你会解吗?_( )+( )+( )=30_把下面的数字填到框里_(1,3,5,7,9,11,13_百度知道
你会解吗?_( )+( )+( )=30_把下面的数字填到框里_(1,3,5,7,9,11,13
我有更好的答案
3+52/3=90/3）加起来就是4/3+34&#47。这不就刚好等于30怎么会是无解，你用分数不就好了。1（1/3）+11（1/3）+13（13/3
采纳率：100%
曾经看到过，好像是无解，三个任何奇数的和都是奇数。当然了如果括号里面可以天两个的话就另当别论了，
本回答被网友采纳
可以用阶乘么？3！+11+13=30
答案太简单了，最后一行的提示&提示以上数字可以重复使用&，以上数字包括有2.30.1.3.5.7.9.11.13.15答案就是2+13+15=30
图片上面有一个“只有百分之2的人会解”而且它说的是把数字填进去你把2填进去就对了
就当作选择题或脑筋急转弯做吧！说了可以重复使用，但没说不可以怎么样？所以有解。
很简单这题坑人的，因为以上都是奇数，奇数加奇数等于偶数，偶数加奇数永远不可能偶数，等于偶数所以这题无解，但是如果非要答案我告诉你是你把以下数字的9到过来就成6了，有6就有解了。奇数+奇数=偶数，偶数+奇数=奇数
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我们会通过消息、邮箱等方式尽快将举报结果通知您。OXIDOREDUCTASE/ELECTRON TRANSPORT
CRYSTAL STRUCTURE OF CYTOCHROME P450CAM-PUTIDAREDOXIN COMPLEX
MOL_ID: 1;
2 MOLECULE: CAMPHOR 5-MONOOXYGENASE;
3 CHAIN: A, B;
4 SYNONYM: CYTOCHROME P450-CAM, CYTOCHROME P450CAM;
5 EC: 1.14.15.1;
6 ENGINEERED: YES;
7 MUTATION: YES;
8 MOL_ID: 2;
9 MOLECULE: PUTIDAREDOXIN;
10 CHAIN: C, D;
11 SYNONYM: PDX;
12 ENGINEERED: YES
MOL_ID: 1;
2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
3 ORGANISM_TAXID: 303;
4 GENE: CAMC, CYP101;
5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
6 EXPRESSION_SYSTEM_TAXID: 469008;
7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
9 EXPRESSION_SYSTEM_PLASMID: PET15B;
10 MOL_ID: 2;
11 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
12 ORGANISM_TAXID: 303;
13 GENE: CAMB;
14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
15 EXPRESSION_SYSTEM_TAXID: 469008;
16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
18 EXPRESSION_SYSTEM_PLASMID: PET28A
P450CAM-PDX COMPLEX, REDOX PARTNERS, OXIDOREDUCTASE-ELECTRON
2 TRANSPORT COMPLEX
X-RAY DIFFRACTION
S.M.TRIPATHI,H.LI,T.L.POULOS
19-JUN-13 4JWS
S.TRIPATHI,H.LI,T.L.POULOS
STRUCTURAL BASIS FOR EFFECTOR CONTROL AND REDOX PARTNER
TITL 2 RECOGNITION IN CYTOCHROME P450.
10.1126/SCIENCE.1235797
2 RESOLUTION.
2.15 ANGSTROMS.
3 REFINEMENT.
: PHENIX (PHENIX.REFINE: 1.8.2_1309)
: 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) : 2.15
RESOLUTION RANGE LOW
(ANGSTROMS) : 54.80
MIN(FOBS/SIGMA_FOBS)
COMPLETENESS FOR RANGE
(%) : 99.8
NUMBER OF REFLECTIONS
FIT TO DATA USED IN REFINEMENT.
(WORKING + TEST SET) : 0.178
(WORKING SET) : 0.175
FREE R VALUE
FREE R VALUE TEST SET SIZE
(%) : 5.010
FREE R VALUE TEST SET COUNT
FIT TO DATA USED IN REFINEMENT (IN BINS).
RESOLUTION RANGE
NWORK NFREE
1 54.8171 -
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) : 24.360
FROM WILSON PLOT
(A**2) : NULL
MEAN B VALUE
(OVERALL, A**2) : NULL
OVERALL ANISOTROPIC B VALUE.
B11 (A**2) : NULL
B22 (A**2) : NULL
B33 (A**2) : NULL
B12 (A**2) : NULL
B13 (A**2) : NULL
B23 (A**2) : NULL
TWINNING INFORMATION.
FRACTION: NULL
OPERATOR: NULL
DEVIATIONS FROM IDEAL VALUES.
CHIRALITY :
PLANARITY :
TLS DETAILS
NUMBER OF TLS GROUPS
TLS GROUP : 1
SELECTION: (chain A and resid 10:414)
ORIGIN FOR THE GROUP (A):
0.1990 T22:
0.3708 T12:
0.0347 T23:
1.9045 L22:
2.5507 L12:
0.4411 L23:
0.0329 S12:
-0.0045 S13:
-0.2045 S22:
-0.0028 S23:
0.2316 S32:
-0.0401 S33:
TLS GROUP : 2
SELECTION: (chain B and resid 10:414)
ORIGIN FOR THE GROUP (A):
0.4375 T22:
0.2803 T12:
-0.0667 T23:
2.3918 L22:
1.7380 L12:
-0.8132 L23:
0.1992 S12:
0.0446 S13:
0.2591 S22:
-0.0007 S23:
0.0613 S32:
-0.1156 S33:
TLS GROUP : 3
SELECTION: (chain C and resid 1:106)
ORIGIN FOR THE GROUP (A):
0.3661 T22:
0.6318 T12:
0.0259 T23:
7.3420 L22:
4.8362 L12:
-1.0045 L23:
-0.0864 S12:
-0.2987 S13:
0.1045 S22:
0.0904 S23:
-0.4322 S32:
-0.3565 S33:
TLS GROUP : 4
SELECTION: (chain D and resid 1:106)
ORIGIN FOR THE GROUP (A):
0.8789 T22:
0.4170 T12:
-0.2230 T23:
3.2596 L22:
5.5267 L12:
1.3614 L23:
0.1166 S12:
-0.2187 S13:
0.0487 S22:
0.0470 S23:
0.8845 S32:
0.3210 S33:
NCS DETAILS
NUMBER OF NCS GROUPS : 2
NCS GROUP : 1
NCS GROUP : 2
NCS OPERATOR : 1
REFERENCE SELECTION: NULL
ATOM PAIRS NUMBER
OTHER REFINEMENT REMARKS: NULL
4 4JWS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB078602.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200
EXPERIMENT TYPE
: X-RAY DIFFRACTION
REMARK 200
DATE OF DATA COLLECTION
: 14-SEP-12
