.65
1.00 44.31
1.00 47.50
1.00 47.97
1.00 33.10
1.00 37.70
1.00 42.12
1.00 44.34
1.00 40.99
CG1 ILE A 290
1.00 45.51
CG1 ILE A 290
CG2 ILE A 290
1.00 40.16
CG2 ILE A 290
CD1 ILE A 290
1.00 48.56
CD1 ILE A 290
1.00 43.76
1.00 52.05
1.00 51.30
1.00 49.70
1.00 58.29
1.00 64.73
1.00 70.61
OE1 GLU A 291
1.00 71.81
OE1 GLU A 291
OE2 GLU A 291
1.00 72.91
OE2 GLU A 291
1.00 56.00
1.00 58.51
1.00 58.31
1.00 59.46
1.00 58.69
1.00 57.82
1.00 57.44
1.00 55.86
1.00 54.93
1.00 54.88
1.00 55.86
1.00 51.37
1.00 47.89
1.00 45.39
1.00 44.60
1.00 46.41
1.00 47.92
1.00 52.01
OE1 GLU A 294
1.00 51.56
OE1 GLU A 294
OE2 GLU A 294
1.00 55.85
OE2 GLU A 294
1.00 40.73
1.00 39.67
1.00 38.14
1.00 38.43
1.00 42.75
1.00 46.97
CD1 LEU A 295
1.00 48.45
CD1 LEU A 295
CD2 LEU A 295
1.00 48.71
CD2 LEU A 295
1.00 35.40
1.00 32.74
1.00 32.82
1.00 33.92
1.00 32.65
1.00 32.43
CD1 TYR A 296
1.00 36.81
CD1 TYR A 296
CD2 TYR A 296
1.00 33.94
CD2 TYR A 296
CE1 TYR A 296
1.00 36.93
CE1 TYR A 296
CE2 TYR A 296
1.00 34.78
CE2 TYR A 296
1.00 39.09
1.00 42.26
1.00 30.75
1.00 29.15
1.00 30.36
1.00 27.68
1.00 32.08
1.00 35.25
OD1 ASN A 297
1.00 34.88
OD1 ASN A 297
ND2 ASN A 297
1.00 40.00
ND2 ASN A 297
1.00 29.81
1.00 30.11
1.00 25.53
1.00 26.82
1.00 25.75
1.00 31.71
1.00 26.69
1.00 27.25
1.00 38.21
OG1 THR A 299
1.00 43.23
OG1 THR A 299
CG2 THR A 299
1.00 36.34
CG2 THR A 299
1.00 23.77
1.00 23.16
1.00 23.19
1.00 22.71
1.00 25.99
1.00 37.59
1.00 46.75
1.00 52.65
1.00 51.95
1.00 21.41
1.00 22.56
1.00 20.95
1.00 20.64
1.00 29.15
CG1 VAL A 301
1.00 30.94
CG1 VAL A 301
CG2 VAL A 301
1.00 31.76
CG2 VAL A 301
1.00 21.26
1.00 24.17
1.00 19.94
1.00 20.39
1.00 29.78
OG1 THR A 302
1.00 30.72
OG1 THR A 302
CG2 THR A 302
1.00 31.57
CG2 THR A 302
1.00 21.72
1.00 21.23
1.00 20.09
1.00 20.31
1.00 28.35
1.00 34.22
1.00 42.96
1.00 47.03
1.00 49.46
1.00 20.45
1.00 20.39
1.00 19.94
1.00 20.05
1.00 27.44
1.00 38.37
1.00 50.67
1.00 41.01
1.00 19.10
1.00 21.78
1.00 19.43
1.00 18.97
1.00 24.85
1.00 29.59
1.00 35.42
OE1 GLU A 305
1.00 38.87
OE1 GLU A 305
OE2 GLU A 305
1.00 37.41
OE2 GLU A 305
1.00 19.03
1.00 20.20
1.00 17.28
1.00 19.14
1.00 22.65
1.00 36.81
OD1 ASP A 306
1.00 41.02
OD1 ASP A 306
OD2 ASP A 306
1.00 40.09
OD2 ASP A 306
1.00 18.19
1.00 18.56
1.00 17.83
1.00 15.75
1.00 18.79
1.00 28.45
OD1 ASP A 307
1.00 33.30
OD1 ASP A 307
OD2 ASP A 307
1.00 27.52
OD2 ASP A 307
1.00 16.38
1.00 16.18
1.00 12.84
1.00 15.87
1.00 16.29
CG1 ILE A 308
1.00 18.27
CG1 ILE A 308
CG2 ILE A 308
1.00 17.59
CG2 ILE A 308
CD1 ILE A 308
1.00 20.79
CD1 ILE A 308
1.00 14.30
1.00 14.54
1.00 14.66
1.00 15.88
1.00 19.07
1.00 21.09
1.00 26.55
1.00 35.46
1.00 40.08
1.00 15.11
1.00 16.23
1.00 14.84
1.00 16.30
1.00 18.87
1.00 25.96
1.00 32.22
1.00 38.67
1.00 40.44
1.00 15.10
1.00 15.04
1.00 14.18
1.00 15.84
1.00 17.03
1.00 21.01
CD1 LEU A 311
1.00 24.22
CD1 LEU A 311
CD2 LEU A 311
1.00 24.97
CD2 LEU A 311
1.00 14.71
1.00 14.99
1.00 15.44
1.00 15.21
1.00 15.34
1.00 17.53
CD1 LEU A 312
1.00 19.86
CD1 LEU A 312
CD2 LEU A 312
1.00 18.85
CD2 LEU A 312
1.00 14.66
1.00 14.56
1.00 14.27
1.00 12.68
1.00 14.86
CA AARG A 314
0.53 15.20
CA AARG A 314
CA BARG A 314
0.47 15.95
CA BARG A 314
1.00 15.95
1.00 18.44
CB AARG A 314
0.53 14.14
CB AARG A 314
CB BARG A 314
0.47 16.32
CB BARG A 314
CG AARG A 314
0.53 16.74
CG AARG A 314
CG BARG A 314
0.47 19.34
CG BARG A 314
CD AARG A 314
0.53 17.82
CD AARG A 314
CD BARG A 314
0.47 16.67
CD BARG A 314
NE AARG A 314
0.53 20.35
NE AARG A 314
NE BARG A 314
0.47 15.13
NE BARG A 314
CZ AARG A 314
0.53 21.42
CZ AARG A 314
CZ BARG A 314
0.47 16.26
CZ BARG A 314
NH1AARG A 314
0.53 19.81
NH1AARG A 314
NH1BARG A 314
0.47 18.32
NH1BARG A 314
NH2AARG A 314
0.53 18.56
NH2AARG A 314
NH2BARG A 314
0.47 13.45
NH2BARG A 314
1.00 14.94
1.00 16.83
1.00 15.61
1.00 23.98
1.00 19.45
1.00 20.24
CD1 TYR A 315
1.00 24.35
CD1 TYR A 315
CD2 TYR A 315
1.00 24.07
CD2 TYR A 315
CE1 TYR A 315
1.00 28.02
CE1 TYR A 315
CE2 TYR A 315
1.00 27.89
CE2 TYR A 315
1.00 31.37
1.00 39.03
1.00 14.81
1.00 17.61
1.00 14.42
1.00 16.19
1.00 14.19
1.00 16.46
1.00 17.19
1.00 19.30
1.00 14.65
1.00 16.20
CD1 TYR A 317
1.00 17.40
CD1 TYR A 317
CD2 TYR A 317
1.00 16.82
CD2 TYR A 317
CE1 TYR A 317
1.00 20.08
CE1 TYR A 317
CE2 TYR A 317
1.00 18.19
CE2 TYR A 317
1.00 21.43
1.00 25.02
1.00 17.31
1.00 20.14
1.00 21.13
1.00 22.20
1.00 19.80
1.00 18.07
1.00 20.60
1.00 21.55
1.00 24.97
1.00 24.01
1.00 25.84
CD1 TYR A 319
1.00 30.74
CD1 TYR A 319
CD2 TYR A 319
1.00 24.45
CD2 TYR A 319
CE1 TYR A 319
1.00 31.35
CE1 TYR A 319
CE2 TYR A 319
1.00 24.97
CE2 TYR A 319
1.00 30.11
1.00 35.07
1.00 21.46
1.00 22.22
1.00 25.03
1.00 27.93
1.00 24.50
1.00 22.44
1.00 20.47
1.00 26.56
1.00 27.33
1.00 27.72
1.00 26.20
1.00 32.20
1.00 39.94
1.00 49.23
1.00 57.10
1.00 60.39
NH1 ARG A 321
1.00 63.17
NH1 ARG A 321
NH2 ARG A 321
1.00 61.05
NH2 ARG A 321
1.00 24.82
1.00 24.40
1.00 29.56
1.00 32.04
1.00 26.66
CG1 VAL A 322
1.00 26.27
CG1 VAL A 322
CG2 VAL A 322
1.00 24.67
CG2 VAL A 322
1.00 28.42
1.00 31.54
1.00 31.59
1.00 33.44
1.00 38.91
1.00 49.05
1.00 59.05
OE1 GLN A 323
1.00 62.28
OE1 GLN A 323
NE2 GLN A 323
1.00 63.12
NE2 GLN A 323
1.00 28.44
1.00 30.31
1.00 32.95
1.00 35.19
1.00 33.64
1.00 36.09
1.00 33.98
1.00 36.33
1.00 35.31
1.00 36.59
1.00 45.66
1.00 57.96
1.00 66.41
1.00 64.70
1.00 32.39
1.00 34.03
1.00 34.27
1.00 35.95
1.00 36.96
1.00 38.15
1.00 35.03
1.00 31.40
1.00 35.64
1.00 34.03
1.00 32.59
1.00 39.84
1.00 50.91
1.00 58.81
OE1 GLU A 327
1.00 61.33
OE1 GLU A 327
OE2 GLU A 327
1.00 62.26
OE2 GLU A 327
1.00 32.98
1.00 34.23
1.00 36.56
1.00 39.95
1.00 34.80
CG1 ILE A 328
1.00 35.14
CG1 ILE A 328
CG2 ILE A 328
1.00 36.14
CG2 ILE A 328
CD1 ILE A 328
1.00 38.45
CD1 ILE A 328
1.00 39.95
1.00 43.07
1.00 43.63
1.00 41.71
1.00 45.34
1.00 48.87
OD1 ASN A 329
1.00 48.09
OD1 ASN A 329
ND2 ASN A 329
1.00 50.42
ND2 ASN A 329
1.00 47.28
1.00 49.32
1.00 48.92
1.00 51.53
1.00 50.20
1.00 53.70
OD1 ASP A 330
1.00 53.36
OD1 ASP A 330
OD2 ASP A 330
1.00 56.85
OD2 ASP A 330
1.00 49.49
1.00 52.52
1.00 54.07
1.00 53.44
1.00 53.33
1.00 54.08
1.00 54.98
1.00 50.72
1.00 50.01
1.00 60.61
1.00 66.77
OD1 ASP A 332
1.00 69.52
OD1 ASP A 332
OD2 ASP A 332
1.00 68.23
OD2 ASP A 332
1.00 49.25
1.00 48.42
1.00 44.81
1.00 44.72
1.00 52.50
1.00 58.20
1.00 61.23
1.00 65.04
1.00 67.19
1.00 39.56
1.00 38.36
1.00 39.12
1.00 41.18
1.00 41.81
OG1 THR A 334
1.00 41.58
OG1 THR A 334
CG2 THR A 334
1.00 44.42
CG2 THR A 334
1.00 35.72
1.00 34.99
1.00 33.64
1.00 34.93
1.00 32.69
CG1 VAL A 335
1.00 33.92
CG1 VAL A 335
CG2 VAL A 335
1.00 35.18
CG2 VAL A 335
1.00 31.32
1.00 32.91
1.00 34.50
1.00 36.62
1.00 37.36
1.00 43.59
1.00 48.33
1.00 51.49
1.00 54.09
1.00 28.63
1.00 31.21
1.00 28.88
1.00 31.65
1.00 34.73
1.00 37.26
CD1 LEU A 337
1.00 39.08
CD1 LEU A 337
CD2 LEU A 337
1.00 42.36
CD2 LEU A 337
1.00 29.40
1.00 33.81
1.00 33.85
1.00 35.66
1.00 37.14
1.00 46.40
1.00 53.70
1.00 61.48
1.00 64.90
NH1 ARG A 338
1.00 65.46
NH1 ARG A 338
NH2 ARG A 338
1.00 65.88
NH2 ARG A 338
1.00 30.15
1.00 29.53
1.00 28.33
1.00 32.95
1.00 30.08
CG1 VAL A 339
1.00 29.53
CG1 VAL A 339
CG2 VAL A 339
1.00 29.40
CG2 VAL A 339
1.00 25.59
1.00 27.66
1.00 28.22
1.00 28.56
1.00 31.05
1.00 40.63
OD1 ASN A 340
1.00 44.63
OD1 ASN A 340
ND2 ASN A 340
1.00 44.21
ND2 ASN A 340
1.00 25.48
1.00 23.12
1.00 25.28
1.00 28.45
1.00 23.65
CG1 VAL A 341
1.00 26.15
CG1 VAL A 341
CG2 VAL A 341
1.00 27.49
CG2 VAL A 341
1.00 26.14
1.00 29.78
1.00 27.59
1.00 27.50
1.00 34.94
1.00 42.96
OD1 ASP A 342
1.00 43.88
OD1 ASP A 342
OD2 ASP A 342
1.00 47.51
OD2 ASP A 342
1.00 23.34
1.00 19.66
1.00 20.91
1.00 20.31
1.00 19.50
1.00 23.58
1.00 23.95
1.00 21.30
1.00 23.21
1.00 23.27
1.00 22.24
1.00 18.78
1.00 16.96
15.228 -10.223
1.00 28.47
14.934 -11.572
1.00 41.13
OD1 ASN A 345
13.916 -12.191
1.00 50.41
OD1 ASN A 345
ND2 ASN A 345
15.818 -12.029
1.00 39.27
ND2 ASN A 345
1.00 21.38
1.00 16.94
19.653 -10.120
1.00 15.70
19.374 -11.312
1.00 18.39
1.00 20.03
1.00 16.39
1.00 18.75
1.00 21.17
1.00 25.91
NH1 ARG A 346
1.00 29.29
NH1 ARG A 346
NH2 ARG A 346
1.00 32.04
NH2 ARG A 346
1.00 13.07
21.321 -10.511
1.00 12.50
22.785 -10.664
1.00 12.11
1.00 11.36
1.00 13.65
1.00 14.17
CD1 PHE A 347
19.436 -10.974
1.00 16.29
CD1 PHE A 347
CD2 PHE A 347
1.00 17.80
CD2 PHE A 347
CE1 PHE A 347
18.163 -10.988
1.00 18.12
CE1 PHE A 347
CE2 PHE A 347
1.00 22.23
CE2 PHE A 347
1.00 20.67
23.341 -11.831
1.00 11.65
24.782 -12.022
25.366 -12.324
1.00 10.12
24.638 -12.668
1.00 10.86
25.151 -13.095
1.00 11.79
24.768 -14.508
1.00 12.58
CD1 TYR A 348
25.684 -15.377
1.00 15.90
CD1 TYR A 348
CD2 TYR A 348
23.506 -14.999
1.00 15.69
CD2 TYR A 348
CE1 TYR A 348
25.341 -16.690
1.00 16.20
CE1 TYR A 348
CE2 TYR A 348
23.158 -16.310
1.00 18.26
CE2 TYR A 348
24.076 -17.147
1.00 17.90
23.702 -18.443
1.00 20.80
26.680 -12.198
1.00 10.30
27.334 -12.277
27.799 -13.698
1.00 10.33
28.531 -14.306
1.00 12.14
28.522 -11.299
1.00 10.98
CG1 VAL A 349
29.263 -11.465
1.00 12.41
CG1 VAL A 349
CG2 VAL A 349
1.00 11.34
CG2 VAL A 349
27.377 -14.216
27.834 -15.516
1.00 10.39
29.209 -15.349
1.00 12.60
30.207 -15.886
1.00 17.67
26.821 -16.118
1.00 13.30
27.193 -17.508
1.00 14.83
26.350 -17.911
1.00 16.85
26.776 -17.220
1.00 19.09
27.592 -17.741
1.00 21.09
NH1 ARG A 350
28.086 -18.970
1.00 26.86
NH1 ARG A 350
NH2 ARG A 350
27.921 -17.030
1.00 23.89
NH2 ARG A 350
29.257 -14.597
1.00 12.06
30.508 -14.372
1.00 12.13
30.674 -12.921
1.00 10.07
29.698 -12.220
1.00 11.80
30.589 -15.229
1.00 17.09
30.831 -16.703
1.00 26.52
32.180 -16.938
1.00 38.10
33.315 -16.430
1.00 43.26
34.642 -16.526
1.00 44.19
31.922 -12.480
1.00 10.94
32.293 -11.238
32.879 -11.624
33.805 -12.438
1.00 10.66
33.328 -10.452
CG1 ILE A 352
32.733 -10.007
1.00 12.09
CG1 ILE A 352
CG2 ILE A 352
1.00 11.15
CG2 ILE A 352
CD1 ILE A 352
1.00 16.98
CD1 ILE A 352
32.324 -11.029
32.678 -11.330 -10.485
33.186 -10.070 -11.178
-8.983 -10.970
1.00 12.79
31.443 -11.862 -11.210
1.00 11.25
31.034 -13.269 -10.777
1.00 15.36
29.540 -13.540 -10.987
1.00 18.88
29.088 -13.185 -12.330
1.00 18.14
27.814 -12.997 -12.674
1.00 19.27
NH1 ARG A 353