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) : 1.02
REMARK 200
MONOCHROMATOR
: DOUBLE CRYSTAL SI(111)
REMARK 200
REMARK 200
REMARK 200
DETECTOR TYPE
REMARK 200
DETECTOR MANUFACTURER
: ADSC QUANTUM 315R
REMARK 200
INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200
DATA SCALING SOFTWARE
REMARK 200
REMARK 200
NUMBER OF UNIQUE REFLECTIONS
REMARK 200
RESOLUTION RANGE HIGH
(A) : 2.150
REMARK 200
RESOLUTION RANGE LOW
(A) : 54.800
REMARK 200
REJECTION CRITERIA
(SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200
COMPLETENESS FOR RANGE
(%) : 100.0
REMARK 200
DATA REDUNDANCY
REMARK 200
(I) : 0.10300
REMARK 200
(I) : 0.10300
REMARK 200
FOR THE DATA SET
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200
HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200
HIGHEST RESOLUTION SHELL, RANGE LOW
(A) : 2.27
REMARK 200
COMPLETENESS FOR SHELL
(%) : 100.0
REMARK 200
DATA REDUNDANCY IN SHELL
REMARK 200
R MERGE FOR SHELL
(I) : 0.79200
REMARK 200
R SYM FOR SHELL
(I) : 0.79200
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 ENTRIES 2CPP AND 1XLO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS
(%): 44.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE HYDRATE, 14-22%
REMARK 280
PEG3350, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290
REMARK 290
REMARK 290
REMARK 290
-X,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350
1...000000
REMARK 350
0...000000
REMARK 350
0...000000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470
M RES CSSEQI
REMARK 470
REMARK 470
REMARK 470
REMARK 470
REMARK 470
REMARK 470
REMARK 470
REMARK 470
REMARK 470
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500
M RES CSSEQI ATM1
REMARK 500
ANGL. DEV. =
11.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500
M RES CSSEQI
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:
M RES CSSEQI METAL
REMARK 620
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C
REMARK 620 2 FES C 201
REMARK 620 3 FES C 201
115.4 101.1
REMARK 620 4 CYS C
106.4 111.5 113.9
REMARK 620 N
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:
M RES CSSEQI METAL
REMARK 620
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D
REMARK 620 2 FES D 201
REMARK 620 3 FES D 201
REMARK 620 4 CYS D
121.8 103.3 106.9
REMARK 620 N
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:
M RES CSSEQI METAL
REMARK 620
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C
REMARK 620 2 FES C 201
REMARK 620 3 FES C 201
111.5 100.2
REMARK 620 4 CYS C
109.9 117.6 107.9
REMARK 620 N
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:
M RES CSSEQI METAL
REMARK 620
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D
REMARK 620 2 FES D 201
REMARK 620 3 FES D 201
REMARK 620 4 CYS D
108.2 109.6 113.5
REMARK 620 N
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:
M RES CSSEQI METAL
REMARK 620
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 198
REMARK 620 2 ASP A 202
REMARK 620 3 ASP A 202
REMARK 620 4 ALA B
REMARK 620 N
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:
M RES CSSEQI METAL
REMARK 620
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 357
REMARK 620 2 HEM A 501
REMARK 620 3 HEM A 501
REMARK 620 4 HEM A 501
90.7 166.5
REMARK 620 5 HEM A 501
91.8 167.1
REMARK 620 6 HOH A 701
REMARK 620 N
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:
M RES CSSEQI METAL
REMARK 620
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 357
REMARK 620 2 HEM B 501
REMARK 620 3 HEM B 501
REMARK 620 4 HEM B 501
91.5 164.6
REMARK 620 5 HEM B 501
89.3 167.2
REMARK 620 N
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:
M RES CSSEQI METAL
REMARK 620
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 198
REMARK 620 2 ASP B 202
REMARK 620 3 ASP B 202
REMARK 620 N
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1N0 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1N0 B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES D 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JWU
RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF OXIDIZED CYTOCHROME P450CAM-