26.834 -13.132 -11.778
1.00 19.69
NH1 ARG A 353
NH2 ARG A 353
27.517 -12.655 -13.915
1.00 20.78
NH2 ARG A 353
34.224 -10.224 -11.987
-9.150 -12.824
-9.539 -14.271
34.844 -10.626 -14.707
1.00 11.15
-8.974 -12.581
1.00 10.08
-8.668 -11.153
CD1 PHE A 354
-7.426 -10.614
1.00 11.32
CD1 PHE A 354
CD2 PHE A 354
-9.620 -10.329
1.00 10.71
CD2 PHE A 354
CE1 PHE A 354
1.00 12.38
CE1 PHE A 354
CE2 PHE A 354
1.00 10.93
CE2 PHE A 354
1.00 10.99
-8.666 -15.006
1.00 10.10
-8.932 -16.392
1.00 11.00
-7.818 -17.262
1.00 12.94
-6.654 -17.034
1.00 14.83
-9.086 -16.586
1.00 14.10
31.443 -10.325 -15.877
1.00 18.61
29.982 -10.623 -16.168
1.00 24.62
OE1 GLU A 355
-9.734 -16.674
1.00 29.33
OE1 GLU A 355
OE2 GLU A 355
29.551 -11.763 -15.876
1.00 29.66
OE2 GLU A 355
-8.181 -18.252
1.00 12.64
-7.203 -19.158
1.00 11.19
-7.025 -18.998
1.00 12.23
-6.358 -19.812
1.00 15.24
-7.615 -17.953
1.00 13.98
-7.529 -17.739
1.00 15.98
-8.521 -18.648
1.00 18.33
-9.673 -18.291
1.00 28.21
-7.748 -16.261
1.00 14.02
-9.100 -15.745
1.00 14.23
OD1 ASN A 357
-9.477 -15.878
1.00 14.21
OD1 ASN A 357
ND2 ASN A 357
-9.837 -15.147
1.00 17.06
ND2 ASN A 357
-8.053 -19.822
1.00 23.55
-8.894 -20.819
1.00 30.07
-8.930 -20.668
1.00 34.80
-9.906 -21.060
1.00 41.07
-8.419 -22.236
1.00 36.09
-8.616 -22.581
1.00 46.83
OD1 ASP A 358
-9.655 -22.184
1.00 50.80
OD1 ASP A 358
OD2 ASP A 358
-7.735 -23.251
1.00 50.62
OD2 ASP A 358
-7.857 -20.124
1.00 30.88
-7.726 -20.000
1.00 31.47
-7.806 -18.542
1.00 30.83
-8.474 -18.192
1.00 32.75
-6.388 -20.570
1.00 38.37
OG1 THR A 359
-6.320 -21.970
1.00 45.01
OG1 THR A 359
CG2 THR A 359
-6.245 -20.368
1.00 42.78
CG2 THR A 359
-7.117 -17.698
1.00 24.40
-7.126 -16.264
1.00 21.81
-8.426 -15.645
1.00 22.23
-8.776 -15.743
1.00 24.24
-5.934 -15.602
1.00 21.50
-4.726 -16.038
1.00 27.43
-9.140 -15.008
1.00 20.19
44.279 -10.418 -14.411
1.00 20.81
43.355 -10.270 -13.209
1.00 19.04
-9.287 -12.468
1.00 17.72
45.561 -11.133 -13.984
1.00 23.56
46.498 -11.507 -15.128
1.00 29.30
45.808 -12.423 -16.121
1.00 32.08
46.813 -13.120 -17.017
1.00 42.78
47.650 -12.154 -17.774
1.00 48.34
42.517 -11.272 -13.018
1.00 16.23
41.611 -11.304 -11.889
1.00 13.04
42.268 -10.896 -10.562
1.00 12.60
41.677 -10.140
1.00 13.08
41.017 -12.705 -11.769
1.00 15.57
39.967 -12.794 -10.687
1.00 18.60
OD1 ASP A 362
38.778 -12.535 -10.996
1.00 20.74
OD1 ASP A 362
OD2 ASP A 362
40.330 -13.125
1.00 19.69
OD2 ASP A 362
43.473 -11.394 -10.280
1.00 14.07
44.093 -11.174
1.00 13.38
1.00 11.45
1.00 13.87
45.403 -11.954
1.00 17.92
1.00 13.00
1.00 17.45
1.00 14.36
1.00 15.52
-6.930 -10.930
1.00 21.27
CG1 VAL A 364
-5.421 -10.868
1.00 26.56
CG1 VAL A 364
CG2 VAL A 364
-7.540 -11.216
1.00 24.66
CG2 VAL A 364
1.00 13.52
CA ALEU A 365
0.55 11.41
CA ALEU A 365
CA BLEU A 365
0.45 12.15
CA BLEU A 365
1.00 10.81
CB ALEU A 365
-6.813 -10.449
0.55 11.19
CB ALEU A 365
CB BLEU A 365
-6.981 -10.406
0.45 13.98
CB BLEU A 365
CG ALEU A 365
-6.035 -11.759
0.55 13.07
CG ALEU A 365
CG BLEU A 365
-6.619 -11.875
0.45 18.40
CG BLEU A 365
CD1ALEU A 365
-4.995 -11.598
0.55 16.11
CD1ALEU A 365
CD1BLEU A 365
-7.848 -12.648
0.45 22.68
CD1BLEU A 365
CD2ALEU A 365
-6.959 -12.883
0.55 14.82
CD2ALEU A 365
CD2BLEU A 365
-6.015 -12.482
0.45 14.18
CD2BLEU A 365
1.00 10.07
1.00 10.88
1.00 12.93
40.529 -10.461
1.00 12.97
39.526 -11.179
1.00 15.20
39.323 -12.655
1.00 15.03
38.670 -12.791
1.00 16.60
37.354 -12.779
1.00 16.73
NH1 ARG A 366
36.513 -12.651
1.00 16.25
NH1 ARG A 366
NH2 ARG A 366
36.874 -12.910
1.00 17.72
NH2 ARG A 366
1.00 11.54
1.00 12.93
1.00 14.28
1.00 17.24
1.00 14.98
1.00 16.29
1.00 18.00
1.00 18.16
1.00 17.28
NH1 ARG A 367
1.00 21.88
NH1 ARG A 367
NH2 ARG A 367
1.00 19.12
NH2 ARG A 367
1.00 12.06
1.00 13.16
1.00 12.06
1.00 15.41
1.00 11.52
1.00 15.01
1.00 19.58
OE1 GLU A 368
1.00 19.81
OE1 GLU A 368
OE2 GLU A 368
1.00 22.15
OE2 GLU A 368
1.00 10.53
1.00 11.22
1.00 10.97
1.00 14.92
1.00 10.06
1.00 13.06
1.00 12.72
1.00 10.18
1.00 10.25
1.00 14.02
1.00 13.21
1.00 18.45
1.00 23.00
1.00 30.54
1.00 39.14
NH1 ARG A 370
1.00 40.41
NH1 ARG A 370
NH2 ARG A 370
1.00 37.74
NH2 ARG A 370
1.00 10.17
1.00 11.62
OE1 GLN A 371
1.00 11.70
OE1 GLN A 371
NE2 GLN A 371
NE2 GLN A 371
34.048 -10.433
32.953 -11.356
1.00 10.56
31.770 -11.157
1.00 11.44
34.409 -10.821
1.00 12.54
1.00 16.39
37.051 -10.113
1.00 24.13
1.00 27.91
33.353 -12.381
1.00 10.16
32.403 -13.381
31.953 -14.236
1.00 11.05
32.774 -14.671
1.00 10.68
33.022 -14.249
1.00 11.56
33.263 -13.459
1.00 14.26
34.210 -14.164
1.00 20.34
OE1 GLU A 373
35.170 -14.816
1.00 31.93
OE1 GLU A 373
OE2 GLU A 373
34.000 -14.063
1.00 18.66
OE2 GLU A 373
30.649 -14.455
1.00 10.57
30.076 -15.227
1.00 12.17
29.498 -14.351
1.00 11.39
28.701 -14.819
1.00 12.75
29.882 -13.072
1.00 10.39
29.456 -12.153
1.00 10.84
28.220 -11.388
1.00 11.10
27.906 -11.337
1.00 10.90
30.590 -11.156
1.00 10.71
27.530 -10.775
1.00 10.29
1.00 11.24
1.00 11.07
1.00 11.17
1.00 13.96
25.181 -10.058
1.00 14.58
CD1 TRP A 376
25.511 -10.236
1.00 20.98
CD1 TRP A 376
CD2 TRP A 376
24.019 -10.867
1.00 15.53
CD2 TRP A 376
NE1 TRP A 376
24.637 -11.112
1.00 21.15
NE1 TRP A 376
CE2 TRP A 376
23.711 -11.511
1.00 19.34
CE2 TRP A 376
CE3 TRP A 376
23.216 -11.108
1.00 15.03
CE3 TRP A 376
CZ2 TRP A 376
22.636 -12.392
1.00 21.42
CZ2 TRP A 376
CZ3 TRP A 376
22.152 -11.989
1.00 16.44
CZ3 TRP A 376
CH2 TRP A 376
21.867 -12.611
1.00 19.60
CH2 TRP A 376
1.00 10.99
1.00 11.92
1.00 13.98
1.00 14.78
1.00 10.50
1.00 12.70
CD1 LEU A 377
1.00 14.47
CD1 LEU A 377
CD2 LEU A 377
1.00 15.52
CD2 LEU A 377
1.00 12.79
1.00 12.98
1.00 11.89
1.00 13.48
1.00 12.11
1.00 13.47
1.00 10.31
1.00 13.48
1.00 18.31
1.00 23.52
1.00 12.05
1.00 12.24
1.00 10.93
1.00 13.37
1.00 13.82
1.00 20.12
OD1 ASP A 380
1.00 19.97
OD1 ASP A 380
OD2 ASP A 380
1.00 25.71
OD2 ASP A 380
1.00 10.34
1.00 10.75
1.00 10.12
1.00 11.40
1.00 11.67
1.00 14.19
CD1 LEU A 381
1.00 14.74
CD1 LEU A 381
CD2 LEU A 381
1.00 16.41
CD2 LEU A 381
1.00 11.24
1.00 10.39
CG1 VAL A 382
1.00 13.21
CG1 VAL A 382
CG2 VAL A 382
1.00 14.02
CG2 VAL A 382
1.00 10.72
1.00 11.36
1.00 10.92
1.00 10.10
1.00 14.72
1.00 25.05
OD1 ASP A 383
1.00 27.32
OD1 ASP A 383
OD2 ASP A 383
1.00 28.05
OD2 ASP A 383
1.00 10.78
1.00 11.57
1.00 10.23
1.00 12.29
1.00 14.46
1.00 18.70
OE1 GLN A 384
1.00 22.29
OE1 GLN A 384
NE2 GLN A 384
1.00 24.14
NE2 GLN A 384
1.00 10.08
1.00 10.32
1.00 10.03
1.00 12.89
1.00 16.53
1.00 31.21
1.00 39.87
1.00 46.88
1.00 10.03
1.00 10.90
1.00 19.92
OE1 GLU A 387
1.00 21.36
OE1 GLU A 387
OE2 GLU A 387
1.00 23.56
OE2 GLU A 387
1.00 10.45
1.00 10.61
1.00 12.92
1.00 10.12
1.00 12.35
1.00 17.97
1.00 21.06
NH1 ARG A 388
1.00 28.80
NH1 ARG A 388
NH2 ARG A 388
1.00 23.78
NH2 ARG A 388
1.00 10.79
1.00 10.92
ANISOU 1000
1.225 -10.282
1.00 12.24
ANISOU 1001
1.271 -11.149
1.00 13.88
ANISOU 1002
1.00 12.94
ANISOU 1003
1.00 12.66
ANISOU 1004
CD1 LEU A 389
1.00 17.43
ANISOU 1005
CD1 LEU A 389
CD2 LEU A 389
1.00 15.52
ANISOU 1006
CD2 LEU A 389
2.208 -10.092
ANISOU 1007
CA AASN A 390
3.430 -10.874
0.65 10.82
ANISOU 1008
CA AASN A 390
CA BASN A 390
3.441 -10.875
0.35 10.77
ANISOU 1009
CA BASN A 390
4.183 -10.679
1.00 12.05
ANISOU 1010
4.744 -11.626
1.00 16.06
ANISOU 1011
CB AASN A 390
4.328 -10.519
0.65 12.45
ANISOU 1012
CB AASN A 390
CB BASN A 390
4.379 -10.536
0.35 11.05
ANISOU 1013
CB BASN A 390
CG AASN A 390
5.611 -11.283
0.65 14.88
ANISOU 1014
CG AASN A 390
CG BASN A 390
4.024 -11.272
0.35 12.18
ANISOU 1015
CG BASN A 390
OD1AASN A 390
5.610 -12.502
0.65 16.50
ANISOU 1016
OD1AASN A 390
OD1BASN A 390
3.467 -12.372
0.35 17.85
ANISOU 1017
OD1BASN A 390
ND2AASN A 390
6.726 -10.573
0.65 18.14
ANISOU 1018
ND2AASN A 390
ND2BASN A 390
4.343 -10.673
0.35 14.65
ANISOU 1019
ND2BASN A 390
1.00 10.20
ANISOU 1020
CA AARG A 391
0.64 12.77
ANISOU 1021
CA AARG A 391
CA BARG A 391
0.36 12.37
ANISOU 1022
CA BARG A 391
1.00 13.75
ANISOU 1023
5.115 -10.279
1.00 16.83
ANISOU 1024
CB AARG A 391
0.64 14.34
ANISOU 1025
CB AARG A 391
CB BARG A 391
0.36 10.35
ANISOU 1026
CB BARG A 391
CG AARG A 391
0.64 15.43
ANISOU 1027
CG AARG A 391
CG BARG A 391
0.36 10.68
ANISOU 1028
CG BARG A 391
CD AARG A 391
0.64 18.31
ANISOU 1029
CD AARG A 391
CD BARG A 391
0.36 10.48
ANISOU 1030
CD BARG A 391
NE AARG A 391
0.64 19.47
ANISOU 1031
NE AARG A 391
NE BARG A 391
0.36 11.31
ANISOU 1032
NE BARG A 391
CZ AARG A 391
0.64 20.32
ANISOU 1033
CZ AARG A 391
CZ BARG A 391
0.36 13.18
ANISOU 1034
CZ BARG A 391
NH1AARG A 391
0.64 20.02
ANISOU 1035
NH1AARG A 391
NH1BARG A 391
0.36 10.20
ANISOU 1036
NH1BARG A 391
NH2AARG A 391
0.64 22.74
ANISOU 1037
NH2AARG A 391
NH2BARG A 391
0.36 17.52
ANISOU 1038
NH2BARG A 391
3.064 -10.196
1.00 13.88
ANISOU 1039
2.395 -10.889
1.00 16.27
ANISOU 1040
2.938 -12.277
1.00 16.68
ANISOU 1041
2.891 -12.715
1.00 19.69
ANISOU 1042
0.890 -10.988
1.00 17.77
ANISOU 1043
1.00 23.24
ANISOU 1044
CD1 LEU A 392
1.00 26.04
ANISOU 1045
CD1 LEU A 392
CD2 LEU A 392
1.00 24.25
ANISOU 1046
CD2 LEU A 392
3.407 -12.978
1.00 14.69
ANISOU 1047
3.969 -14.306
1.00 17.29
ANISOU 1048
2.923 -15.398
1.00 16.11
ANISOU 1049
3.254 -16.546
1.00 17.25
ANISOU 1050
1.662 -15.049
1.00 15.47
ANISOU 1051
0.574 -16.031
1.00 15.61
ANISOU 1052
0.515 -16.906
1.00 15.25
ANISOU 1053
-0.026 -18.015
1.00 17.33
ANISOU 1054
-0.781 -15.333
1.00 18.15
ANISOU 1055
-0.911 -14.494
1.00 21.28
ANISOU 1056
CD1 PHE A 394
-0.064 -14.681
1.00 24.45
ANISOU 1057
CD1 PHE A 394
CD2 PHE A 394
-1.896 -13.522
1.00 24.12
ANISOU 1058
CD2 PHE A 394
CE1 PHE A 394
-0.193 -13.907
1.00 25.87
ANISOU 1059
CE1 PHE A 394
CE2 PHE A 394
-2.033 -12.747
1.00 24.72
ANISOU 1060
CE2 PHE A 394
-1.181 -12.938
1.00 27.88
ANISOU 1061
1.037 -16.394
1.00 14.08
ANISOU 1062
0.896 -17.058
1.00 14.52
ANISOU 1063
2.232 -17.479
1.00 14.51
ANISOU 1064
3.225 -16.750
1.00 19.13
ANISOU 1065
0.129 -16.143
1.00 15.12
ANISOU 1066
-1.098 -15.548
1.00 17.26
ANISOU 1067
CD1 PHE A 395
-2.184 -16.349
1.00 20.22
ANISOU 1068
CD1 PHE A 395
CD2 PHE A 395
-1.149 -14.203
1.00 18.11
ANISOU 1069
CD2 PHE A 395
CE1 PHE A 395
-3.303 -15.810
1.00 20.99
ANISOU 1070
CE1 PHE A 395
CE2 PHE A 395
-2.278 -13.656
1.00 22.42
ANISOU 1071
CE2 PHE A 395
-3.352 -14.460
1.00 21.80
ANISOU 1072
2.240 -18.650
1.00 15.13
ANISOU 1073
3.397 -19.104
1.00 17.34
ANISOU 1074
3.578 -18.240
1.00 17.60
ANISOU 1075
4.704 -17.905
1.00 19.01
ANISOU 1076
3.203 -20.550
1.00 24.91
ANISOU 1077
3.134 -21.579
1.00 29.25
ANISOU 1078
3.114 -23.005
1.00 30.29
ANISOU 1079
OE1 GLU A 396
2.927 -23.174
1.00 34.63
ANISOU 1080
OE1 GLU A 396
OE2 GLU A 396
3.289 -23.948
1.00 34.76
ANISOU 1081
OE2 GLU A 396
2.462 -17.917
1.00 19.27
ANISOU 1082
2.464 -17.125
1.00 18.96
ANISOU 1083
1.305 -16.131
1.00 15.81
ANISOU 1084
0.250 -16.426
1.00 15.35
ANISOU 1085
2.317 -18.012
1.00 21.27
ANISOU 1086
OG1 THR A 397
1.055 -18.694
1.00 28.14
ANISOU 1087
OG1 THR A 397
CG2 THR A 397
3.424 -19.032
1.00 23.65
ANISOU 1088
CG2 THR A 397
1.541 -14.956
1.00 15.15
ANISOU 1089
0.523 -13.953
1.00 14.93
ANISOU 1090
0.748 -13.425
1.00 18.22
ANISOU 1091
1.824 -12.922
1.00 21.11
ANISOU 1092
0.636 -12.770
1.00 15.51
ANISOU 1093
CG1 VAL A 398
-0.466 -11.764
1.00 15.06
ANISOU 1094
CG1 VAL A 398
CG2 VAL A 398
0.556 -13.260
1.00 15.96
ANISOU 1095
CG2 VAL A 398
-0.260 -13.577
1.00 18.67
ANISOU 1096
-0.201 -13.086
1.00 21.54
ANISOU 1097
-1.386 -12.170
1.00 17.86
ANISOU 1098
-2.414 -12.304
1.00 19.08
ANISOU 1099
-0.233 -14.259
1.00 29.61
ANISOU 1100
1.001 -15.143
1.00 47.37
ANISOU 1101
OD1 ASP A 399
2.132 -14.605
1.00 52.19
ANISOU 1102
OD1 ASP A 399
OD2 ASP A 399
0.840 -16.378
1.00 51.64
ANISOU 1103
OD2 ASP A 399
-1.241 -11.213
1.00 15.17
ANISOU 1104
-2.387 -10.389
1.00 15.94
ANISOU 1105
-2.748 -10.569
1.00 15.70
ANISOU 1106
-1.885 -10.759
1.00 19.31
ANISOU 1107
1.00 18.84
ANISOU 1108
OG1 THR A 400
1.00 20.65
ANISOU 1109
OG1 THR A 400
CG2 THR A 400
1.00 26.30
ANISOU 1110
CG2 THR A 400
-4.046 -10.494
1.00 16.24
ANISOU 1111
-4.592 -10.563
1.00 20.23
ANISOU 1112
1.00 16.92
ANISOU 1113
1.00 18.95
ANISOU 1114
-5.267 -11.916
1.00 23.63
ANISOU 1115
-5.674 -12.137
1.00 35.47
ANISOU 1116
OD1 ASP A 401
-5.168 -11.413
1.00 41.55
ANISOU 1117
OD1 ASP A 401
OD2 ASP A 401
-6.500 -13.044
1.00 37.13
ANISOU 1118
OD2 ASP A 401
1.00 16.09
ANISOU 1119
1.00 17.98
ANISOU 1120
1.00 22.63
ANISOU 1121
1.00 29.21
ANISOU 1122
1.00 22.49
ANISOU 1123
OG1 THR A 402
1.00 22.31
ANISOU 1124
OG1 THR A 402
CG2 THR A 402
1.00 22.34
ANISOU 1125
CG2 THR A 402
1.00 21.23
ANISOU 1126
1.00 24.64
ANISOU 1127
21.835 -10.329
1.00 22.95
ANISOU 1128
22.616 -11.001
1.00 19.58
ANISOU 1129
-9.898 -10.195
1.00 26.56
ANISOU 1130
-9.041 -11.192
1.00 34.10
ANISOU 1131
-9.880 -12.329
1.00 39.60
ANISOU 1132
OE1 GLN A 403
24.339 -11.110 -12.239
1.00 42.37
ANISOU 1133
OE1 GLN A 403
NE2 GLN A 403
-9.220 -13.403
1.00 39.95
ANISOU 1134
NE2 GLN A 403
20.533 -10.583
1.00 24.04
ANISOU 1135
CA AARG A 404
19.967 -11.736
0.51 24.53
ANISOU 1136
CA AARG A 404
CA BARG A 404
20.013 -11.736
0.49 24.13
ANISOU 1137
CA BARG A 404
20.507 -13.022
1.00 25.43
ANISOU 1138
20.814 -13.054
1.00 26.59
ANISOU 1139
CB AARG A 404
18.440 -11.720
0.51 26.31
ANISOU 1140
CB AARG A 404
CB BARG A 404
18.486 -11.710
0.49 25.54
ANISOU 1141
CB BARG A 404
CG AARG A 404
17.782 -10.446
0.51 27.71
ANISOU 1142
CG AARG A 404
CG BARG A 404
17.940 -10.608
0.49 25.73
ANISOU 1143
CG BARG A 404
CD AARG A 404
16.289 -10.436
0.51 26.53
ANISOU 1144
CD AARG A 404
CD BARG A 404
16.522 -10.912
0.49 28.51
ANISOU 1145
CD BARG A 404
NE AARG A 404
0.51 29.16
ANISOU 1146
NE AARG A 404
NE BARG A 404
16.471 -12.048
0.49 26.54
ANISOU 1147
NE BARG A 404
CZ AARG A 404
0.51 30.59
ANISOU 1148
CZ AARG A 404
CZ BARG A 404
15.375 -12.436
0.49 34.47
ANISOU 1149
CZ BARG A 404
NH1AARG A 404
15.066 -10.350
0.51 28.51
ANISOU 1150
NH1AARG A 404
NH1BARG A 404
14.238 -11.779
0.49 39.06
ANISOU 1151
NH1BARG A 404
NH2AARG A 404
0.51 32.79
ANISOU 1152
NH2AARG A 404
NH2BARG A 404
15.415 -13.477
0.49 36.95
ANISOU 1153
NH2BARG A 404
20.611 -14.077
1.00 23.00
ANISOU 1154
21.105 -15.365
1.00 24.08
ANISOU 1155
19.949 -16.337
1.00 25.12
ANISOU 1156
19.213 -16.675
1.00 27.10
ANISOU 1157
22.099 -16.003
1.00 21.51
ANISOU 1158
CG1 VAL A 405
22.485 -17.401
1.00 24.82
ANISOU 1159
CG1 VAL A 405
CG2 VAL A 405
23.339 -15.140
1.00 22.73
ANISOU 1160
CG2 VAL A 405
19.776 -16.785
1.00 28.51
ANISOU 1161
18.705 -17.752
1.00 32.89
ANISOU 1162
18.777 -18.983
1.00 33.84
ANISOU 1163
19.833 -19.611
1.00 35.63
ANISOU 1164
18.980 -18.156 -10.963
1.00 33.82
ANISOU 1165
19.691 -16.981 -11.549
1.00 36.17
ANISOU 1166
20.523 -16.405 -10.438
1.00 30.66
ANISOU 1167
17.674 -19.315
1.00 33.18
ANISOU 1168
17.619 -20.483
1.00 29.38
ANISOU 1169
18.029 -20.257
1.00 29.92
ANISOU 1170
17.801 -21.118
1.00 31.99
ANISOU 1171
18.624 -19.103
1.00 28.59
ANISOU 1172
19.110 -18.790
1.00 30.78
ANISOU 1173
18.616 -17.433
1.00 32.73
ANISOU 1174
19.295 -16.423
1.00 30.01
ANISOU 1175
20.643 -18.808
1.00 31.28
ANISOU 1176
21.154 -20.109
1.00 34.35
ANISOU 1177
17.452 -17.421
1.00 32.65
ANISOU 1178
16.677 -16.249
1.00 33.67
ANISOU 1179
17.421 -15.206
1.00 28.58
ANISOU 1180
17.018 -14.041
1.00 29.61
ANISOU 1181
15.595 -16.864
1.00 38.68
ANISOU 1182
15.475 -18.254
1.00 43.16
ANISOU 1183
16.839 -18.681
1.00 36.99
ANISOU 1184
18.453 -15.598
1.00 21.16
ANISOU 1185
CA AASP A 410
19.119 -14.615
0.54 20.91
ANISOU 1186
CA AASP A 410
CA BASP A 410
19.152 -14.686
0.46 21.12
ANISOU 1187
CA BASP A 410
20.532 -14.281
1.00 16.31
ANISOU 1188
21.274 -13.599
1.00 15.31
ANISOU 1189
CB AASP A 410
19.087 -15.028
0.54 26.18
ANISOU 1190
CB AASP A 410
CB BASP A 410
19.310 -15.328
0.46 25.95
ANISOU 1191
CB BASP A 410
CG AASP A 410
19.589 -16.434
0.54 31.39
ANISOU 1192
CG AASP A 410
CG BASP A 410
17.989 -15.726
0.46 34.76
ANISOU 1193
CG BASP A 410
OD1AASP A 410
20.193 -17.004
0.54 30.70
ANISOU 1194
OD1AASP A 410
OD1BASP A 410
16.982 -15.032
0.46 37.38
ANISOU 1195
OD1BASP A 410
OD2AASP A 410
19.388 -16.966
0.54 36.70
ANISOU 1196
OD2AASP A 410
OD2BASP A 410
17.962 -16.733
0.46 37.10
ANISOU 1197
OD2BASP A 410
20.885 -14.722
1.00 15.72
ANISOU 1198
22.205 -14.432
1.00 15.06
ANISOU 1199
22.162 -13.384
1.00 14.25
ANISOU 1200
21.201 -13.313
1.00 17.91
ANISOU 1201
22.855 -15.703
1.00 16.21
ANISOU 1202
23.190 -16.765
1.00 17.49
ANISOU 1203
23.780 -18.003
1.00 21.27
ANISOU 1204
OE1 GLN A 411
23.907 -18.084
1.00 20.10
ANISOU 1205
OE1 GLN A 411
NE2 GLN A 411
24.127 -18.986
1.00 23.08
ANISOU 1206
NE2 GLN A 411
23.225 -12.587
1.00 12.48
ANISOU 1207
23.495 -11.769
1.00 11.78
ANISOU 1208
24.894 -12.069
1.00 12.22
ANISOU 1209
25.763 -12.469
1.00 11.08
ANISOU 1210
23.397 -10.241
1.00 14.18
ANISOU 1211
CG1 VAL A 412
1.00 15.85
ANISOU 1212
CG1 VAL A 412
CG2 VAL A 412
1.00 13.29
ANISOU 1213
CG2 VAL A 412
25.109 -11.874
1.00 13.09
ANISOU 1214
26.463 -11.743
1.00 11.47
ANISOU 1215
26.729 -10.260
1.00 10.55
ANISOU 1216
1.00 14.56
ANISOU 1217
26.608 -12.371
1.00 11.71
ANISOU 1218
26.728 -13.875
1.00 14.47
ANISOU 1219
OD1 ASP A 413
26.906 -14.439
1.00 15.81
ANISOU 1220
OD1 ASP A 413
OD2 ASP A 413
26.677 -14.489
1.00 18.16
ANISOU 1221
OD2 ASP A 413
1.00 10.01
ANISOU 1222
1.00 10.38
ANISOU 1223
1.00 10.75
ANISOU 1224
1.00 11.93
ANISOU 1225
1.00 11.97
ANISOU 1226
CG1 VAL A 414
1.00 13.24
ANISOU 1227
CG1 VAL A 414
CG2 VAL A 414
1.00 13.53
ANISOU 1228
CG2 VAL A 414
ANISOU 1229
-7.924 -10.640
ANISOU 1230
-6.560 -10.954
1.00 10.14
ANISOU 1231
-5.563 -11.037
1.00 13.44
ANISOU 1232
-8.350 -11.772
1.00 12.10
ANISOU 1233
CG1 VAL A 415
-8.538 -13.074
1.00 14.81
ANISOU 1234
CG1 VAL A 415
CG2 VAL A 415
-9.648 -11.404
1.00 13.29
ANISOU 1235
CG2 VAL A 415
-6.518 -11.072
ANISOU 1236
-5.328 -11.548
ANISOU 1237
-5.462 -13.053
ANISOU 1238
-6.358 -13.528
1.00 12.23
ANISOU 1239
-5.204 -10.867
1.00 10.65
ANISOU 1240
ANISOU 1241
CD1 TYR A 416
1.00 11.66
ANISOU 1242
CD1 TYR A 416
CD2 TYR A 416
ANISOU 1243
CD2 TYR A 416
CE1 TYR A 416
1.00 13.30
ANISOU 1244
CE1 TYR A 416
CE2 TYR A 416
1.00 10.67
ANISOU 1245
CE2 TYR A 416
1.00 10.66
ANISOU 1246
1.00 10.51
ANISOU 1247
-4.594 -13.801
1.00 12.10
ANISOU 1248
-4.587 -15.243
1.00 13.74
ANISOU 1249
-3.509 -15.606
1.00 13.02
ANISOU 1250
-2.326 -15.294
1.00 15.52
ANISOU 1251
-4.314 -15.877
1.00 20.57
ANISOU 1252
-5.403 -15.570
1.00 26.91
ANISOU 1253
-4.932 -15.845
1.00 34.47
ANISOU 1254
-5.955 -15.376
1.00 42.61
ANISOU 1255
-7.207 -16.186
1.00 45.62
ANISOU 1256
-3.929 -16.228
1.00 14.06
ANISOU 1257
-3.014 -16.594
1.00 13.43
ANISOU 1258
-3.018 -18.102
1.00 14.14
ANISOU 1259
-4.017 -18.785
1.00 16.13
ANISOU 1260
-3.338 -15.859
1.00 14.15
ANISOU 1261
CG1 VAL A 418
-3.403 -14.363
1.00 18.21
ANISOU 1262
CG1 VAL A 418
CG2 VAL A 418
-4.630 -16.362
1.00 14.13
ANISOU 1263
CG2 VAL A 418
-1.901 -18.611
1.00 16.48
ANISOU 1264
-1.781 -20.015
1.00 16.09
ANISOU 1265
-1.336 -20.050
1.00 15.96
ANISOU 1266
-0.311 -19.455
1.00 17.82
ANISOU 1267
-0.741 -20.696
1.00 20.23
ANISOU 1268
-0.234 -22.046
1.00 27.59
ANISOU 1269
-1.155 -23.187
1.00 31.28
ANISOU 1270
-0.508 -24.535
1.00 31.41
ANISOU 1271
-1.373 -25.685
1.00 38.78
ANISOU 1272
-2.113 -20.723
1.00 20.40
ANISOU 1273
-1.765 -20.864
1.00 26.86
ANISOU 1274
-0.937 -22.120
1.00 36.54
ANISOU 1275
-0.556 -22.836
1.00 40.19
ANISOU 1276
-3.026 -20.877
1.00 30.40
ANISOU 1277
-3.814 -19.581
1.00 27.09
ANISOU 1278
-5.021 -19.606
1.00 32.09
ANISOU 1279
OE1 GLU A 420
-5.455 -20.711
1.00 38.63
ANISOU 1280
OE1 GLU A 420
OE2 GLU A 420
-5.535 -18.520
1.00 25.99
ANISOU 1281
OE2 GLU A 420
HETATM 1283
1.00 10.34
ANISOU 1283
HETATM 1284
1.00 14.57
ANISOU 1284
HETATM 1285
36.685 -11.597 -15.738
1.00 10.83
ANISOU 1285
HETATM 1286
1.00 15.73
ANISOU 1286
HETATM 1287
36.056 -12.633
1.00 17.45
ANISOU 1287
HETATM 1288
1.00 14.32
ANISOU 1288
HETATM 1289
35.403 -12.882 -12.043
1.00 17.04
ANISOU 1289
HETATM 1290
28.788 -11.107
1.00 14.05
ANISOU 1290
HETATM 1291
1.00 19.19
ANISOU 1291
HETATM 1292
1.00 16.38
ANISOU 1292
HETATM 1293
1.00 22.37
ANISOU 1293
HETATM 1294
2.259 -13.780
1.00 19.31
ANISOU 1294
HETATM 1295
35.520 -14.909
1.00 17.93
ANISOU 1295
HETATM 1296
7.204 -18.301
1.00 21.55
ANISOU 1296
HETATM 1297
36.729 -10.156
1.00 19.65
ANISOU 1297
HETATM 1298
30.997 -13.591 -14.552
1.00 20.81
ANISOU 1298
HETATM 1299
36.754 -12.096
1.00 28.57
ANISOU 1299
HETATM 1300
1.00 22.90