REMARK 900 PUTIDAREDOXIN COMPLEX
REMARK 900 RELATED ID: 4JX1
RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF REDUCED CYTOCHROME P450CAM-
REMARK 900 PUTIDAREDOXIN COMPLEX BOUND TO CAMPHOR AND 5-EXO-
REMARK 900 HYDROXYCAMPHOR
CPXA_PSEPU
CPXA_PSEPU
PUTX_PSEPU
PUTX_PSEPU
SEQADV 4JWS SER A
59 ENGINEERED MUTATION
SEQADV 4JWS SER A
86 ENGINEERED MUTATION
SEQADV 4JWS SER A
137 ENGINEERED MUTATION
SEQADV 4JWS SER A
286 ENGINEERED MUTATION
SEQADV 4JWS ALA A
335 ENGINEERED MUTATION
SEQADV 4JWS CYS A
345 ENGINEERED MUTATION
SEQADV 4JWS SER B
59 ENGINEERED MUTATION
SEQADV 4JWS SER B
86 ENGINEERED MUTATION
SEQADV 4JWS SER B
137 ENGINEERED MUTATION
SEQADV 4JWS SER B
286 ENGINEERED MUTATION
SEQADV 4JWS ALA B
335 ENGINEERED MUTATION
SEQADV 4JWS CYS B
345 ENGINEERED MUTATION
SEQADV 4JWS HIS C
EXPRESSION TAG
SEQADV 4JWS HIS C
EXPRESSION TAG
SEQADV 4JWS HIS C
EXPRESSION TAG
SEQADV 4JWS HIS C
EXPRESSION TAG
SEQADV 4JWS HIS C
EXPRESSION TAG
SEQADV 4JWS HIS C
EXPRESSION TAG
SEQADV 4JWS HIS D
EXPRESSION TAG
SEQADV 4JWS HIS D
EXPRESSION TAG
SEQADV 4JWS HIS D
EXPRESSION TAG
SEQADV 4JWS HIS D
EXPRESSION TAG
SEQADV 4JWS HIS D
EXPRESSION TAG
SEQADV 4JWS HIS D
EXPRESSION TAG
MET THR THR GLU THR ILE GLN SER ASN ALA ASN LEU ALA
PRO LEU PRO PRO HIS VAL PRO GLU HIS LEU VAL PHE ASP
PHE ASP MET TYR ASN PRO SER ASN LEU SER ALA GLY VAL
GLN GLU ALA TRP ALA VAL LEU GLN GLU SER ASN VAL PRO
ASP LEU VAL TRP THR ARG SER ASN GLY GLY HIS TRP ILE
ALA THR ARG GLY GLN LEU ILE ARG GLU ALA TYR GLU ASP
TYR ARG HIS PHE SER SER GLU SER PRO PHE ILE PRO ARG
GLU ALA GLY GLU ALA TYR ASP PHE ILE PRO THR SER MET
ASP PRO PRO GLU GLN ARG GLN PHE ARG ALA LEU ALA ASN
GLN VAL VAL GLY MET PRO VAL VAL ASP LYS LEU GLU ASN
ARG ILE GLN GLU LEU ALA SER SER LEU ILE GLU SER LEU
ARG PRO GLN GLY GLN CYS ASN PHE THR GLU ASP TYR ALA
GLU PRO PHE PRO ILE ARG ILE PHE MET LEU LEU ALA GLY
LEU PRO GLU GLU ASP ILE PRO HIS LEU LYS TYR LEU THR
ASP GLN MET THR ARG PRO ASP GLY SER MET THR PHE ALA
GLU ALA LYS GLU ALA LEU TYR ASP TYR LEU ILE PRO ILE
ILE GLU GLN ARG ARG GLN LYS PRO GLY THR ASP ALA ILE
SER ILE VAL ALA ASN GLY GLN VAL ASN GLY ARG PRO ILE
THR SER ASP GLU ALA LYS ARG MET CYS GLY LEU LEU LEU
VAL GLY GLY LEU ASP THR VAL VAL ASN PHE LEU SER PHE
SER MET GLU PHE LEU ALA LYS SER PRO GLU HIS ARG GLN
GLU LEU ILE GLU ARG PRO GLU ARG ILE PRO ALA ALA SER
GLU GLU LEU LEU ARG ARG PHE SER LEU VAL ALA ASP GLY
ARG ILE LEU THR SER ASP TYR GLU PHE HIS GLY VAL GLN
LEU LYS LYS GLY ASP GLN ILE LEU LEU PRO GLN MET LEU
SER GLY LEU ASP GLU ARG GLU ASN ALA ALA PRO MET HIS
VAL ASP PHE SER ARG GLN CYS VAL SER HIS THR THR PHE
GLY HIS GLY SER HIS LEU CYS LEU GLY GLN HIS LEU ALA
ARG ARG GLU ILE ILE VAL THR LEU LYS GLU TRP LEU THR
ARG ILE PRO ASP PHE SER ILE ALA PRO GLY ALA GLN ILE
GLN HIS LYS SER GLY ILE VAL SER GLY VAL GLN ALA LEU
PRO LEU VAL TRP ASP PRO ALA THR THR LYS ALA VAL
MET THR THR GLU THR ILE GLN SER ASN ALA ASN LEU ALA
PRO LEU PRO PRO HIS VAL PRO GLU HIS LEU VAL PHE ASP
PHE ASP MET TYR ASN PRO SER ASN LEU SER ALA GLY VAL
GLN GLU ALA TRP ALA VAL LEU GLN GLU SER ASN VAL PRO
ASP LEU VAL TRP THR ARG SER ASN GLY GLY HIS TRP ILE
ALA THR ARG GLY GLN LEU ILE ARG GLU ALA TYR GLU ASP
TYR ARG HIS PHE SER SER GLU SER PRO PHE ILE PRO ARG
GLU ALA GLY GLU ALA TYR ASP PHE ILE PRO THR SER MET
ASP PRO PRO GLU GLN ARG GLN PHE ARG ALA LEU ALA ASN
GLN VAL VAL GLY MET PRO VAL VAL ASP LYS LEU GLU ASN
ARG ILE GLN GLU LEU ALA SER SER LEU ILE GLU SER LEU
ARG PRO GLN GLY GLN CYS ASN PHE THR GLU ASP TYR ALA
GLU PRO PHE PRO ILE ARG ILE PHE MET LEU LEU ALA GLY
LEU PRO GLU GLU ASP ILE PRO HIS LEU LYS TYR LEU THR
ASP GLN MET THR ARG PRO ASP GLY SER MET THR PHE ALA
GLU ALA LYS GLU ALA LEU TYR ASP TYR LEU ILE PRO ILE
ILE GLU GLN ARG ARG GLN LYS PRO GLY THR ASP ALA ILE
SER ILE VAL ALA ASN GLY GLN VAL ASN GLY ARG PRO ILE
THR SER ASP GLU ALA LYS ARG MET CYS GLY LEU LEU LEU
VAL GLY GLY LEU ASP THR VAL VAL ASN PHE LEU SER PHE
SER MET GLU PHE LEU ALA LYS SER PRO GLU HIS ARG GLN
GLU LEU ILE GLU ARG PRO GLU ARG ILE PRO ALA ALA SER
GLU GLU LEU LEU ARG ARG PHE SER LEU VAL ALA ASP GLY