ANISOU 1300
HETATM 1301
1.00 22.65
ANISOU 1301
HETATM 1302
1.00 28.57
ANISOU 1302
HETATM 1303
18.706 -13.922
1.00 28.68
ANISOU 1303
HETATM 1304
1.00 24.43
ANISOU 1304
HETATM 1305
-4.633 -21.868
1.00 26.28
ANISOU 1305
HETATM 1306
1.00 28.13
ANISOU 1306
HETATM 1307
1.00 28.13
ANISOU 1307
HETATM 1308
5.926 -16.089
1.00 26.76
ANISOU 1308
HETATM 1309
41.691 -13.167 -15.192
1.00 41.47
ANISOU 1309
HETATM 1310
1.00 22.24
ANISOU 1310
HETATM 1311
35.850 -10.961 -18.182
1.00 24.74
ANISOU 1311
HETATM 1312
-8.560 -24.439
1.00 32.37
ANISOU 1312
HETATM 1313
26.992 -21.184
1.00 32.08
ANISOU 1313
HETATM 1314
1.00 41.61
ANISOU 1314
HETATM 1315
1.00 35.65
ANISOU 1315
HETATM 1316
44.261 -11.083
1.00 21.32
ANISOU 1316
HETATM 1317
1.00 26.89
ANISOU 1317
HETATM 1318
1.00 41.10
ANISOU 1318
HETATM 1319
1.425 -11.113
1.00 36.05
ANISOU 1319
HETATM 1320
1.00 30.37
ANISOU 1320
HETATM 1321
1.00 30.59
ANISOU 1321
HETATM 1322
1.00 31.39
ANISOU 1322
HETATM 1323
1.00 69.72
ANISOU 1323
HETATM 1324
1.00 32.84
ANISOU 1324
HETATM 1325
1.00 29.18
ANISOU 1325
HETATM 1326
20.246 -10.765
1.00 40.23
ANISOU 1326
HETATM 1327
1.947 -11.149
1.00 30.62
ANISOU 1327
HETATM 1328
1.00 24.90
ANISOU 1328
HETATM 1329
19.768 -18.835
1.00 31.33
ANISOU 1329
HETATM 1330
24.160 -20.575
1.00 35.69
ANISOU 1330
HETATM 1331
42.816 -14.332
1.00 23.55
ANISOU 1331
HETATM 1332
1.00 41.00
ANISOU 1332
HETATM 1333
3.651 -15.000
1.00 41.62
ANISOU 1333
HETATM 1334
7.138 -14.695
1.00 39.12
ANISOU 1334
HETATM 1335
1.00 29.99
ANISOU 1335
HETATM 1336
28.285 -13.284 -17.552
1.00 42.03
ANISOU 1336
HETATM 1337
3.324 -26.984
1.00 61.56
ANISOU 1337
HETATM 1338
1.00 36.15
ANISOU 1338
HETATM 1339
28.521 -17.028
1.00 38.71
ANISOU 1339
HETATM 1340
18.643 -13.195
1.00 32.81
ANISOU 1340
HETATM 1341
1.00 38.48
ANISOU 1341
HETATM 1342
6.464 -13.693
1.00 28.72
ANISOU 1342
HETATM 1343
26.444 -10.161 -16.245
1.00 43.99
ANISOU 1343
HETATM 1344
1.00 50.95
ANISOU 1344
HETATM 1345
21.289 -21.143
1.00 39.62
ANISOU 1345
HETATM 1346
1.00 31.44
ANISOU 1346
HETATM 1347
1.00 37.76
ANISOU 1347
HETATM 1348
1.00 39.04
ANISOU 1348
HETATM 1349
4.570 -14.038
1.00 42.01
ANISOU 1349
HETATM 1350
16.175 -10.986
1.00 38.44
ANISOU 1350
HETATM 1351
24.611 -15.800 -10.207
1.00 33.17
ANISOU 1351
HETATM 1352
1.00 44.60
ANISOU 1352
HETATM 1353
1.00 49.05
ANISOU 1353
HETATM 1354
4.639 -22.428
1.00 44.17
ANISOU 1354
HETATM 1355
5.419 -10.180
1.00 55.67
ANISOU 1355
HETATM 1356
1.00 45.47
ANISOU 1356
HETATM 1357
-0.809 -17.596
1.00 45.27
ANISOU 1357
HETATM 1358
1.00 53.94
ANISOU 1358
HETATM 1359
28.211 -10.614
1.00 38.28
ANISOU 1359
HETATM 1360
1.00 42.45
ANISOU 1360
HETATM 1361
42.686 -10.998
1.00 32.90
ANISOU 1361
HETATM 1362
1.00 35.24
ANISOU 1362
HETATM 1363
1.00 35.90
ANISOU 1363
HETATM 1364
1.00 29.75
ANISOU 1364
HETATM 1365
-3.427 -18.199
1.00 46.37
ANISOU 1365
HETATM 1366
1.00 35.34
ANISOU 1366
HETATM 1367
1.00 37.40
ANISOU 1367
HETATM 1368
1.00 41.73
ANISOU 1368
HETATM 1369
1.00 36.06
ANISOU 1369
HETATM 1370
1.00 33.97
ANISOU 1370
HETATM 1371
1.00 34.02
ANISOU 1371
HETATM 1372
-4.712 -21.994
1.00 40.95
ANISOU 1372
HETATM 1373
1.00 39.65
ANISOU 1373
HETATM 1374
1.00 35.73
ANISOU 1374
HETATM 1375
1.00 41.40
ANISOU 1375
HETATM 1376
1.00 42.33
ANISOU 1376
HETATM 1377
18.513 -12.335
1.00 49.69
ANISOU 1377
HETATM 1378
1.00 47.09
ANISOU 1378
HETATM 1379
1.00 58.48
ANISOU 1379
HETATM 1380
1.00 57.51
ANISOU 1380
HETATM 1381
1.00 54.79
ANISOU 1381
HETATM 1382
-9.152 -10.130
1.00 44.33
ANISOU 1382
HETATM 1383
1.00 42.31
ANISOU 1383
HETATM 1384
-8.008 -18.801
1.00 49.03
ANISOU 1384
HETATM 1385
5.533 -18.086
1.00 41.96
ANISOU 1385
HETATM 1386
2.709 -17.487
1.00 52.00
ANISOU 1386
HETATM 1387
42.341 -11.390 -17.890
1.00 38.69
ANISOU 1387
HETATM 1388
1.00 52.26
ANISOU 1388
HETATM 1389
1.00 38.93
ANISOU 1389
HETATM 1390
25.179 -20.905
1.00 35.04
ANISOU 1390
HETATM 1391
22.740 -13.665 -11.061
1.00 45.56
ANISOU 1391
HETATM 1392
1.00 44.46
ANISOU 1392
HETATM 1393
1.00 41.67
ANISOU 1393
HETATM 1394
1.00 52.45
ANISOU 1394
HETATM 1395
1.00 43.79
ANISOU 1395
HETATM 1396
1.00 41.27
ANISOU 1396
HETATM 1397
1.00 54.76
ANISOU 1397
HETATM 1398
36.848 -10.105 -20.521
1.00 46.24
ANISOU 1398
HETATM 1399
1.00 45.39
ANISOU 1399
HETATM 1400
-5.117 -23.200
1.00 43.46
ANISOU 1400
HETATM 1401
21.849 -16.093
1.00 33.58
ANISOU 1401
HETATM 1402
1.00 49.95
ANISOU 1402
HETATM 1403
1.00 35.86
ANISOU 1403
HETATM 1404
1.00 48.72
ANISOU 1404
HETATM 1405
1.00 58.25
ANISOU 1405
HETATM 1406
1.00 48.60
ANISOU 1406
HETATM 1407
1.00 50.84
ANISOU 1407
HETATM 1408
15.985 -14.285
1.00 57.33
ANISOU 1408
HETATM 1409
-2.952 -24.659
1.00 52.24
ANISOU 1409
HETATM 1410
1.00 36.45
ANISOU 1410
HETATM 1411
3.835 -14.474
1.00 40.84
ANISOU 1411
HETATM 1412
1.00 58.73
ANISOU 1412
HETATM 1413
1.00 45.94
ANISOU 1413
HETATM 1414
1.00 36.35
ANISOU 1414
HETATM 1415
1.00 51.77
ANISOU 1415
HETATM 1416
1.00 49.26
ANISOU 1416
HETATM 1417
1.00 36.43
ANISOU 1417
HETATM 1418
39.966 -12.444
1.00 36.00
ANISOU 1418
HETATM 1419
1.00 46.30
ANISOU 1419
HETATM 1420
1.00 43.90
ANISOU 1420
HETATM 1421
20.127 -15.555
1.00 44.65
ANISOU 1421
HETATM 1422
1.00 47.72
ANISOU 1422
HETATM 1423
38.846 -11.303
1.00 60.70
ANISOU 1423}
THE HIGH-RESOLUTION AND NEW FORM CRYSTAL STRUCTURE OF BAMA POTRA4-5
2 FROM E.COLI
MOL_ID: 1;
2 MOLECULE: OUTER MEMBRANE PROTEIN ASSEMBLY COMPLEX, YAET PROTEIN;
3 CHAIN: A;
4 FRAGMENT: POTRA45 DOMAIN (UNP RESIDUES 266-420);
5 ENGINEERED: YES
MOL_ID: 1;
2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
3 ORGANISM_TAXID: 83333;
4 STRAIN: K-12;
5 GENE: ECDH1_3426, YAET;
6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
7 EXPRESSION_SYSTEM_TAXID: 562;
8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
10 EXPRESSION_SYSTEM_PLASMID: PET-28A
POTRA FOLD, INSERTION OF OUTER MEMBRANE PROTEINS, PROTEIN BINDING
X-RAY DIFFRACTION
Z.Q.GAO,H.ZHANG,Y.H.DONG
10-AUG-11 3Q6B
H.ZHANG,Z.Q.GAO,H.F.HOU,J.H.XU,L.F.LI,X.D.SU,Y.H.DONG
HIGH-RESOLUTION STRUCTURE OF A NEW CRYSTAL FORM OF BAMA
TITL 2 POTRA4-5 FROM ESCHERICHIA COLI.
ACTA CRYSTALLOGR.,SECT.F
2 RESOLUTION.
1.50 ANGSTROMS.
3 REFINEMENT.
: PHENIX (PHENIX.REFINE: 1.6.4_486)
: PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
: DAVIS,KRESHNA GOPAL,RALF GROSSE-
: KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
: TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
: MORIARTY,REETAL PAI,RANDY READ,JANE
: RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
: SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
: LAURENT STORONI,TOM TERWILLIGER,PETER
REFINEMENT TARGET : ML
DATA USED IN REFINEMENT.
RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
RESOLUTION RANGE LOW
(ANGSTROMS) : 25.79
MIN(FOBS/SIGMA_FOBS)
COMPLETENESS FOR RANGE
(%) : 92.9
NUMBER OF REFLECTIONS
FIT TO DATA USED IN REFINEMENT.
(WORKING + TEST SET) : 0.149
(WORKING SET) : 0.147
FREE R VALUE
FREE R VALUE TEST SET SIZE
(%) : 5.060
FREE R VALUE TEST SET COUNT
FIT TO DATA USED IN REFINEMENT (IN BINS).
RESOLUTION RANGE
NWORK NFREE
1 25.7975 -
BULK SOLVENT MODELLING.
METHOD USED
: FLAT BULK SOLVENT MODEL
SOLVENT RADIUS
SHRINKAGE RADIUS
ERROR ESTIMATES.
COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)
PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
FROM WILSON PLOT
(A**2) : NULL
MEAN B VALUE
(OVERALL, A**2) : NULL
OVERALL ANISOTROPIC B VALUE.
B11 (A**2) : 0.28620
B22 (A**2) : -1.58070
B33 (A**2) : 1.29450
B12 (A**2) : -0.00000
B13 (A**2) : -0.22290
B23 (A**2) : -0.00000
TWINNING INFORMATION.
FRACTION: NULL
OPERATOR: NULL
DEVIATIONS FROM IDEAL VALUES.
CHIRALITY :
PLANARITY :
TLS DETAILS
NUMBER OF TLS GROUPS
NCS DETAILS
NUMBER OF NCS GROUPS : NULL
OTHER REFINEMENT REMARKS: NULL
4 3Q6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-JAN-11.
REMARK 100 THE RCSB ID CODE IS RCSB063248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200
EXPERIMENT TYPE
: X-RAY DIFFRACTION
REMARK 200
DATE OF DATA COLLECTION
: 04-DEC-10
REMARK 200
TEMPERATURE
(KELVIN) : 100
REMARK 200
REMARK 200
NUMBER OF CRYSTALS USED
REMARK 200
REMARK 200
SYNCHROTRON
REMARK 200
RADIATION SOURCE
REMARK 200
REMARK 200
X-RAY GENERATOR MODEL
REMARK 200
MONOCHROMATIC OR LAUE
REMARK 200
WAVELENGTH OR RANGE
(A) : NULL
REMARK 200
MONOCHROMATOR
: DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200
REMARK 200
REMARK 200
DETECTOR TYPE
REMARK 200
DETECTOR MANUFACTURER
: MARMOSAIC 225 MM CCD
REMARK 200
INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200
DATA SCALING SOFTWARE
: HKL-2000
REMARK 200
REMARK 200
NUMBER OF UNIQUE REFLECTIONS
REMARK 200
RESOLUTION RANGE HIGH
(A) : 1.500
REMARK 200
RESOLUTION RANGE LOW
(A) : 50.000
REMARK 200
REJECTION CRITERIA
(SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200
COMPLETENESS FOR RANGE
(%) : 95.3
REMARK 200
DATA REDUNDANCY
REMARK 200
(I) : 0.07400
REMARK 200
(I) : 0.07400
REMARK 200
FOR THE DATA SET
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200
HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200
HIGHEST RESOLUTION SHELL, RANGE LOW
(A) : 1.55
REMARK 200
COMPLETENESS FOR SHELL
(%) : 83.1
REMARK 200
DATA REDUNDANCY IN SHELL
REMARK 200
R MERGE FOR SHELL
(I) : 0.33600
REMARK 200
R SYM FOR SHELL
(I) : NULL
REMARK 200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3OG5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS
(%): 38.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1M SODIUM
REMARK 280
CACODYLATE PH 6.5, 30% PEG 8000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280
TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290
REMARK 290
REMARK 290
REMARK 290
REMARK 290
X+1/2,Y+1/2,Z
REMARK 290
-X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290
WHERE NNN -> OPERATOR NUMBER
REMARK 290
MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290
1...000000
REMARK 290
0...000000
REMARK 290
0...000000
REMARK 290
2 -1...000000
REMARK 290
0...000000
REMARK 290
0...000000
REMARK 290
1...000000
REMARK 290
0...000000
REMARK 290
0...000000
REMARK 290
4 -1...000000
REMARK 290
0...000000
REMARK 290
0...000000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.
BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350
1...000000
REMARK 350
0...000000
REMARK 350
0...000000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465
M RES C SSSEQI
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 465
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OG5
RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BAMA POTRA45 TANDEM
C9QRL1_ECOD1
SEQADV 3Q6B MET A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B GLU A
EXPRESSION TAG
SEQADV 3Q6B ASN A
EXPRESSION TAG
SEQADV 3Q6B LEU A
EXPRESSION TAG
SEQADV 3Q6B TYR A
EXPRESSION TAG
SEQADV 3Q6B PHE A
EXPRESSION TAG
SEQADV 3Q6B GLU A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B HIS A
EXPRESSION TAG
SEQADV 3Q6B MET A
EXPRESSION TAG
SEQADV 3Q6B ALA A
EXPRESSION TAG
SEQADV 3Q6B SER A
EXPRESSION TAG
SEQADV 3Q6B MET A
EXPRESSION TAG
SEQADV 3Q6B THR A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B GLN A
EXPRESSION TAG
SEQADV 3Q6B GLN A
EXPRESSION TAG
SEQADV 3Q6B MET A
EXPRESSION TAG
SEQADV 3Q6B GLY A
EXPRESSION TAG
SEQADV 3Q6B ARG A
EXPRESSION TAG
MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
GLU ASN LEU TYR PHE GLU GLY SER HIS MET ALA SER MET
THR GLY GLY GLN GLN MET GLY ARG TYR LYS LEU SER GLY
VAL GLU VAL SER GLY ASN LEU ALA GLY HIS SER ALA GLU
ILE GLU GLN LEU THR LYS ILE GLU PRO GLY GLU LEU TYR
ASN GLY THR LYS VAL THR LYS MET GLU ASP ASP ILE LYS
LYS LEU LEU GLY ARG TYR GLY TYR ALA TYR PRO ARG VAL
GLN SER MET PRO GLU ILE ASN ASP ALA ASP LYS THR VAL
LYS LEU ARG VAL ASN VAL ASP ALA GLY ASN ARG PHE TYR
VAL ARG LYS ILE ARG PHE GLU GLY ASN ASP THR SER LYS
ASP ALA VAL LEU ARG ARG GLU MET ARG GLN MET GLU GLY
ALA TRP LEU GLY SER ASP LEU VAL ASP GLN GLY LYS GLU
ARG LEU ASN ARG LEU GLY PHE PHE GLU THR VAL ASP THR
ASP THR GLN ARG VAL PRO GLY SER PRO ASP GLN VAL ASP
VAL VAL TYR LYS VAL LYS GLU
*141(H2 O)
A 3 LYS A 267
A 3 THR A 334
A 3 ARG A 321
ASN A 329 -1
B 3 TYR A 348
B 3 SER A 408
B 3 THR A 397
VAL A 405 -1
90.00 101.00
90.00 C 1 2 1
1...000000
0...000000
0...000000
0...001413
0...000000
0...031286
1.00 49.14
1.00 45.61
1.00 42.37
1.00 44.15
1.00 47.33
1.00 52.65
CD1 TYR A 266
1.00 53.12
CD1 TYR A 266
CD2 TYR A 266
1.00 54.47
CD2 TYR A 266
CE1 TYR A 266
1.00 55.76
CE1 TYR A 266
CE2 TYR A 266
1.00 56.05
CE2 TYR A 266
1.00 57.32
1.00 63.36
1.00 37.64
1.00 39.31
1.00 39.64
1.00 42.01
1.00 42.05
1.00 47.70
1.00 51.52
1.00 55.23
1.00 56.97
1.00 37.80
1.00 39.58
1.00 43.23
1.00 47.99
1.00 40.16
1.00 40.68
CD1 LEU A 268
1.00 42.94
CD1 LEU A 268
CD2 LEU A 268
1.00 40.27
CD2 LEU A 268
1.00 40.35
1.00 41.44
1.00 44.38
1.00 48.47
1.00 43.20
1.00 43.93
1.00 42.55
1.00 40.28
1.00 37.63
1.00 34.98
1.00 35.59
1.00 34.66
1.00 37.00
1.00 38.63
1.00 34.96
CG1 VAL A 271
1.00 37.00
CG1 VAL A 271
CG2 VAL A 271
1.00 36.61
CG2 VAL A 271
1.00 33.24
1.00 34.46
1.00 34.34
1.00 33.96
1.00 41.61
1.00 51.22
1.00 59.02
OE1 GLU A 272
1.00 60.50
OE1 GLU A 272
OE2 GLU A 272
1.00 63.72
OE2 GLU A 272
1.00 35.27
1.00 33.04
1.00 33.81
1.00 37.68
1.00 35.17
CG1 VAL A 273
1.00 36.37
CG1 VAL A 273
CG2 VAL A 273
1.00 35.13
CG2 VAL A 273
1.00 32.79
1.00 31.78
1.00 27.96
1.00 28.97
1.00 40.09
1.00 44.16
1.00 28.00
1.00 27.41
1.00 30.40
1.00 34.84
1.00 28.55
1.00 27.28
1.00 26.32
1.00 25.73
1.00 31.77
1.00 41.17
OD1 ASN A 276
1.00 44.11
OD1 ASN A 276
ND2 ASN A 276
1.00 42.29
ND2 ASN A 276
1.00 24.63
1.00 23.81
1.00 24.19
1.00 23.73
1.00 26.57
1.00 33.54
CD1 LEU A 277
1.00 38.44
CD1 LEU A 277
CD2 LEU A 277
1.00 36.52
CD2 LEU A 277
1.00 25.33
1.00 24.85
1.00 25.23
1.00 27.09
1.00 24.90
1.00 23.49
1.00 26.07
1.00 26.44
1.00 33.55
1.00 23.97
1.00 24.36
1.00 24.78
1.00 25.65
1.00 25.09
1.00 26.58
ND1 HIS A 280
1.00 30.54
ND1 HIS A 280
CD2 HIS A 280
1.00 30.15
CD2 HIS A 280
CE1 HIS A 280
1.00 30.94
CE1 HIS A 280
NE2 HIS A 280
1.00 29.14
NE2 HIS A 280
1.00 27.93
1.00 28.30
1.00 28.04
1.00 29.39
1.00 34.11
1.00 42.36
1.00 26.22
1.00 26.82
1.00 24.97
1.00 27.55
1.00 30.60
1.00 22.32
CA AGLU A 283
0.44 21.77
CA AGLU A 283
CA BGLU A 283
0.56 20.89
CA BGLU A 283
1.00 21.73
1.00 21.71
CB AGLU A 283
0.44 26.26
CB AGLU A 283
CB BGLU A 283
0.56 24.48
CB BGLU A 283
CG AGLU A 283
0.44 28.74
CG AGLU A 283
CG BGLU A 283
0.56 27.47
CG BGLU A 283
CD AGLU A 283
0.44 29.28
CD AGLU A 283
CD BGLU A 283
0.56 26.90
CD BGLU A 283
OE1AGLU A 283
0.44 32.22
OE1AGLU A 283
OE1BGLU A 283
0.56 32.71
OE1BGLU A 283
OE2AGLU A 283
0.44 26.43
OE2AGLU A 283
OE2BGLU A 283
0.56 24.41
OE2BGLU A 283
1.00 22.32
1.00 22.46
1.00 23.26
1.00 25.89
1.00 22.34
CG1 ILE A 284
1.00 22.97
CG1 ILE A 284
CG2 ILE A 284
1.00 25.07
CG2 ILE A 284
CD1 ILE A 284
1.00 24.24
CD1 ILE A 284
1.00 25.18
1.00 29.37
1.00 27.86
1.00 31.09
1.00 37.57
1.00 49.13
1.00 58.26
OE1 GLU A 285
1.00 62.94
OE1 GLU A 285
OE2 GLU A 285
1.00 59.62
OE2 GLU A 285
1.00 23.13
1.00 21.93
1.00 16.96
1.00 21.26
1.00 20.49
1.00 25.57
1.00 30.51
OE1 GLN A 286
1.00 30.87
OE1 GLN A 286
NE2 GLN A 286
1.00 31.66
NE2 GLN A 286
1.00 18.10
1.00 15.16
1.00 18.22
1.00 20.64
1.00 17.49
1.00 17.59
CD1 LEU A 287
1.00 20.84
CD1 LEU A 287
CD2 LEU A 287
1.00 19.24
CD2 LEU A 287
1.00 22.27
1.00 23.39
1.00 25.87
1.00 29.82
1.00 26.43
OG1 THR A 288
1.00 31.55
OG1 THR A 288
CG2 THR A 288
1.00 29.30
CG2 THR A 288
1.00 26.12
1.00 30.87
1.00 32.23
1.00 33.37
1.00 34.05
1.00 41.65
1.00 44.31
1.00 47.50
1.00 47.97
1.00 33.10
1.00 37.70
1.00 42.12
1.00 44.34
1.00 40.99
CG1 ILE A 290
1.00 45.51
CG1 ILE A 290
CG2 ILE A 290
1.00 40.16
CG2 ILE A 290
CD1 ILE A 290
1.00 48.56
CD1 ILE A 290
1.00 43.76
1.00 52.05
1.00 51.30
1.00 49.70
1.00 58.29
1.00 64.73
1.00 70.61
OE1 GLU A 291
1.00 71.81
OE1 GLU A 291
OE2 GLU A 291
1.00 72.91
OE2 GLU A 291
1.00 56.00
1.00 58.51
1.00 58.31
1.00 59.46
1.00 58.69
1.00 57.82
1.00 57.44
1.00 55.86
1.00 54.93
1.00 54.88
1.00 55.86
1.00 51.37
1.00 47.89
1.00 45.39
1.00 44.60
1.00 46.41
1.00 47.92
1.00 52.01
OE1 GLU A 294
1.00 51.56
OE1 GLU A 294
OE2 GLU A 294
1.00 55.85
OE2 GLU A 294
1.00 40.73
1.00 39.67
1.00 38.14
1.00 38.43
1.00 42.75
1.00 46.97
CD1 LEU A 295
1.00 48.45
CD1 LEU A 295
CD2 LEU A 295
1.00 48.71
CD2 LEU A 295
1.00 35.40
1.00 32.74
1.00 32.82
1.00 33.92
1.00 32.65
1.00 32.43
CD1 TYR A 296
1.00 36.81
CD1 TYR A 296
CD2 TYR A 296
1.00 33.94
CD2 TYR A 296
CE1 TYR A 296
1.00 36.93
CE1 TYR A 296
CE2 TYR A 296
1.00 34.78
CE2 TYR A 296
1.00 39.09
1.00 42.26
1.00 30.75
1.00 29.15
1.00 30.36
1.00 27.68
1.00 32.08
1.00 35.25
OD1 ASN A 297
1.00 34.88
OD1 ASN A 297
ND2 ASN A 297
1.00 40.00
ND2 ASN A 297
1.00 29.81
1.00 30.11
1.00 25.53
1.00 26.82
1.00 25.75
1.00 31.71
1.00 26.69
1.00 27.25
1.00 38.21
OG1 THR A 299
1.00 43.23
OG1 THR A 299
CG2 THR A 299
1.00 36.34
CG2 THR A 299
1.00 23.77
1.00 23.16
1.00 23.19
1.00 22.71
1.00 25.99
1.00 37.59
1.00 46.75
1.00 52.65
1.00 51.95
1.00 21.41
1.00 22.56
1.00 20.95
1.00 20.64
1.00 29.15
CG1 VAL A 301
1.00 30.94
CG1 VAL A 301
CG2 VAL A 301
1.00 31.76
CG2 VAL A 301
1.00 21.26
1.00 24.17
1.00 19.94
1.00 20.39
1.00 29.78
OG1 THR A 302
1.00 30.72
OG1 THR A 302
CG2 THR A 302
1.00 31.57
CG2 THR A 302
1.00 21.72
1.00 21.23
1.00 20.09
1.00 20.31
1.00 28.35
1.00 34.22
1.00 42.96
1.00 47.03
1.00 49.46
1.00 20.45
1.00 20.39
1.00 19.94
1.00 20.05
1.00 27.44
1.00 38.37
1.00 50.67
1.00 41.01
1.00 19.10
1.00 21.78
1.00 19.43
1.00 18.97
1.00 24.85
1.00 29.59
1.00 35.42
OE1 GLU A 305
1.00 38.87
OE1 GLU A 305
OE2 GLU A 305
1.00 37.41
OE2 GLU A 305
1.00 19.03
1.00 20.20
1.00 17.28
1.00 19.14
1.00 22.65
1.00 36.81
OD1 ASP A 306
1.00 41.02
OD1 ASP A 306
OD2 ASP A 306
1.00 40.09
OD2 ASP A 306
1.00 18.19
1.00 18.56
1.00 17.83
1.00 15.75
1.00 18.79
1.00 28.45
OD1 ASP A 307
1.00 33.30
OD1 ASP A 307
OD2 ASP A 307
1.00 27.52
OD2 ASP A 307
1.00 16.38
1.00 16.18
1.00 12.84
1.00 15.87
1.00 16.29
CG1 ILE A 308
1.00 18.27
CG1 ILE A 308
CG2 ILE A 308
1.00 17.59
CG2 ILE A 308
CD1 ILE A 308
1.00 20.79
CD1 ILE A 308
1.00 14.30
1.00 14.54
1.00 14.66
1.00 15.88
1.00 19.07
1.00 21.09
1.00 26.55
1.00 35.46
1.00 40.08
1.00 15.11
1.00 16.23
1.00 14.84
1.00 16.30
1.00 18.87
1.00 25.96
1.00 32.22
1.00 38.67
1.00 40.44
1.00 15.10
1.00 15.04
1.00 14.18
1.00 15.84
1.00 17.03
1.00 21.01
CD1 LEU A 311
1.00 24.22
CD1 LEU A 311
CD2 LEU A 311
1.00 24.97
CD2 LEU A 311
1.00 14.71
1.00 14.99
1.00 15.44
1.00 15.21
1.00 15.34
1.00 17.53
CD1 LEU A 312
1.00 19.86
CD1 LEU A 312
CD2 LEU A 312
1.00 18.85
CD2 LEU A 312
1.00 14.66
1.00 14.56
1.00 14.27
1.00 12.68
1.00 14.86
CA AARG A 314
0.53 15.20
CA AARG A 314
CA BARG A 314
0.47 15.95
CA BARG A 314
1.00 15.95
1.00 18.44
CB AARG A 314
0.53 14.14
CB AARG A 314
CB BARG A 314
0.47 16.32
CB BARG A 314
CG AARG A 314
0.53 16.74
CG AARG A 314
CG BARG A 314
0.47 19.34
CG BARG A 314
CD AARG A 314
0.53 17.82
CD AARG A 314
CD BARG A 314
0.47 16.67
CD BARG A 314
NE AARG A 314
0.53 20.35
NE AARG A 314
NE BARG A 314
0.47 15.13
NE BARG A 314
CZ AARG A 314
0.53 21.42
CZ AARG A 314
CZ BARG A 314
0.47 16.26
CZ BARG A 314
NH1AARG A 314
0.53 19.81
NH1AARG A 314
NH1BARG A 314
0.47 18.32
NH1BARG A 314
NH2AARG A 314
0.53 18.56
NH2AARG A 314
NH2BARG A 314
0.47 13.45
NH2BARG A 314
1.00 14.94
1.00 16.83
1.00 15.61
1.00 23.98
1.00 19.45
1.00 20.24
CD1 TYR A 315
1.00 24.35
CD1 TYR A 315
CD2 TYR A 315
1.00 24.07
CD2 TYR A 315
CE1 TYR A 315
1.00 28.02
CE1 TYR A 315
CE2 TYR A 315
1.00 27.89
CE2 TYR A 315
1.00 31.37
1.00 39.03
1.00 14.81
1.00 17.61
1.00 14.42
1.00 16.19
1.00 14.19
1.00 16.46
1.00 17.19
1.00 19.30
1.00 14.65
1.00 16.20
CD1 TYR A 317
1.00 17.40
CD1 TYR A 317
CD2 TYR A 317
1.00 16.82
CD2 TYR A 317
CE1 TYR A 317
1.00 20.08
CE1 TYR A 317
CE2 TYR A 317
1.00 18.19
CE2 TYR A 317
1.00 21.43
1.00 25.02
1.00 17.31
1.00 20.14
1.00 21.13
1.00 22.20
1.00 19.80
1.00 18.07
1.00 20.60
1.00 21.55
1.00 24.97
1.00 24.01
1.00 25.84
CD1 TYR A 319
1.00 30.74
CD1 TYR A 319
CD2 TYR A 319
1.00 24.45
CD2 TYR A 319
CE1 TYR A 319
1.00 31.35
CE1 TYR A 319
CE2 TYR A 319
1.00 24.97
CE2 TYR A 319
1.00 30.11
1.00 35.07
1.00 21.46
1.00 22.22
1.00 25.03
1.00 27.93
1.00 24.50
1.00 22.44
1.00 20.47
1.00 26.56
1.00 27.33
1.00 27.72
1.00 26.20
1.00 32.20
1.00 39.94
1.00 49.23
1.00 57.10
1.00 60.39
NH1 ARG A 321
1.00 63.17
NH1 ARG A 321
NH2 ARG A 321
1.00 61.05
NH2 ARG A 321
1.00 24.82
1.00 24.40
1.00 29.56
1.00 32.04
1.00 26.66
CG1 VAL A 322
1.00 26.27
CG1 VAL A 322
CG2 VAL A 322
1.00 24.67
CG2 VAL A 322
1.00 28.42
1.00 31.54
1.00 31.59
1.00 33.44
1.00 38.91
1.00 49.05
1.00 59.05
OE1 GLN A 323
1.00 62.28
OE1 GLN A 323
NE2 GLN A 323
1.00 63.12
NE2 GLN A 323
1.00 28.44
1.00 30.31
1.00 32.95
1.00 35.19
1.00 33.64
1.00 36.09
1.00 33.98
1.00 36.33
1.00 35.31
1.00 36.59
1.00 45.66
1.00 57.96
1.00 66.41
1.00 64.70
1.00 32.39
1.00 34.03
1.00 34.27
1.00 35.95
1.00 36.96
1.00 38.15
1.00 35.03
1.00 31.40
1.00 35.64
1.00 34.03
1.00 32.59
1.00 39.84
1.00 50.91
1.00 58.81
OE1 GLU A 327
1.00 61.33
OE1 GLU A 327
OE2 GLU A 327
1.00 62.26
OE2 GLU A 327
1.00 32.98
1.00 34.23
1.00 36.56
1.00 39.95
1.00 34.80
CG1 ILE A 328
1.00 35.14
CG1 ILE A 328
CG2 ILE A 328
1.00 36.14
CG2 ILE A 328
CD1 ILE A 328
1.00 38.45
CD1 ILE A 328
1.00 39.95
1.00 43.07
1.00 43.63
1.00 41.71
1.00 45.34
1.00 48.87
OD1 ASN A 329
1.00 48.09
OD1 ASN A 329
ND2 ASN A 329
1.00 50.42
ND2 ASN A 329
1.00 47.28
1.00 49.32
1.00 48.92
1.00 51.53
1.00 50.20
1.00 53.70
OD1 ASP A 330
1.00 53.36
OD1 ASP A 330
OD2 ASP A 330
1.00 56.85
OD2 ASP A 330
1.00 49.49
1.00 52.52
1.00 54.07
1.00 53.44
1.00 53.33
1.00 54.08
1.00 54.98
1.00 50.72
1.00 50.01
1.00 60.61
1.00 66.77
OD1 ASP A 332
1.00 69.52
OD1 ASP A 332
OD2 ASP A 332
1.00 68.23
OD2 ASP A 332
1.00 49.25
1.00 48.42
1.00 44.81
1.00 44.72
1.00 52.50
1.00 58.20
1.00 61.23
1.00 65.04
1.00 67.19
1.00 39.56
1.00 38.36
1.00 39.12
1.00 41.18
1.00 41.81
OG1 THR A 334
1.00 41.58
OG1 THR A 334
CG2 THR A 334
1.00 44.42
CG2 THR A 334
1.00 35.72
1.00 34.99
1.00 33.64
1.00 34.93
1.00 32.69
CG1 VAL A 335
1.00 33.92
CG1 VAL A 335
CG2 VAL A 335
1.00 35.18
CG2 VAL A 335
1.00 31.32
1.00 32.91
1.00 34.50
1.00 36.62
1.00 37.36
1.00 43.59
1.00 48.33
1.00 51.49
1.00 54.09
1.00 28.63
1.00 31.21
1.00 28.88
1.00 31.65
1.00 34.73
1.00 37.26
CD1 LEU A 337
1.00 39.08
CD1 LEU A 337
CD2 LEU A 337
1.00 42.36
CD2 LEU A 337
1.00 29.40
1.00 33.81
1.00 33.85
1.00 35.66
1.00 37.14
1.00 46.40
1.00 53.70
1.00 61.48
1.00 64.90
NH1 ARG A 338
1.00 65.46
NH1 ARG A 338
NH2 ARG A 338
1.00 65.88
NH2 ARG A 338
1.00 30.15
1.00 29.53
1.00 28.33
1.00 32.95
1.00 30.08
CG1 VAL A 339
1.00 29.53
CG1 VAL A 339
CG2 VAL A 339
1.00 29.40
CG2 VAL A 339
1.00 25.59
1.00 27.66
1.00 28.22
1.00 28.56
1.00 31.05
1.00 40.63
OD1 ASN A 340
1.00 44.63
OD1 ASN A 340
ND2 ASN A 340
1.00 44.21
ND2 ASN A 340
1.00 25.48
1.00 23.12
1.00 25.28
1.00 28.45
1.00 23.65
CG1 VAL A 341
1.00 26.15
CG1 VAL A 341
CG2 VAL A 341
1.00 27.49
CG2 VAL A 341
1.00 26.14
1.00 29.78
1.00 27.59
1.00 27.50
1.00 34.94
1.00 42.96
OD1 ASP A 342
1.00 43.88
OD1 ASP A 342
OD2 ASP A 342
1.00 47.51
OD2 ASP A 342
1.00 23.34
1.00 19.66
1.00 20.91
1.00 20.31
1.00 19.50
1.00 23.58
1.00 23.95
1.00 21.30
1.00 23.21
1.00 23.27
1.00 22.24
1.00 18.78
1.00 16.96
15.228 -10.223
1.00 28.47
14.934 -11.572
1.00 41.13
OD1 ASN A 345
13.916 -12.191
1.00 50.41
OD1 ASN A 345
ND2 ASN A 345
15.818 -12.029
1.00 39.27
ND2 ASN A 345
1.00 21.38
1.00 16.94
19.653 -10.120
1.00 15.70
19.374 -11.312
1.00 18.39
1.00 20.03
1.00 16.39
1.00 18.75
1.00 21.17
1.00 25.91
NH1 ARG A 346
1.00 29.29
NH1 ARG A 346
NH2 ARG A 346
1.00 32.04
NH2 ARG A 346
1.00 13.07
21.321 -10.511
1.00 12.50
22.785 -10.664
1.00 12.11
1.00 11.36
1.00 13.65
1.00 14.17
CD1 PHE A 347
19.436 -10.974
1.00 16.29
CD1 PHE A 347
CD2 PHE A 347
1.00 17.80
CD2 PHE A 347
CE1 PHE A 347
18.163 -10.988
1.00 18.12
CE1 PHE A 347
CE2 PHE A 347
1.00 22.23
CE2 PHE A 347
1.00 20.67
23.341 -11.831
1.00 11.65
24.782 -12.022
25.366 -12.324
1.00 10.12
24.638 -12.668
1.00 10.86
25.151 -13.095
1.00 11.79
24.768 -14.508
1.00 12.58
CD1 TYR A 348
25.684 -15.377
1.00 15.90
CD1 TYR A 348
CD2 TYR A 348
23.506 -14.999
1.00 15.69
CD2 TYR A 348
CE1 TYR A 348
25.341 -16.690
1.00 16.20
CE1 TYR A 348
CE2 TYR A 348
23.158 -16.310
1.00 18.26
CE2 TYR A 348
24.076 -17.147
1.00 17.90
23.702 -18.443
1.00 20.80
26.680 -12.198
1.00 10.30
27.334 -12.277
27.799 -13.698
1.00 10.33
28.531 -14.306
1.00 12.14
28.522 -11.299
1.00 10.98
CG1 VAL A 349
29.263 -11.465
1.00 12.41
CG1 VAL A 349
CG2 VAL A 349
1.00 11.34
CG2 VAL A 349
27.377 -14.216
27.834 -15.516
1.00 10.39
29.209 -15.349
1.00 12.60
30.207 -15.886
1.00 17.67
26.821 -16.118
1.00 13.30
27.193 -17.508
1.00 14.83
26.350 -17.911
1.00 16.85
26.776 -17.220
1.00 19.09
27.592 -17.741
1.00 21.09
NH1 ARG A 350
28.086 -18.970
1.00 26.86
NH1 ARG A 350
NH2 ARG A 350
27.921 -17.030
1.00 23.89
NH2 ARG A 350
29.257 -14.597
1.00 12.06
30.508 -14.372
1.00 12.13
30.674 -12.921
1.00 10.07
29.698 -12.220
1.00 11.80
30.589 -15.229
1.00 17.09
30.831 -16.703
1.00 26.52
32.180 -16.938
1.00 38.10
33.315 -16.430
1.00 43.26
34.642 -16.526
1.00 44.19
31.922 -12.480
1.00 10.94
32.293 -11.238
32.879 -11.624
33.805 -12.438
1.00 10.66
33.328 -10.452
CG1 ILE A 352
32.733 -10.007
1.00 12.09
CG1 ILE A 352
CG2 ILE A 352
1.00 11.15
CG2 ILE A 352
CD1 ILE A 352
1.00 16.98
CD1 ILE A 352
32.324 -11.029
32.678 -11.330 -10.485
33.186 -10.070 -11.178
-8.983 -10.970
1.00 12.79
31.443 -11.862 -11.210
1.00 11.25
31.034 -13.269 -10.777
1.00 15.36
29.540 -13.540 -10.987
1.00 18.88
29.088 -13.185 -12.330
1.00 18.14
27.814 -12.997 -12.674
1.00 19.27
NH1 ARG A 353
26.834 -13.132 -11.778
1.00 19.69
NH1 ARG A 353
NH2 ARG A 353
27.517 -12.655 -13.915
1.00 20.78
NH2 ARG A 353
34.224 -10.224 -11.987
-9.150 -12.824
-9.539 -14.271
34.844 -10.626 -14.707
1.00 11.15
-8.974 -12.581
1.00 10.08
-8.668 -11.153
CD1 PHE A 354
-7.426 -10.614
1.00 11.32
CD1 PHE A 354
CD2 PHE A 354
-9.620 -10.329
1.00 10.71
CD2 PHE A 354
CE1 PHE A 354
1.00 12.38
CE1 PHE A 354
CE2 PHE A 354
1.00 10.93
CE2 PHE A 354
1.00 10.99
-8.666 -15.006
1.00 10.10
-8.932 -16.392
1.00 11.00
-7.818 -17.262
1.00 12.94
-6.654 -17.034
1.00 14.83
-9.086 -16.586
1.00 14.10
31.443 -10.325 -15.877
1.00 18.61
29.982 -10.623 -16.168
1.00 24.62
OE1 GLU A 355
-9.734 -16.674
1.00 29.33
OE1 GLU A 355
OE2 GLU A 355
29.551 -11.763 -15.876
1.00 29.66
OE2 GLU A 355
-8.181 -18.252
1.00 12.64
-7.203 -19.158
1.00 11.19
-7.025 -18.998
1.00 12.23
-6.358 -19.812
1.00 15.24
-7.615 -17.953
1.00 13.98
-7.529 -17.739
1.00 15.98
-8.521 -18.648
1.00 18.33
-9.673 -18.291
1.00 28.21
-7.748 -16.261
1.00 14.02
-9.100 -15.745
1.00 14.23
OD1 ASN A 357
-9.477 -15.878
1.00 14.21
OD1 ASN A 357
ND2 ASN A 357
-9.837 -15.147
1.00 17.06
ND2 ASN A 357
-8.053 -19.822
1.00 23.55
-8.894 -20.819
1.00 30.07
-8.930 -20.668
1.00 34.80
-9.906 -21.060
1.00 41.07
-8.419 -22.236
1.00 36.09
-8.616 -22.581
1.00 46.83
OD1 ASP A 358
-9.655 -22.184
1.00 50.80
OD1 ASP A 358
OD2 ASP A 358
-7.735 -23.251
1.00 50.62
OD2 ASP A 358
-7.857 -20.124
1.00 30.88
-7.726 -20.000
1.00 31.47
-7.806 -18.542
1.00 30.83
-8.474 -18.192
1.00 32.75
-6.388 -20.570
1.00 38.37
OG1 THR A 359
-6.320 -21.970
1.00 45.01
OG1 THR A 359
CG2 THR A 359
-6.245 -20.368
1.00 42.78
CG2 THR A 359
-7.117 -17.698
1.00 24.40
-7.126 -16.264
1.00 21.81
-8.426 -15.645
1.00 22.23
-8.776 -15.743
1.00 24.24
-5.934 -15.602
1.00 21.50
-4.726 -16.038
1.00 27.43
-9.140 -15.008
1.00 20.19
44.279 -10.418 -14.411
1.00 20.81
43.355 -10.270 -13.209
1.00 19.04
-9.287 -12.468
1.00 17.72
45.561 -11.133 -13.984
1.00 23.56
46.498 -11.507 -15.128
1.00 29.30
45.808 -12.423 -16.121
1.00 32.08
46.813 -13.120 -17.017
1.00 42.78
47.650 -12.154 -17.774
1.00 48.34
42.517 -11.272 -13.018
1.00 16.23
41.611 -11.304 -11.889
1.00 13.04
42.268 -10.896 -10.562
1.00 12.60
41.677 -10.140
1.00 13.08
41.017 -12.705 -11.769
1.00 15.57
39.967 -12.794 -10.687
1.00 18.60
OD1 ASP A 362
38.778 -12.535 -10.996
1.00 20.74
OD1 ASP A 362
OD2 ASP A 362
40.330 -13.125
1.00 19.69
OD2 ASP A 362
43.473 -11.394 -10.280
1.00 14.07
44.093 -11.174
1.00 13.38
1.00 11.45
1.00 13.87
45.403 -11.954
1.00 17.92
1.00 13.00
1.00 17.45
1.00 14.36
1.00 15.52
-6.930 -10.930
1.00 21.27
CG1 VAL A 364
-5.421 -10.868
1.00 26.56
CG1 VAL A 364
CG2 VAL A 364
-7.540 -11.216
1.00 24.66
CG2 VAL A 364
1.00 13.52
CA ALEU A 365
0.55 11.41
CA ALEU A 365
CA BLEU A 365
0.45 12.15
CA BLEU A 365
1.00 10.81
CB ALEU A 365
-6.813 -10.449
0.55 11.19
CB ALEU A 365
CB BLEU A 365
-6.981 -10.406
0.45 13.98
CB BLEU A 365
CG ALEU A 365
-6.035 -11.759
0.55 13.07
CG ALEU A 365
CG BLEU A 365
-6.619 -11.875
0.45 18.40
CG BLEU A 365
CD1ALEU A 365
-4.995 -11.598
0.55 16.11
CD1ALEU A 365
CD1BLEU A 365
-7.848 -12.648
0.45 22.68
CD1BLEU A 365
CD2ALEU A 365
-6.959 -12.883
0.55 14.82
CD2ALEU A 365
CD2BLEU A 365
-6.015 -12.482
0.45 14.18
CD2BLEU A 365
1.00 10.07
1.00 10.88
1.00 12.93
40.529 -10.461
1.00 12.97
39.526 -11.179
1.00 15.20
39.323 -12.655
1.00 15.03
38.670 -12.791
1.00 16.60
37.354 -12.779
1.00 16.73
NH1 ARG A 366
36.513 -12.651
1.00 16.25
NH1 ARG A 366
NH2 ARG A 366
36.874 -12.910
1.00 17.72
NH2 ARG A 366
1.00 11.54
1.00 12.93
1.00 14.28
1.00 17.24
1.00 14.98
1.00 16.29
1.00 18.00
1.00 18.16
1.00 17.28
NH1 ARG A 367
1.00 21.88
NH1 ARG A 367
NH2 ARG A 367
1.00 19.12
NH2 ARG A 367
1.00 12.06
1.00 13.16
1.00 12.06
1.00 15.41
1.00 11.52
1.00 15.01
1.00 19.58
OE1 GLU A 368
1.00 19.81
OE1 GLU A 368
OE2 GLU A 368
1.00 22.15
OE2 GLU A 368
1.00 10.53
1.00 11.22
1.00 10.97
1.00 14.92
1.00 10.06
1.00 13.06
1.00 12.72
1.00 10.18
1.00 10.25
1.00 14.02
1.00 13.21
1.00 18.45
1.00 23.00
1.00 30.54
1.00 39.14
NH1 ARG A 370
1.00 40.41
NH1 ARG A 370
NH2 ARG A 370
1.00 37.74
NH2 ARG A 370
1.00 10.17
1.00 11.62
OE1 GLN A 371
1.00 11.70
OE1 GLN A 371
NE2 GLN A 371
NE2 GLN A 371
34.048 -10.433
32.953 -11.356
1.00 10.56
31.770 -11.157
1.00 11.44
34.409 -10.821
1.00 12.54
1.00 16.39
37.051 -10.113
1.00 24.13
1.00 27.91
33.353 -12.381
1.00 10.16
32.403 -13.381
31.953 -14.236
1.00 11.05
32.774 -14.671
1.00 10.68
33.022 -14.249
1.00 11.56
33.263 -13.459
1.00 14.26
34.210 -14.164
1.00 20.34
OE1 GLU A 373
35.170 -14.816
1.00 31.93
OE1 GLU A 373
OE2 GLU A 373
34.000 -14.063
1.00 18.66
OE2 GLU A 373
30.649 -14.455
1.00 10.57
30.076 -15.227
1.00 12.17
29.498 -14.351
1.00 11.39
28.701 -14.819
1.00 12.75
29.882 -13.072
1.00 10.39
29.456 -12.153
1.00 10.84
28.220 -11.388
1.00 11.10
27.906 -11.337
1.00 10.90
30.590 -11.156
1.00 10.71
27.530 -10.775
1.00 10.29
1.00 11.24
1.00 11.07
1.00 11.17
1.00 13.96
25.181 -10.058
1.00 14.58
CD1 TRP A 376
25.511 -10.236
1.00 20.98
CD1 TRP A 376
CD2 TRP A 376