ARG ILE LEU THR SER ASP TYR GLU PHE HIS GLY VAL GLN
LEU LYS LYS GLY ASP GLN ILE LEU LEU PRO GLN MET LEU
SER GLY LEU ASP GLU ARG GLU ASN ALA ALA PRO MET HIS
VAL ASP PHE SER ARG GLN CYS VAL SER HIS THR THR PHE
GLY HIS GLY SER HIS LEU CYS LEU GLY GLN HIS LEU ALA
ARG ARG GLU ILE ILE VAL THR LEU LYS GLU TRP LEU THR
ARG ILE PRO ASP PHE SER ILE ALA PRO GLY ALA GLN ILE
GLN HIS LYS SER GLY ILE VAL SER GLY VAL GLN ALA LEU
PRO LEU VAL TRP ASP PRO ALA THR THR LYS ALA VAL
HIS HIS HIS HIS HIS HIS SER LYS VAL VAL TYR VAL SER
HIS ASP GLY THR ARG ARG GLU LEU ASP VAL ALA ASP GLY
VAL SER LEU MET GLN ALA ALA VAL SER ASN GLY ILE TYR
ASP ILE VAL GLY ASP CYS GLY GLY SER ALA SER CYS ALA
THR CYS HIS VAL TYR VAL ASN GLU ALA PHE THR ASP LYS
VAL PRO ALA ALA ASN GLU ARG GLU ILE GLY MET LEU GLU
CYS VAL THR ALA GLU LEU LYS PRO ASN SER ARG LEU CYS
CYS GLN ILE ILE MET THR PRO GLU LEU ASP GLY ILE VAL
VAL ASP VAL PRO ASP ARG GLN TRP
HIS HIS HIS HIS HIS HIS SER LYS VAL VAL TYR VAL SER
HIS ASP GLY THR ARG ARG GLU LEU ASP VAL ALA ASP GLY
VAL SER LEU MET GLN ALA ALA VAL SER ASN GLY ILE TYR
ASP ILE VAL GLY ASP CYS GLY GLY SER ALA SER CYS ALA
THR CYS HIS VAL TYR VAL ASN GLU ALA PHE THR ASP LYS
VAL PRO ALA ALA ASN GLU ARG GLU ILE GLY MET LEU GLU
CYS VAL THR ALA GLU LEU LYS PRO ASN SER ARG LEU CYS
CYS GLN ILE ILE MET THR PRO GLU LEU ASP GLY ILE VAL
VAL ASP VAL PRO ASP ARG GLN TRP
HEM PROTOPORPHYRIN IX CONTAINING FE
CA CALCIUM ION
1N0 1,1'-HEXANE-1,6-DIYLDIPYRROLIDINE-2,5-DIONE
FES FE2/S2 (INORGANIC) CLUSTER
1N0 BIS(MALEIMIDO)HEXANE, BOUND FORM
2(C34 H32 FE N4 O4)
2(C14 H20 N2 O4)
*231(H2 O)
A 5 GLN A 317
A 5 GLY A 298
LEU A 301 -1
B 3 GLN A 147
B 3 PRO A 403
VAL A 405 -1
B 3 SER A 382
ILE A 383 -1
C 2 GLN A 227
C 2 ARG A 231
PRO A 232 -1
D 2 TYR A 305
D 2 VAL A 310
LEU A 312 -1
E 2 HIS A 391
E 2 GLY A 398
VAL A 399 -1
F 5 GLN B 317
F 5 GLY B 298
LEU B 301 -1
G 3 GLN B 147
G 3 PRO B 403
VAL B 405 -1
G 3 SER B 382
ILE B 383 -1
H 2 GLN B 227
H 2 ARG B 231
PRO B 232 -1
I 2 TYR B 305
I 2 VAL B 310
LEU B 312 -1
J 2 HIS B 391
J 2 GLY B 398
VAL B 399 -1
NE2 HIS A 355
NE2 HIS B 355
C16 1N0 A 503
C16 1N0 B 503
OE2 GLU A 198
OE2 GLU B 198
OD2 ASP A 202
OD1 ASP A 202
OD1 ASP B 202
OD2 ASP B 202
1 AC1 18 GLN A 108
2 AC1 18 GLY A 249
3 AC1 18 ARG A 299
4 AC1 18 GLY A 351
5 AC1 18 HOH A 602
3 GLU A 198
7 HIS A 355
1 AC4 19 GLN B 108
2 AC4 19 GLY B 249
3 AC4 19 ASP B 297
4 AC4 19 PHE B 350
5 AC4 19 ALA B 363
6 GLU B 198
7 HIS B 355
90.00 107.91
90.00 P 1 21 1
1...000000
0...000000
0...000000
0...005612
0...000000
0...011848
37.216 -17.045
1.00 98.23
37.557 -16.534
1.00 99.58
37.490 -15.001
1.00 93.28
36.637 -14.433
1.00 86.99
36.622 -17.142
1.00101.16
37.138 -16.965
1.00105.60
38.342 -16.818
1.00106.96
36.223 -16.964
1.00105.96
38.376 -14.337
1.00 85.49
38.238 -12.900
1.00 70.74
39.258 -12.007
1.00 70.02
40.442 -12.349
1.00 70.53
38.287 -12.631
1.00 64.97
37.182 -13.345
1.00 70.44
37.083 -12.800
1.00 68.94
35.829 -13.225
1.00 70.46
38.793 -10.821
1.00 57.69
1.00 51.73
1.00 52.79
1.00 50.50
1.00 37.15
1.00 54.08
1.00 52.75
1.00 48.42
1.00 53.41
1.00 51.02
1.00 58.13
1.00 60.00
1.00 53.92
1.00 45.69
1.00 55.23
1.00 70.91
1.00 49.10
1.00 54.87
1.00 48.88
1.00 50.97
1.00 55.06
1.00 43.24
1.00 44.92
1.00 51.98
1.00 43.33
1.00 44.62
1.00 50.61
1.00 49.14
1.00 53.36
1.00 52.47
1.00 54.49
1.00 57.02
1.00 58.73
1.00 54.22
1.00 46.27
1.00 53.82
1.00 50.62
1.00 53.43
1.00 44.56
1.00 45.84
1.00 44.10
1.00 49.83
1.00 48.14
1.00 43.80
1.00 44.82
1.00 43.15
1.00 45.43
1.00 43.44
1.00 38.87
1.00 39.13
1.00 37.50
1.00 45.30
1.00 51.59
1.00 55.01
1.00 55.23
1.00 51.91
1.00 53.13
1.00 48.83
1.00 55.29
1.00 50.46
1.00 42.36
1.00 44.98
1.00 67.77
1.00 84.71
1.00 99.20
1.00102.49
1.00106.20
1.00 42.90
1.00 41.94
1.00 39.34
1.00 38.40
1.00 58.90
1.00 59.82
1.00 65.31
1.00 56.56
1.00 56.27
1.00 56.46
1.00 38.32
1.00 35.98
1.00 34.75
1.00 32.97
1.00 39.83
1.00 40.08
1.00 37.44
1.00 37.25
1.00 35.89
1.00 36.13
1.00 39.40
1.00 39.74
1.00 39.20
1.00 44.03
1.00 37.95
1.00 32.64
1.00 31.82
1.00 41.73
1.00 48.60
1.00 40.86
1.00 44.94
1.00 49.38
1.00 47.96
1.00 47.33
1.00 47.29
1.00 37.06
1.00 44.80
1.00 54.00
30.489 -10.331
1.00 49.06
29.686 -10.930
1.00 49.77
32.365 -10.970
1.00 62.65
32.780 -12.267
1.00 75.51
32.883 -12.279
1.00 77.79
33.020 -13.272
1.00 81.58
1.00 34.13
28.865 -10.314
1.00 33.58
29.008 -10.867
1.00 35.23
29.594 -10.220
1.00 26.86
1.00 26.56
1.00 28.82
25.615 -10.049
1.00 30.63
1.00 31.41
24.298 -10.408
1.00 34.45
1.00 27.73
23.781 -10.203
1.00 30.88
28.510 -12.081
1.00 32.38
28.510 -12.704
1.00 30.96
27.078 -12.798
1.00 33.37
26.347 -13.656
1.00 30.90
29.154 -14.091
1.00 40.10
29.196 -14.779
1.00 43.44
28.637 -14.266
1.00 40.18
29.795 -15.871
1.00 53.34
26.674 -11.927
1.00 24.70
25.265 -11.855
1.00 30.29
24.748 -13.128
1.00 31.20
23.543 -13.269
1.00 30.21
25.049 -10.694
1.00 24.38
25.944 -10.794
1.00 34.35
1.00 39.62
1.00 28.27
25.656 -14.032
1.00 33.29
25.259 -15.309
1.00 33.79
25.241 -16.424
1.00 33.92
24.722 -17.498
1.00 39.89
26.183 -15.698
1.00 32.29
26.023 -14.735
1.00 32.82
24.889 -14.783
1.00 43.63
26.983 -13.767
1.00 31.94
24.695 -13.890
1.00 41.40
26.800 -12.850
1.00 33.58
25.654 -12.933
1.00 41.18
25.448 -12.040
1.00 36.80
25.801 -16.171
1.00 33.95
25.814 -17.185
1.00 33.93
25.920 -16.589
1.00 35.15
26.904 -16.805
1.00 36.08
26.946 -18.182
1.00 33.11
26.837 -19.391
1.00 49.89
25.728 -19.877
1.00 59.20
27.976 -19.894
1.00 50.78
24.909 -15.810
1.00 32.53
25.062 -15.112
1.00 31.21
24.941 -16.043
1.00 36.86
24.206 -17.030
1.00 41.33
23.918 -14.088
1.00 29.49
22.883 -14.679
1.00 33.59
23.639 -15.496
1.00 31.31
25.639 -15.713
1.00 40.30
25.784 -16.616
1.00 45.66
24.437 -17.117
1.00 49.70
24.299 -18.310
1.00 58.26
26.614 -15.954
1.00 53.23
25.964 -14.825
1.00 63.87
23.458 -16.238
1.00 44.12
22.238 -16.688
1.00 44.78
21.072 -17.067
1.00 46.51
19.887 -16.866
1.00 45.68
21.731 -15.602
1.00 46.13
22.695 -15.312
1.00 52.60
23.645 -16.064
1.00 55.80
22.425 -14.257
1.00 56.45
21.402 -17.647
1.00 37.37
20.409 -17.945
1.00 42.09
19.271 -18.861
1.00 38.76
18.117 -18.757
1.00 42.94
21.114 -18.569
1.00 39.56
20.282 -18.849
1.00 42.56
19.570 -17.569
1.00 37.81
21.177 -19.417
1.00 42.15
19.573 -19.715
1.00 34.56
18.565 -20.662
1.00 42.99
17.469 -19.995
1.00 36.85
16.419 -20.591
1.00 39.12
19.216 -21.783
1.00 52.81
19.726 -21.250
1.00 66.02
17.684 -18.773
1.00 33.57
16.560 -18.100
1.00 41.33
15.627 -17.499
1.00 40.25
14.575 -16.977
1.00 40.51
17.042 -17.021
1.00 36.22
16.032 -17.543
1.00 39.46
15.261 -16.902
1.00 39.57
16.109 -15.828
1.00 33.61
16.989 -15.245
1.00 31.03
15.905 -15.580
1.00 30.71
16.876 -14.758
1.00 31.46
16.735 -13.275
1.00 30.85
17.730 -12.586
1.00 32.11
16.773 -14.924
1.00 36.65
15.387 -14.559
1.00 40.45
17.862 -14.092
1.00 33.49
15.518 -12.795
1.00 27.38
15.360 -11.409
1.00 30.57
16.065 -11.215
1.00 32.57
16.753 -10.211
1.00 29.66
13.868 -11.028
1.00 35.34
13.201 -10.876
1.00 29.88
12.823 -12.229
1.00 30.42
12.734 -13.265
1.00 30.88
12.643 -12.215
1.00 33.88
15.928 -12.199
1.00 32.58
16.616 -12.211
1.00 34.75
18.150 -12.206
1.00 37.71
18.870 -11.503
1.00 29.88
16.192 -13.448
1.00 29.07
14.819 -13.373
1.00 36.17
13.678 -13.734
1.00 53.95
13.938 -13.983
1.00 51.65
12.514 -13.758
1.00 49.03
18.648 -13.000
1.00 34.31
20.080 -13.051
1.00 34.13
20.614 -11.685
1.00 31.85
21.664 -11.260
1.00 40.34
20.417 -14.131
1.00 28.89
19.874 -10.975
1.00 31.14
1.00 25.24
1.00 35.55
1.00 26.92
1.00 27.80
1.00 27.69
19.886 -11.221
1.00 31.60
1.00 27.63
20.469 -11.463
1.00 31.30
20.992 -10.283
1.00 30.39
1.00 27.55
21.685 -10.028
1.00 26.22
1.00 24.46
1.00 26.80
1.00 28.86
1.00 34.23
1.00 34.25
1.00 35.47
1.00 29.70
1.00 34.07
1.00 40.17
1.00 38.74
1.00 36.75
1.00 42.04
22.348 -11.000
1.00 48.41
1.00 39.64
1.00 26.43
1.00 26.24
1.00 30.73
1.00 34.27
1.00 24.93
1.00 31.73
1.00 24.84
1.00 35.27
1.00 27.06
1.00 37.72
1.00 33.79
1.00 38.07
1.00 29.11
1.00 32.80
1.00 32.44
1.00 36.72
1.00 28.96
1.00 38.62
1.00 38.50
1.00 45.80
1.00 36.48
1.00 44.98
1.00 57.31
1.00 72.97
1.00 80.28
1.00 79.05
1.00 54.16
1.00 59.18
1.00 63.59
1.00 74.86
1.00 57.62
1.00 67.87
1.00 38.91
1.00 52.30
1.00 53.72