24.019 -10.867
1.00 15.53
CD2 TRP A 376
NE1 TRP A 376
24.637 -11.112
1.00 21.15
NE1 TRP A 376
CE2 TRP A 376
23.711 -11.511
1.00 19.34
CE2 TRP A 376
CE3 TRP A 376
23.216 -11.108
1.00 15.03
CE3 TRP A 376
CZ2 TRP A 376
22.636 -12.392
1.00 21.42
CZ2 TRP A 376
CZ3 TRP A 376
22.152 -11.989
1.00 16.44
CZ3 TRP A 376
CH2 TRP A 376
21.867 -12.611
1.00 19.60
CH2 TRP A 376
1.00 10.99
1.00 11.92
1.00 13.98
1.00 14.78
1.00 10.50
1.00 12.70
CD1 LEU A 377
1.00 14.47
CD1 LEU A 377
CD2 LEU A 377
1.00 15.52
CD2 LEU A 377
1.00 12.79
1.00 12.98
1.00 11.89
1.00 13.48
1.00 12.11
1.00 13.47
1.00 10.31
1.00 13.48
1.00 18.31
1.00 23.52
1.00 12.05
1.00 12.24
1.00 10.93
1.00 13.37
1.00 13.82
1.00 20.12
OD1 ASP A 380
1.00 19.97
OD1 ASP A 380
OD2 ASP A 380
1.00 25.71
OD2 ASP A 380
1.00 10.34
1.00 10.75
1.00 10.12
1.00 11.40
1.00 11.67
1.00 14.19
CD1 LEU A 381
1.00 14.74
CD1 LEU A 381
CD2 LEU A 381
1.00 16.41
CD2 LEU A 381
1.00 11.24
1.00 10.39
CG1 VAL A 382
1.00 13.21
CG1 VAL A 382
CG2 VAL A 382
1.00 14.02
CG2 VAL A 382
1.00 10.72
1.00 11.36
1.00 10.92
1.00 10.10
1.00 14.72
1.00 25.05
OD1 ASP A 383
1.00 27.32
OD1 ASP A 383
OD2 ASP A 383
1.00 28.05
OD2 ASP A 383
1.00 10.78
1.00 11.57
1.00 10.23
1.00 12.29
1.00 14.46
1.00 18.70
OE1 GLN A 384
1.00 22.29
OE1 GLN A 384
NE2 GLN A 384
1.00 24.14
NE2 GLN A 384
1.00 10.08
1.00 10.32
1.00 10.03
1.00 12.89
1.00 16.53
1.00 31.21
1.00 39.87
1.00 46.88
1.00 10.03
1.00 10.90
1.00 19.92
OE1 GLU A 387
1.00 21.36
OE1 GLU A 387
OE2 GLU A 387
1.00 23.56
OE2 GLU A 387
1.00 10.45
1.00 10.61
1.00 12.92
1.00 10.12
1.00 12.35
1.00 17.97
1.00 21.06
NH1 ARG A 388
1.00 28.80
NH1 ARG A 388
NH2 ARG A 388
1.00 23.78
NH2 ARG A 388
1.00 10.79
1.00 10.92
ANISOU 1000
1.225 -10.282
1.00 12.24
ANISOU 1001
1.271 -11.149
1.00 13.88
ANISOU 1002
1.00 12.94
ANISOU 1003
1.00 12.66
ANISOU 1004
CD1 LEU A 389
1.00 17.43
ANISOU 1005
CD1 LEU A 389
CD2 LEU A 389
1.00 15.52
ANISOU 1006
CD2 LEU A 389
2.208 -10.092
ANISOU 1007
CA AASN A 390
3.430 -10.874
0.65 10.82
ANISOU 1008
CA AASN A 390
CA BASN A 390
3.441 -10.875
0.35 10.77
ANISOU 1009
CA BASN A 390
4.183 -10.679
1.00 12.05
ANISOU 1010
4.744 -11.626
1.00 16.06
ANISOU 1011
CB AASN A 390
4.328 -10.519
0.65 12.45
ANISOU 1012
CB AASN A 390
CB BASN A 390
4.379 -10.536
0.35 11.05
ANISOU 1013
CB BASN A 390
CG AASN A 390
5.611 -11.283
0.65 14.88
ANISOU 1014
CG AASN A 390
CG BASN A 390
4.024 -11.272
0.35 12.18
ANISOU 1015
CG BASN A 390
OD1AASN A 390
5.610 -12.502
0.65 16.50
ANISOU 1016
OD1AASN A 390
OD1BASN A 390
3.467 -12.372
0.35 17.85
ANISOU 1017
OD1BASN A 390
ND2AASN A 390
6.726 -10.573
0.65 18.14
ANISOU 1018
ND2AASN A 390
ND2BASN A 390
4.343 -10.673
0.35 14.65
ANISOU 1019
ND2BASN A 390
1.00 10.20
ANISOU 1020
CA AARG A 391
0.64 12.77
ANISOU 1021
CA AARG A 391
CA BARG A 391
0.36 12.37
ANISOU 1022
CA BARG A 391
1.00 13.75
ANISOU 1023
5.115 -10.279
1.00 16.83
ANISOU 1024
CB AARG A 391
0.64 14.34
ANISOU 1025
CB AARG A 391
CB BARG A 391
0.36 10.35
ANISOU 1026
CB BARG A 391
CG AARG A 391
0.64 15.43
ANISOU 1027
CG AARG A 391
CG BARG A 391
0.36 10.68
ANISOU 1028
CG BARG A 391
CD AARG A 391
0.64 18.31
ANISOU 1029
CD AARG A 391
CD BARG A 391
0.36 10.48
ANISOU 1030
CD BARG A 391
NE AARG A 391
0.64 19.47
ANISOU 1031
NE AARG A 391
NE BARG A 391
0.36 11.31
ANISOU 1032
NE BARG A 391
CZ AARG A 391
0.64 20.32
ANISOU 1033
CZ AARG A 391
CZ BARG A 391
0.36 13.18
ANISOU 1034
CZ BARG A 391
NH1AARG A 391
0.64 20.02
ANISOU 1035
NH1AARG A 391
NH1BARG A 391
0.36 10.20
ANISOU 1036
NH1BARG A 391
NH2AARG A 391
0.64 22.74
ANISOU 1037
NH2AARG A 391
NH2BARG A 391
0.36 17.52
ANISOU 1038
NH2BARG A 391
3.064 -10.196
1.00 13.88
ANISOU 1039
2.395 -10.889
1.00 16.27
ANISOU 1040
2.938 -12.277
1.00 16.68
ANISOU 1041
2.891 -12.715
1.00 19.69
ANISOU 1042
0.890 -10.988
1.00 17.77
ANISOU 1043
1.00 23.24
ANISOU 1044
CD1 LEU A 392
1.00 26.04
ANISOU 1045
CD1 LEU A 392
CD2 LEU A 392
1.00 24.25
ANISOU 1046
CD2 LEU A 392
3.407 -12.978
1.00 14.69
ANISOU 1047
3.969 -14.306
1.00 17.29
ANISOU 1048
2.923 -15.398
1.00 16.11
ANISOU 1049
3.254 -16.546
1.00 17.25
ANISOU 1050
1.662 -15.049
1.00 15.47
ANISOU 1051
0.574 -16.031
1.00 15.61
ANISOU 1052
0.515 -16.906
1.00 15.25
ANISOU 1053
-0.026 -18.015
1.00 17.33
ANISOU 1054
-0.781 -15.333
1.00 18.15
ANISOU 1055
-0.911 -14.494
1.00 21.28
ANISOU 1056
CD1 PHE A 394
-0.064 -14.681
1.00 24.45
ANISOU 1057
CD1 PHE A 394
CD2 PHE A 394
-1.896 -13.522
1.00 24.12
ANISOU 1058
CD2 PHE A 394
CE1 PHE A 394
-0.193 -13.907
1.00 25.87
ANISOU 1059
CE1 PHE A 394
CE2 PHE A 394
-2.033 -12.747
1.00 24.72
ANISOU 1060
CE2 PHE A 394
-1.181 -12.938
1.00 27.88
ANISOU 1061
1.037 -16.394
1.00 14.08
ANISOU 1062
0.896 -17.058
1.00 14.52
ANISOU 1063
2.232 -17.479
1.00 14.51
ANISOU 1064
3.225 -16.750
1.00 19.13
ANISOU 1065
0.129 -16.143
1.00 15.12
ANISOU 1066
-1.098 -15.548
1.00 17.26
ANISOU 1067
CD1 PHE A 395
-2.184 -16.349
1.00 20.22
ANISOU 1068
CD1 PHE A 395
CD2 PHE A 395
-1.149 -14.203
1.00 18.11
ANISOU 1069
CD2 PHE A 395
CE1 PHE A 395
-3.303 -15.810
1.00 20.99
ANISOU 1070
CE1 PHE A 395
CE2 PHE A 395
-2.278 -13.656
1.00 22.42
ANISOU 1071
CE2 PHE A 395
-3.352 -14.460
1.00 21.80
ANISOU 1072
2.240 -18.650
1.00 15.13
ANISOU 1073
3.397 -19.104
1.00 17.34
ANISOU 1074
3.578 -18.240
1.00 17.60
ANISOU 1075
4.704 -17.905
1.00 19.01
ANISOU 1076
3.203 -20.550
1.00 24.91
ANISOU 1077
3.134 -21.579
1.00 29.25
ANISOU 1078
3.114 -23.005
1.00 30.29
ANISOU 1079
OE1 GLU A 396
2.927 -23.174
1.00 34.63
ANISOU 1080
OE1 GLU A 396
OE2 GLU A 396
3.289 -23.948
1.00 34.76
ANISOU 1081
OE2 GLU A 396
2.462 -17.917
1.00 19.27
ANISOU 1082
2.464 -17.125
1.00 18.96
ANISOU 1083
1.305 -16.131
1.00 15.81
ANISOU 1084
0.250 -16.426
1.00 15.35
ANISOU 1085
2.317 -18.012
1.00 21.27
ANISOU 1086
OG1 THR A 397
1.055 -18.694
1.00 28.14
ANISOU 1087
OG1 THR A 397
CG2 THR A 397
3.424 -19.032
1.00 23.65
ANISOU 1088
CG2 THR A 397
1.541 -14.956
1.00 15.15
ANISOU 1089
0.523 -13.953
1.00 14.93
ANISOU 1090
0.748 -13.425
1.00 18.22
ANISOU 1091
1.824 -12.922
1.00 21.11
ANISOU 1092
0.636 -12.770
1.00 15.51
ANISOU 1093
CG1 VAL A 398
-0.466 -11.764
1.00 15.06
ANISOU 1094
CG1 VAL A 398
CG2 VAL A 398
0.556 -13.260
1.00 15.96
ANISOU 1095
CG2 VAL A 398
-0.260 -13.577
1.00 18.67
ANISOU 1096
-0.201 -13.086
1.00 21.54
ANISOU 1097
-1.386 -12.170
1.00 17.86
ANISOU 1098
-2.414 -12.304
1.00 19.08
ANISOU 1099
-0.233 -14.259
1.00 29.61
ANISOU 1100
1.001 -15.143
1.00 47.37
ANISOU 1101
OD1 ASP A 399
2.132 -14.605
1.00 52.19
ANISOU 1102
OD1 ASP A 399
OD2 ASP A 399
0.840 -16.378
1.00 51.64
ANISOU 1103
OD2 ASP A 399
-1.241 -11.213
1.00 15.17
ANISOU 1104
-2.387 -10.389
1.00 15.94
ANISOU 1105
-2.748 -10.569
1.00 15.70
ANISOU 1106
-1.885 -10.759
1.00 19.31
ANISOU 1107
1.00 18.84
ANISOU 1108
OG1 THR A 400
1.00 20.65
ANISOU 1109
OG1 THR A 400
CG2 THR A 400
1.00 26.30
ANISOU 1110
CG2 THR A 400
-4.046 -10.494
1.00 16.24
ANISOU 1111
-4.592 -10.563
1.00 20.23
ANISOU 1112
1.00 16.92
ANISOU 1113
1.00 18.95
ANISOU 1114
-5.267 -11.916
1.00 23.63
ANISOU 1115
-5.674 -12.137
1.00 35.47
ANISOU 1116
OD1 ASP A 401
-5.168 -11.413
1.00 41.55
ANISOU 1117
OD1 ASP A 401
OD2 ASP A 401
-6.500 -13.044
1.00 37.13
ANISOU 1118
OD2 ASP A 401
1.00 16.09
ANISOU 1119
1.00 17.98
ANISOU 1120
1.00 22.63
ANISOU 1121
1.00 29.21
ANISOU 1122
1.00 22.49
ANISOU 1123
OG1 THR A 402
1.00 22.31
ANISOU 1124
OG1 THR A 402
CG2 THR A 402
1.00 22.34
ANISOU 1125
CG2 THR A 402
1.00 21.23
ANISOU 1126
1.00 24.64
ANISOU 1127
21.835 -10.329
1.00 22.95
ANISOU 1128
22.616 -11.001
1.00 19.58
ANISOU 1129
-9.898 -10.195
1.00 26.56
ANISOU 1130
-9.041 -11.192
1.00 34.10
ANISOU 1131
-9.880 -12.329
1.00 39.60
ANISOU 1132
OE1 GLN A 403
24.339 -11.110 -12.239
1.00 42.37
ANISOU 1133
OE1 GLN A 403
NE2 GLN A 403
-9.220 -13.403
1.00 39.95
ANISOU 1134
NE2 GLN A 403
20.533 -10.583
1.00 24.04
ANISOU 1135
CA AARG A 404
19.967 -11.736
0.51 24.53
ANISOU 1136
CA AARG A 404
CA BARG A 404
20.013 -11.736
0.49 24.13
ANISOU 1137
CA BARG A 404
20.507 -13.022
1.00 25.43
ANISOU 1138
20.814 -13.054
1.00 26.59
ANISOU 1139
CB AARG A 404
18.440 -11.720
0.51 26.31
ANISOU 1140
CB AARG A 404
CB BARG A 404
18.486 -11.710
0.49 25.54
ANISOU 1141
CB BARG A 404
CG AARG A 404
17.782 -10.446
0.51 27.71
ANISOU 1142
CG AARG A 404
CG BARG A 404
17.940 -10.608
0.49 25.73
ANISOU 1143
CG BARG A 404
CD AARG A 404
16.289 -10.436
0.51 26.53
ANISOU 1144
CD AARG A 404
CD BARG A 404
16.522 -10.912
0.49 28.51
ANISOU 1145
CD BARG A 404
NE AARG A 404
0.51 29.16
ANISOU 1146
NE AARG A 404
NE BARG A 404
16.471 -12.048
0.49 26.54
ANISOU 1147
NE BARG A 404
CZ AARG A 404
0.51 30.59
ANISOU 1148
CZ AARG A 404
CZ BARG A 404
15.375 -12.436
0.49 34.47
ANISOU 1149
CZ BARG A 404
NH1AARG A 404
15.066 -10.350
0.51 28.51
ANISOU 1150
NH1AARG A 404
NH1BARG A 404
14.238 -11.779
0.49 39.06
ANISOU 1151
NH1BARG A 404
NH2AARG A 404
0.51 32.79
ANISOU 1152
NH2AARG A 404
NH2BARG A 404
15.415 -13.477
0.49 36.95
ANISOU 1153
NH2BARG A 404
20.611 -14.077
1.00 23.00
ANISOU 1154
21.105 -15.365
1.00 24.08
ANISOU 1155
19.949 -16.337
1.00 25.12
ANISOU 1156
19.213 -16.675
1.00 27.10
ANISOU 1157
22.099 -16.003
1.00 21.51
ANISOU 1158
CG1 VAL A 405
22.485 -17.401
1.00 24.82
ANISOU 1159
CG1 VAL A 405
CG2 VAL A 405
23.339 -15.140
1.00 22.73
ANISOU 1160
CG2 VAL A 405
19.776 -16.785
1.00 28.51
ANISOU 1161
18.705 -17.752
1.00 32.89
ANISOU 1162
18.777 -18.983
1.00 33.84
ANISOU 1163
19.833 -19.611
1.00 35.63
ANISOU 1164
18.980 -18.156 -10.963
1.00 33.82
ANISOU 1165
19.691 -16.981 -11.549
1.00 36.17
ANISOU 1166
20.523 -16.405 -10.438
1.00 30.66
ANISOU 1167
17.674 -19.315
1.00 33.18
ANISOU 1168
17.619 -20.483
1.00 29.38
ANISOU 1169
18.029 -20.257
1.00 29.92
ANISOU 1170
17.801 -21.118
1.00 31.99
ANISOU 1171
18.624 -19.103
1.00 28.59
ANISOU 1172
19.110 -18.790
1.00 30.78
ANISOU 1173
18.616 -17.433
1.00 32.73
ANISOU 1174
19.295 -16.423
1.00 30.01
ANISOU 1175
20.643 -18.808
1.00 31.28
ANISOU 1176
21.154 -20.109
1.00 34.35
ANISOU 1177
17.452 -17.421
1.00 32.65
ANISOU 1178
16.677 -16.249
1.00 33.67
ANISOU 1179
17.421 -15.206
1.00 28.58
ANISOU 1180
17.018 -14.041
1.00 29.61
ANISOU 1181
15.595 -16.864
1.00 38.68
ANISOU 1182
15.475 -18.254
1.00 43.16
ANISOU 1183
16.839 -18.681
1.00 36.99
ANISOU 1184
18.453 -15.598
1.00 21.16