1.00 54.72
1.00 49.20
1.00 54.18
1.00 63.69
1.00 55.48
1.00 47.47
1.00 39.33
1.00 35.17
1.00 41.99
1.00 32.77
1.00 33.28
1.00 36.91
1.00 35.86
1.00 38.62
1.00 36.62
1.00 34.24
1.00 39.04
1.00 44.32
1.00 39.11
1.00 33.66
1.00 34.23
1.00 34.66
1.00 30.81
1.00 38.99
1.00 51.26
1.00 48.70
1.00 53.92
1.00 29.72
1.00 33.04
1.00 33.53
1.00 30.92
1.00 34.81
1.00 40.06
1.00 32.83
1.00 36.96
1.00 32.46
1.00 31.22
1.00 28.85
1.00 32.42
1.00 30.50
1.00 29.41
1.00 27.18
1.00 29.97
1.00 30.09
1.00 35.96
1.00 31.16
1.00 31.86
1.00 35.81
1.00 35.05
1.00 36.69
1.00 36.87
1.00 37.89
1.00 31.60
1.00 39.39
1.00 43.17
1.00 41.36
1.00 30.50
1.00 30.65
1.00 37.75
1.00 36.15
1.00 28.18
1.00 28.80
1.00 26.91
1.00 33.35
1.00 39.57
1.00 39.88
1.00 39.02
1.00 37.41
1.00 39.83
1.00 38.17
1.00 51.42
1.00 57.44
1.00 47.75
1.00 55.52
1.00 32.29
33.394 -11.023
1.00 37.46
33.052 -10.572
1.00 37.73
1.00 31.57
32.134 -11.587
1.00 37.72
32.483 -12.264
1.00 47.08
32.950 -11.563
1.00 34.80
32.548 -11.376
1.00 41.76
33.242 -10.218
1.00 34.18
1.00 39.72
31.023 -11.197
1.00 29.86
30.309 -12.368
1.00 39.19
30.391 -13.487
1.00 36.07
29.633 -12.137
1.00 29.00
34.565 -10.158
1.00 42.27
1.00 45.87
1.00 46.03
1.00 47.71
1.00 43.96
1.00 31.28
1.00 34.64
1.00 30.07
1.00 28.95
1.00 28.09
1.00 28.40
1.00 30.94
1.00 26.58
1.00 25.71
1.00 24.69
1.00 25.91
1.00 24.94
1.00 28.71
1.00 27.27
1.00 30.51
1.00 27.82
1.00 25.75
1.00 26.93
1.00 28.62
1.00 37.91
1.00 30.03
1.00 31.24
1.00 33.13
1.00 32.06
1.00 33.57
1.00 34.35
1.00 34.59
1.00 25.08
1.00 23.95
1.00 32.61
1.00 29.74
1.00 25.81
1.00 24.07
1.00 22.82
1.00 24.35
1.00 23.47
1.00 27.75
1.00 30.51
1.00 25.11
1.00 23.70
1.00 28.93
1.00 29.64
1.00 37.69
1.00 33.32
1.00 29.45
1.00 33.56
1.00 28.68
1.00 24.34
1.00 30.35
1.00 32.58
1.00 27.65
1.00 29.09
1.00 31.37
1.00 33.61
1.00 44.33
1.00 46.19
1.00 37.07
1.00 45.88
1.00 32.10
1.00 29.84
1.00 32.64
1.00 32.12
1.00 31.16
1.00 35.73
1.00 41.53
1.00 35.95
1.00 36.72
1.00 49.22
1.00 74.31
1.00 82.36
1.00 86.14
1.00 27.51
1.00 27.40
1.00 26.29
1.00 26.97
1.00 31.73
1.00 33.25
1.00 35.50
1.00 39.34
1.00 28.05
1.00 26.60
1.00 29.36
1.00 28.69
1.00 25.86
1.00 25.22
1.00 26.60
1.00 23.68
1.00 31.59
1.00 32.63
1.00 32.58
1.00 28.28
1.00 29.68
1.00 30.33
1.00 41.71
1.00 49.34
1.00 52.30
1.00 57.75
1.00 45.64
1.00 26.61
1.00 35.48
1.00 37.27
1.00 31.70
1.00 27.46
1.00 45.01
1.00 64.11
1.00 64.06
1.00 65.07
1.00 26.47
1.00 29.68
1.00 33.00
1.00 28.04
1.00 25.59
1.00 29.16
1.00 31.52
1.00 33.36
1.00 34.68
1.00 23.17
1.00 27.37
1.00 24.25
1.00 23.13
1.00 24.57
1.00 25.60
1.00 22.78
1.00 25.02
1.00 32.21
1.00 38.66
1.00 43.54
1.00 38.97
1.00 34.18
1.00 47.45
1.00 54.42
1.00 59.91
1.00 52.11
1.00 43.10
1.00 35.74
1.00 37.77
1.00 41.88
1.00 37.91
1.00 45.48
1.00 45.75
1.00 51.93
1.00 34.35
1.00 36.13
1.00 32.22
1.00 39.04
1.00 44.86
1.00 50.56
1.00 57.26
1.00 58.03
1.00 67.92
1.00 65.96
1.00 71.56
1.00 83.52
1.00 32.98
1.00 36.59
1.00 50.98
1.00 46.05
1.00 53.84
1.00 77.18
1.00 92.38
1.00 94.83
1.00 96.72
1.00100.50
1.00 95.69
1.00 42.46
1.00 42.44
1.00 40.62
1.00 39.61
1.00 49.89
1.00 53.13
1.00 52.59
1.00 53.64
1.00 54.10
1.00 55.72
1.00 33.75
1.00 34.09
1.00 36.23
1.00 29.02
1.00 30.95
1.00 26.19
1.00 25.84
1.00 26.37
1.00 26.63
1.00 31.32
1.00 27.86
1.00 35.78
1.00 38.62
1.00 39.09
1.00 34.09
1.00 39.38
1.00 44.74
1.00 34.84
1.00 36.51
1.00 39.66
1.00 40.32
1.00 40.60
1.00 49.11
1.00 41.55
1.00 51.45
1.00 58.81
1.00 54.50
1.00 62.73
1.00 81.80
1.00 96.62
1.00101.97
1.00100.58
1.00 61.86
1.00 62.19
1.00 59.07
1.00 61.24
1.00 65.19
1.00 70.16
1.00 51.98
1.00 50.14
1.00 48.40
1.00 43.63
1.00 44.08
1.00 48.95
1.00 48.66
1.00 37.24
1.00 51.23
1.00 51.31
1.00 57.05
1.00 63.87
1.00 70.22
1.00 73.64
1.00 74.47
1.00 72.01
1.00 75.85
1.00 71.73
1.00 52.81
1.00 58.70
1.00 55.38
26.834 -10.152
1.00 53.00
1.00 50.85
1.00 46.94
1.00 50.99
1.00 41.71
28.872 -10.092
1.00 56.46
1.00 66.01
1.00 74.53
1.00 67.89
31.165 -10.314
1.00 58.18
30.524 -11.672
1.00 57.85
29.144 -11.540
1.00 55.71
1.00 84.62
1.00 88.81
1.00 82.48
1.00 86.66
1.00 95.30
1.00100.67
1.00107.79
1.00115.30
1.00115.70
1.00115.21
1.00114.66
1.00 83.47
1.00 83.16
1.00 85.83
1.00 83.06
1.00 75.91
1.00 84.41
1.00 74.63
1.00 62.23
1.00 63.48
1.00 83.14
1.00 86.17
1.00 83.28
1.00 79.06
1.00 60.94
1.00 65.08
1.00 63.53
1.00 56.07
1.00 73.42
1.00 85.83
OD1 ASP A 104
1.00 89.60
OD1 ASP A 104
OD2 ASP A 104
1.00 95.74
OD2 ASP A 104
1.00 60.11
1.00 57.00
1.00 55.28
1.00 50.05
1.00 52.69
1.00 47.31
1.00 58.26
1.00 50.06
1.00 56.01
1.00 55.13
1.00 49.29
1.00 60.95
1.00 53.07
1.00 48.58
1.00 47.73
1.00 39.67
1.00 41.43
1.00 35.35
1.00 54.63
1.00 76.26
1.00 88.73
OE1 GLU A 107
1.00 95.98
OE1 GLU A 107
OE2 GLU A 107
1.00 86.73
OE2 GLU A 107
1.00 38.99
1.00 41.44
1.00 37.90
1.00 36.62
1.00 43.06
1.00 54.74
1.00 63.66
OE1 GLN A 108
1.00 77.40
OE1 GLN A 108
NE2 GLN A 108
1.00 49.80
NE2 GLN A 108
1.00 34.99
1.00 40.12
1.00 39.55
1.00 34.71
1.00 37.45
1.00 46.51
1.00 49.34
1.00 61.56
1.00 57.41
NH1 ARG A 109
1.00 42.76
NH1 ARG A 109
NH2 ARG A 109
1.00 68.17
NH2 ARG A 109
1.00 37.85
1.00 40.77
1.00 39.40
1.00 38.12
1.00 42.94
1.00 35.90
1.00 43.84
OE1 GLN A 110
1.00 48.88
OE1 GLN A 110
NE2 GLN A 110
1.00 42.82
NE2 GLN A 110
1.00 35.31
1.00 34.71
1.00 32.22
1.00 34.51
1.00 46.26
1.00 52.09
CD1 PHE A 111
1.00 59.61
CD1 PHE A 111
CD2 PHE A 111
1.00 55.38
CD2 PHE A 111
CE1 PHE A 111
1.00 60.35
CE1 PHE A 111
CE2 PHE A 111
1.00 58.67
CE2 PHE A 111
1.00 58.47
1.00 31.38
1.00 33.14
1.00 33.73
1.00 33.33
1.00 28.53
1.00 45.26
1.00 31.87
1.00 33.96
1.00 32.83
NH1 ARG A 112
1.00 31.95
NH1 ARG A 112
NH2 ARG A 112
1.00 28.91
NH2 ARG A 112
1.00 34.63
1.00 32.34
1.00 32.15
1.00 35.76
1.00 36.05
1.00 35.48
1.00 42.42
1.00 41.02
1.00 39.47
1.00 43.19
1.00 50.09
CD1 LEU A 114
1.00 37.61
CD1 LEU A 114
CD2 LEU A 114
1.00 52.15
CD2 LEU A 114
1.00 40.62
1.00 40.19
1.00 38.55
1.00 35.20
1.00 40.21
1.00 39.11
1.00 30.70
1.00 40.83
1.00 42.13
1.00 31.25
1.00 44.01
OD1 ASN A 116
1.00 40.13
OD1 ASN A 116
ND2 ASN A 116
1.00 47.77
ND2 ASN A 116
1.00 38.86
1.00 42.64
1.00 49.47
1.00 49.94
1.00 47.07
1.00 53.50
1.00 70.01
OE1 GLN A 117
1.00 81.78
OE1 GLN A 117
NE2 GLN A 117
1.00 64.65
NE2 GLN A 117
1.00 41.90
1.00 47.90
1.00 47.57
1.00 47.44
1.00 55.58
CG1 VAL A 118
1.00 54.29
CG1 VAL A 118
CG2 VAL A 118
1.00 66.73
CG2 VAL A 118
1.00 40.25
1.00 34.53
1.00 37.36
1.00 37.38
1.00 41.30
CG1 VAL A 119
1.00 36.04
CG1 VAL A 119
CG2 VAL A 119
1.00 42.60
CG2 VAL A 119
1.00 37.99
1.00 34.73
1.00 42.36
1.00 41.90
1.00 35.82
1.00 34.12
1.00 44.50
1.00 48.67
1.00 34.01
1.00 50.16
1.00 56.98
1.00 72.33
1.00 45.63
1.00 58.16
1.00 56.82
1.00 52.75
1.00 54.06
1.00 53.37
1.00 47.19
1.00 45.23
1.00 45.33
1.00 44.18
1.00 41.80
1.00 45.36
CG1 VAL A 123
1.00 41.10
CG1 VAL A 123
CG2 VAL A 123
1.00 50.68
CG2 VAL A 123
1.00 45.76
1.00 45.30
1.00 46.56
1.00 48.41
1.00 45.21
CG1 VAL A 124
1.00 42.19
CG1 VAL A 124
CG2 VAL A 124
1.00 33.69
CG2 VAL A 124
1.00 40.29
1.00 52.24
1.00 54.18
1.00 58.39
1.00 44.56
1.00 55.83
OD1 ASP A 125
1.00 51.21
OD1 ASP A 125
OD2 ASP A 125
1.00 49.47
OD2 ASP A 125
1.00 50.99
1.00 59.42
1.00 60.12
1.00 56.46
1.00 66.73
1.00 75.68
1.00 79.18
1.00 79.16
1.00 78.22
1.00 54.40
1.00 55.81
1.00 50.30
-6.758 -10.323
1.00 56.32
1.00 62.67
1.00 66.83
CD1 LEU A 127
1.00 72.38
CD1 LEU A 127
CD2 LEU A 127
1.00 71.46
CD2 LEU A 127
1.00 52.41
1.00 60.46
-8.287 -10.196
1.00 57.62
-8.005 -11.177
1.00 52.22
1.00 66.10
1.00 73.02
1.00 78.67
OE1 GLU A 128
1.00 81.97
OE1 GLU A 128
OE2 GLU A 128
1.00 82.77
OE2 GLU A 128
-9.375 -10.149
1.00 61.25
-10.318 -11.257
1.00 62.79
-9.697 -12.531
1.00 57.39
-9.971 -13.617
1.00 60.28
-11.563 -10.918
1.00 62.53
-12.559 -10.112
1.00 73.91
OD1 ASN A 129
-12.721 -10.331
1.00 80.75
OD1 ASN A 129
ND2 ASN A 129
1.00 73.87
ND2 ASN A 129
-8.867 -12.409
1.00 56.30
-8.224 -13.595
1.00 62.27
-7.116 -14.073
1.00 57.49
-6.894 -15.273
1.00 61.26
-7.702 -13.343
1.00 71.58
-8.736 -13.699
1.00 82.20
-8.183 -13.535
1.00 87.14
-7.761 -12.155
1.00 87.34
-7.117 -11.739
1.00 90.25
NH1 ARG A 130
-6.821 -12.595
1.00 94.28
NH1 ARG A 130
NH2 ARG A 130
-6.775 -10.461
1.00 88.08
NH2 ARG A 130