ANISOU 1185
CA AASP A 410
19.119 -14.615
0.54 20.91
ANISOU 1186
CA AASP A 410
CA BASP A 410
19.152 -14.686
0.46 21.12
ANISOU 1187
CA BASP A 410
20.532 -14.281
1.00 16.31
ANISOU 1188
21.274 -13.599
1.00 15.31
ANISOU 1189
CB AASP A 410
19.087 -15.028
0.54 26.18
ANISOU 1190
CB AASP A 410
CB BASP A 410
19.310 -15.328
0.46 25.95
ANISOU 1191
CB BASP A 410
CG AASP A 410
19.589 -16.434
0.54 31.39
ANISOU 1192
CG AASP A 410
CG BASP A 410
17.989 -15.726
0.46 34.76
ANISOU 1193
CG BASP A 410
OD1AASP A 410
20.193 -17.004
0.54 30.70
ANISOU 1194
OD1AASP A 410
OD1BASP A 410
16.982 -15.032
0.46 37.38
ANISOU 1195
OD1BASP A 410
OD2AASP A 410
19.388 -16.966
0.54 36.70
ANISOU 1196
OD2AASP A 410
OD2BASP A 410
17.962 -16.733
0.46 37.10
ANISOU 1197
OD2BASP A 410
20.885 -14.722
1.00 15.72
ANISOU 1198
22.205 -14.432
1.00 15.06
ANISOU 1199
22.162 -13.384
1.00 14.25
ANISOU 1200
21.201 -13.313
1.00 17.91
ANISOU 1201
22.855 -15.703
1.00 16.21
ANISOU 1202
23.190 -16.765
1.00 17.49
ANISOU 1203
23.780 -18.003
1.00 21.27
ANISOU 1204
OE1 GLN A 411
23.907 -18.084
1.00 20.10
ANISOU 1205
OE1 GLN A 411
NE2 GLN A 411
24.127 -18.986
1.00 23.08
ANISOU 1206
NE2 GLN A 411
23.225 -12.587
1.00 12.48
ANISOU 1207
23.495 -11.769
1.00 11.78
ANISOU 1208
24.894 -12.069
1.00 12.22
ANISOU 1209
25.763 -12.469
1.00 11.08
ANISOU 1210
23.397 -10.241
1.00 14.18
ANISOU 1211
CG1 VAL A 412
1.00 15.85
ANISOU 1212
CG1 VAL A 412
CG2 VAL A 412
1.00 13.29
ANISOU 1213
CG2 VAL A 412
25.109 -11.874
1.00 13.09
ANISOU 1214
26.463 -11.743
1.00 11.47
ANISOU 1215
26.729 -10.260
1.00 10.55
ANISOU 1216
1.00 14.56
ANISOU 1217
26.608 -12.371
1.00 11.71
ANISOU 1218
26.728 -13.875
1.00 14.47
ANISOU 1219
OD1 ASP A 413
26.906 -14.439
1.00 15.81
ANISOU 1220
OD1 ASP A 413
OD2 ASP A 413
26.677 -14.489
1.00 18.16
ANISOU 1221
OD2 ASP A 413
1.00 10.01
ANISOU 1222
1.00 10.38
ANISOU 1223
1.00 10.75
ANISOU 1224
1.00 11.93
ANISOU 1225
1.00 11.97
ANISOU 1226
CG1 VAL A 414
1.00 13.24
ANISOU 1227
CG1 VAL A 414
CG2 VAL A 414
1.00 13.53
ANISOU 1228
CG2 VAL A 414
ANISOU 1229
-7.924 -10.640
ANISOU 1230
-6.560 -10.954
1.00 10.14
ANISOU 1231
-5.563 -11.037
1.00 13.44
ANISOU 1232
-8.350 -11.772
1.00 12.10
ANISOU 1233
CG1 VAL A 415
-8.538 -13.074
1.00 14.81
ANISOU 1234
CG1 VAL A 415
CG2 VAL A 415
-9.648 -11.404
1.00 13.29
ANISOU 1235
CG2 VAL A 415
-6.518 -11.072
ANISOU 1236
-5.328 -11.548
ANISOU 1237
-5.462 -13.053
ANISOU 1238
-6.358 -13.528
1.00 12.23
ANISOU 1239
-5.204 -10.867
1.00 10.65
ANISOU 1240
ANISOU 1241
CD1 TYR A 416
1.00 11.66
ANISOU 1242
CD1 TYR A 416
CD2 TYR A 416
ANISOU 1243
CD2 TYR A 416
CE1 TYR A 416
1.00 13.30
ANISOU 1244
CE1 TYR A 416
CE2 TYR A 416
1.00 10.67
ANISOU 1245
CE2 TYR A 416
1.00 10.66
ANISOU 1246
1.00 10.51
ANISOU 1247
-4.594 -13.801
1.00 12.10
ANISOU 1248
-4.587 -15.243
1.00 13.74
ANISOU 1249
-3.509 -15.606
1.00 13.02
ANISOU 1250
-2.326 -15.294
1.00 15.52
ANISOU 1251
-4.314 -15.877
1.00 20.57
ANISOU 1252
-5.403 -15.570
1.00 26.91
ANISOU 1253
-4.932 -15.845
1.00 34.47
ANISOU 1254
-5.955 -15.376
1.00 42.61
ANISOU 1255
-7.207 -16.186
1.00 45.62
ANISOU 1256
-3.929 -16.228
1.00 14.06
ANISOU 1257
-3.014 -16.594
1.00 13.43
ANISOU 1258
-3.018 -18.102
1.00 14.14
ANISOU 1259
-4.017 -18.785
1.00 16.13
ANISOU 1260
-3.338 -15.859
1.00 14.15
ANISOU 1261
CG1 VAL A 418
-3.403 -14.363
1.00 18.21
ANISOU 1262
CG1 VAL A 418
CG2 VAL A 418
-4.630 -16.362
1.00 14.13
ANISOU 1263
CG2 VAL A 418
-1.901 -18.611
1.00 16.48
ANISOU 1264
-1.781 -20.015
1.00 16.09
ANISOU 1265
-1.336 -20.050
1.00 15.96
ANISOU 1266
-0.311 -19.455
1.00 17.82
ANISOU 1267
-0.741 -20.696
1.00 20.23
ANISOU 1268
-0.234 -22.046
1.00 27.59
ANISOU 1269
-1.155 -23.187
1.00 31.28
ANISOU 1270
-0.508 -24.535
1.00 31.41
ANISOU 1271
-1.373 -25.685
1.00 38.78
ANISOU 1272
-2.113 -20.723
1.00 20.40
ANISOU 1273
-1.765 -20.864
1.00 26.86
ANISOU 1274
-0.937 -22.120
1.00 36.54
ANISOU 1275
-0.556 -22.836
1.00 40.19
ANISOU 1276
-3.026 -20.877
1.00 30.40
ANISOU 1277
-3.814 -19.581
1.00 27.09
ANISOU 1278
-5.021 -19.606
1.00 32.09
ANISOU 1279
OE1 GLU A 420
-5.455 -20.711
1.00 38.63
ANISOU 1280
OE1 GLU A 420
OE2 GLU A 420
-5.535 -18.520
1.00 25.99
ANISOU 1281
OE2 GLU A 420
HETATM 1283
1.00 10.34
ANISOU 1283
HETATM 1284
1.00 14.57
ANISOU 1284
HETATM 1285
36.685 -11.597 -15.738
1.00 10.83
ANISOU 1285
HETATM 1286
1.00 15.73
ANISOU 1286
HETATM 1287
36.056 -12.633
1.00 17.45
ANISOU 1287
HETATM 1288
1.00 14.32
ANISOU 1288
HETATM 1289
35.403 -12.882 -12.043
1.00 17.04
ANISOU 1289
HETATM 1290
28.788 -11.107
1.00 14.05
ANISOU 1290
HETATM 1291
1.00 19.19
ANISOU 1291
HETATM 1292
1.00 16.38
ANISOU 1292
HETATM 1293
1.00 22.37
ANISOU 1293
HETATM 1294
2.259 -13.780
1.00 19.31
ANISOU 1294
HETATM 1295
35.520 -14.909
1.00 17.93
ANISOU 1295
HETATM 1296
7.204 -18.301
1.00 21.55
ANISOU 1296
HETATM 1297
36.729 -10.156
1.00 19.65
ANISOU 1297
HETATM 1298
30.997 -13.591 -14.552
1.00 20.81
ANISOU 1298
HETATM 1299
36.754 -12.096
1.00 28.57
ANISOU 1299
HETATM 1300
1.00 22.90
ANISOU 1300
HETATM 1301
1.00 22.65
ANISOU 1301
HETATM 1302
1.00 28.57
ANISOU 1302
HETATM 1303
18.706 -13.922
1.00 28.68
ANISOU 1303
HETATM 1304
1.00 24.43
ANISOU 1304
HETATM 1305
-4.633 -21.868
1.00 26.28
ANISOU 1305
HETATM 1306
1.00 28.13
ANISOU 1306
HETATM 1307
1.00 28.13
ANISOU 1307
HETATM 1308
5.926 -16.089
1.00 26.76
ANISOU 1308
HETATM 1309
41.691 -13.167 -15.192
1.00 41.47
ANISOU 1309
HETATM 1310
1.00 22.24
ANISOU 1310
HETATM 1311
35.850 -10.961 -18.182
1.00 24.74
ANISOU 1311
HETATM 1312
-8.560 -24.439
1.00 32.37
ANISOU 1312
HETATM 1313
26.992 -21.184
1.00 32.08
ANISOU 1313
HETATM 1314
1.00 41.61
ANISOU 1314
HETATM 1315
1.00 35.65
ANISOU 1315
HETATM 1316
44.261 -11.083
1.00 21.32
ANISOU 1316
HETATM 1317
1.00 26.89
ANISOU 1317
HETATM 1318
1.00 41.10
ANISOU 1318
HETATM 1319
1.425 -11.113
1.00 36.05
ANISOU 1319
HETATM 1320
1.00 30.37
ANISOU 1320
HETATM 1321
1.00 30.59
ANISOU 1321
HETATM 1322
1.00 31.39
ANISOU 1322
HETATM 1323
1.00 69.72
ANISOU 1323
HETATM 1324
1.00 32.84
ANISOU 1324
HETATM 1325
1.00 29.18
ANISOU 1325
HETATM 1326
20.246 -10.765
1.00 40.23
ANISOU 1326
HETATM 1327
1.947 -11.149
1.00 30.62
ANISOU 1327
HETATM 1328
1.00 24.90
ANISOU 1328
HETATM 1329
19.768 -18.835
1.00 31.33
ANISOU 1329
HETATM 1330
24.160 -20.575
1.00 35.69
ANISOU 1330
HETATM 1331
42.816 -14.332
1.00 23.55
ANISOU 1331
HETATM 1332
1.00 41.00
ANISOU 1332
HETATM 1333
3.651 -15.000
1.00 41.62
ANISOU 1333
HETATM 1334
7.138 -14.695
1.00 39.12
ANISOU 1334
HETATM 1335
1.00 29.99
ANISOU 1335
HETATM 1336
28.285 -13.284 -17.552
1.00 42.03
ANISOU 1336
HETATM 1337
3.324 -26.984
1.00 61.56
ANISOU 1337
HETATM 1338
1.00 36.15
ANISOU 1338
HETATM 1339
28.521 -17.028
1.00 38.71
ANISOU 1339
HETATM 1340
18.643 -13.195
1.00 32.81
ANISOU 1340
HETATM 1341
1.00 38.48
ANISOU 1341
HETATM 1342
6.464 -13.693
1.00 28.72
ANISOU 1342
HETATM 1343
26.444 -10.161 -16.245
1.00 43.99
ANISOU 1343
HETATM 1344
1.00 50.95
ANISOU 1344
HETATM 1345
21.289 -21.143
1.00 39.62
ANISOU 1345
HETATM 1346
1.00 31.44
ANISOU 1346
HETATM 1347
1.00 37.76
ANISOU 1347
HETATM 1348
1.00 39.04
ANISOU 1348
HETATM 1349
4.570 -14.038
1.00 42.01
ANISOU 1349
HETATM 1350
16.175 -10.986
1.00 38.44
ANISOU 1350
HETATM 1351
24.611 -15.800 -10.207
1.00 33.17
ANISOU 1351
HETATM 1352
1.00 44.60
ANISOU 1352
HETATM 1353
1.00 49.05
ANISOU 1353
HETATM 1354
4.639 -22.428
1.00 44.17
ANISOU 1354
HETATM 1355
5.419 -10.180
1.00 55.67
ANISOU 1355
HETATM 1356
1.00 45.47
ANISOU 1356
HETATM 1357
-0.809 -17.596
1.00 45.27
ANISOU 1357
HETATM 1358
1.00 53.94
ANISOU 1358
HETATM 1359
28.211 -10.614
1.00 38.28
ANISOU 1359
HETATM 1360
1.00 42.45
ANISOU 1360
HETATM 1361
42.686 -10.998
1.00 32.90
ANISOU 1361
HETATM 1362
1.00 35.24
ANISOU 1362
HETATM 1363
1.00 35.90
ANISOU 1363
HETATM 1364
1.00 29.75
ANISOU 1364
HETATM 1365
-3.427 -18.199
1.00 46.37
ANISOU 1365
HETATM 1366
1.00 35.34
ANISOU 1366
HETATM 1367
1.00 37.40
ANISOU 1367
HETATM 1368
1.00 41.73
ANISOU 1368
HETATM 1369
1.00 36.06
ANISOU 1369
HETATM 1370
1.00 33.97
ANISOU 1370
HETATM 1371
1.00 34.02
ANISOU 1371
HETATM 1372
-4.712 -21.994
1.00 40.95
ANISOU 1372
HETATM 1373
1.00 39.65
ANISOU 1373
HETATM 1374
1.00 35.73
ANISOU 1374
HETATM 1375
1.00 41.40
ANISOU 1375
HETATM 1376
1.00 42.33
ANISOU 1376
HETATM 1377
18.513 -12.335
1.00 49.69
ANISOU 1377
HETATM 1378
1.00 47.09
ANISOU 1378
HETATM 1379
1.00 58.48
ANISOU 1379
HETATM 1380
1.00 57.51
ANISOU 1380
HETATM 1381
1.00 54.79
ANISOU 1381
HETATM 1382
-9.152 -10.130
1.00 44.33
ANISOU 1382
HETATM 1383
1.00 42.31
ANISOU 1383
HETATM 1384
-8.008 -18.801
1.00 49.03
ANISOU 1384
HETATM 1385
5.533 -18.086
1.00 41.96
ANISOU 1385
HETATM 1386
2.709 -17.487
1.00 52.00
ANISOU 1386
HETATM 1387
42.341 -11.390 -17.890
1.00 38.69
ANISOU 1387
HETATM 1388
1.00 52.26
ANISOU 1388
HETATM 1389
1.00 38.93
ANISOU 1389
HETATM 1390
25.179 -20.905
1.00 35.04
ANISOU 1390
HETATM 1391
22.740 -13.665 -11.061
1.00 45.56
ANISOU 1391
HETATM 1392
1.00 44.46
ANISOU 1392
HETATM 1393
1.00 41.67
ANISOU 1393
HETATM 1394
1.00 52.45
ANISOU 1394
HETATM 1395
1.00 43.79
ANISOU 1395
HETATM 1396
1.00 41.27
ANISOU 1396
HETATM 1397
1.00 54.76
ANISOU 1397
HETATM 1398
36.848 -10.105 -20.521
1.00 46.24
ANISOU 1398
HETATM 1399
1.00 45.39
ANISOU 1399
HETATM 1400
-5.117 -23.200
1.00 43.46
ANISOU 1400
HETATM 1401
21.849 -16.093
1.00 33.58
ANISOU 1401
HETATM 1402
1.00 49.95
ANISOU 1402
HETATM 1403
1.00 35.86
ANISOU 1403
HETATM 1404
1.00 48.72
ANISOU 1404
HETATM 1405
1.00 58.25
ANISOU 1405
HETATM 1406
1.00 48.60
ANISOU 1406
HETATM 1407
1.00 50.84
ANISOU 1407
HETATM 1408
15.985 -14.285
1.00 57.33
ANISOU 1408
HETATM 1409
-2.952 -24.659
1.00 52.24
ANISOU 1409
HETATM 1410
1.00 36.45
ANISOU 1410
HETATM 1411
3.835 -14.474
1.00 40.84
ANISOU 1411
HETATM 1412
1.00 58.73
ANISOU 1412
HETATM 1413
1.00 45.94
ANISOU 1413
HETATM 1414
1.00 36.35
ANISOU 1414
HETATM 1415
1.00 51.77
ANISOU 1415
HETATM 1416
1.00 49.26
ANISOU 1416
HETATM 1417
1.00 36.43
ANISOU 1417
HETATM 1418
39.966 -12.444
1.00 36.00
ANISOU 1418
HETATM 1419
1.00 46.30
ANISOU 1419
HETATM 1420
1.00 43.90
ANISOU 1420
HETATM 1421
20.127 -15.555
1.00 44.65
ANISOU 1421
HETATM 1422
1.00 47.72
ANISOU 1422
HETATM 1423
38.846 -11.303
1.00 60.70
ANISOU 1423}
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