-6.467 -13.155
1.00 58.14
-5.496 -13.543
1.00 50.45
-6.193 -14.315
1.00 54.80
-5.699 -15.347
1.00 51.61
-4.776 -12.329
1.00 51.13
CG1 ILE A 131
-3.789 -11.717
1.00 42.13
CG1 ILE A 131
CG2 ILE A 131
-4.074 -12.747
1.00 44.54
CG2 ILE A 131
CD1 ILE A 131
-3.343 -10.324
1.00 44.90
CD1 ILE A 131
-7.350 -13.801
1.00 49.48
-8.144 -14.427
1.00 51.29
-8.590 -15.848
1.00 65.90
-8.562 -16.766
1.00 69.27
-9.369 -13.568
1.00 56.17
-10.286 -14.158
1.00 72.11
-11.577 -13.369
1.00 86.53
OE1 GLN A 132
-11.933 -12.542
1.00 88.93
OE1 GLN A 132
NE2 GLN A 132
-12.295 -13.635
1.00 90.61
NE2 GLN A 132
-9.019 -16.025
1.00 60.43
-9.435 -17.348
1.00 66.20
-8.250 -18.308
1.00 66.81
-8.370 -19.468
1.00 66.33
-10.086 -17.289
1.00 75.34
-10.023 -18.622
1.00 88.12
-10.750 -19.767
1.00101.14
OE1 GLU A 133
-11.725 -19.500
1.00105.96
OE1 GLU A 133
OE2 GLU A 133
-10.314 -20.934
1.00102.18
OE2 GLU A 133
-7.103 -17.823
1.00 68.47
-5.901 -18.651
1.00 67.23
-5.520 -19.107
1.00 62.15
-5.234 -20.290
1.00 62.52
-4.729 -17.903
1.00 68.00
-3.418 -18.694
1.00 77.16
CD1 LEU A 134
-3.424 -19.934
1.00 75.77
CD1 LEU A 134
CD2 LEU A 134
-2.200 -17.811
1.00 81.35
CD2 LEU A 134
-5.519 -18.165
1.00 64.67
-5.218 -18.480
1.00 59.08
-6.197 -19.535
1.00 59.27
-5.812 -20.455
1.00 56.56
-5.276 -17.239
1.00 48.45
-7.465 -19.378
1.00 60.81
-8.500 -20.301
1.00 68.19
-8.293 -21.688
1.00 68.50
-8.387 -22.696
1.00 69.31
-9.888 -19.768
1.00 74.33
-10.214 -18.630
1.00 74.55
-8.044 -21.718
1.00 72.39
-7.864 -22.958
1.00 76.96
-6.675 -23.743
1.00 76.74
-6.711 -24.969
1.00 76.01
-7.669 -22.636
1.00 77.29
-7.253 -23.761
1.00 80.57
-5.627 -23.016
1.00 75.35
-4.419 -23.605
1.00 67.88
-4.655 -24.212
1.00 69.50
-4.180 -25.312
1.00 65.86
-3.320 -22.546
1.00 63.64
-1.896 -22.958
1.00 69.01
CD1 LEU A 138
-1.876 -24.003
1.00 70.92
CD1 LEU A 138
CD2 LEU A 138
-1.104 -21.717
1.00 67.53
CD2 LEU A 138
-5.363 -23.472
1.00 72.03
-5.627 -23.892
1.00 71.76
-6.643 -25.040
1.00 76.73
-6.546 -25.931
1.00 80.20
-6.109 -22.686
1.00 57.19
CG1 ILE A 139
-4.977 -21.667
1.00 59.06
CG1 ILE A 139
CG2 ILE A 139
-6.538 -23.105
1.00 58.61
CG2 ILE A 139
CD1 ILE A 139
-5.437 -20.279
1.00 61.44
CD1 ILE A 139
-7.625 -25.015
1.00 76.64
-8.655 -26.053
1.00 85.53
-8.074 -27.418
1.00 80.22
-8.482 -28.439
1.00 74.83
-9.801 -25.675
1.00 93.31
-11.094 -26.436
1.00102.62
-11.496 -26.412
1.00101.03
OE1 GLU A 140
-11.414 -25.333
1.00101.81
OE1 GLU A 140
OE2 GLU A 140
-11.906 -27.473
1.00 92.36
OE2 GLU A 140
-7.087 -27.426
1.00 78.06
-6.420 -28.665
1.00 76.20
-5.530 -29.184
1.00 77.68
-5.198 -30.371
1.00 70.55
-5.611 -28.457
1.00 77.30
-4.559 -27.518
1.00 83.84
-5.203 -28.311
1.00 66.47
-4.362 -28.685
1.00 64.82
-5.202 -29.087
1.00 71.16
-4.834 -29.992
1.00 68.91
-3.438 -27.525
1.00 60.74
-2.383 -27.042
1.00 58.17
CD1 LEU A 142
-1.541 -25.866
1.00 54.46
CD1 LEU A 142
CD2 LEU A 142
-1.489 -28.197
1.00 59.03
CD2 LEU A 142
-6.322 -28.392
1.00 67.85
-7.137 -28.473
1.00 72.98
-7.521 -29.899
1.00 78.24
-7.396 -30.219
1.00 78.37
-8.413 -27.644
1.00 73.85
-9.330 -27.582
1.00 74.67
-10.724 -27.057
1.00 77.83
-11.309 -27.747
1.00 77.63
-11.814 -28.979
1.00 83.93
NH1 ARG A 143
-11.815 -29.656
1.00 82.87
NH1 ARG A 143
NH2 ARG A 143
-12.324 -29.531
1.00 83.91
NH2 ARG A 143
-7.985 -30.767
1.00 80.86
-8.447 -32.057
1.00 84.38
-7.345 -33.080
1.00 80.13
-7.671 -34.216
1.00 83.56
-9.366 -32.567
1.00 83.55
-8.775 -32.013
1.00 81.09
-8.231 -30.654
1.00 82.89
-6.078 -32.686
1.00 87.24
-4.964 -33.608
1.00 85.21
-4.475 -33.584
1.00 80.74
-3.874 -34.550
1.00 76.55
ANISOU 1000
-3.810 -33.281
1.00 85.89
ANISOU 1001
-3.985 -33.867
1.00 92.35
ANISOU 1002
-3.523 -32.933
1.00 92.53
ANISOU 1003
OE1 GLN A 145
-2.394 -32.440
1.00 80.94
ANISOU 1004
OE1 GLN A 145
NE2 GLN A 145
-4.404 -32.687
1.00102.59
ANISOU 1005
NE2 GLN A 145
-4.744 -32.481
1.00 80.12
ANISOU 1006
-4.359 -32.330
1.00 78.27
ANISOU 1007
-2.894 -32.021
1.00 78.49
ANISOU 1008
-2.469 -31.932
1.00 74.80
ANISOU 1009
-2.120 -31.825
1.00 78.57
ANISOU 1010
-0.701 -31.487
1.00 70.24
ANISOU 1011
-0.124 -30.958
1.00 71.05
ANISOU 1012
-0.642 -31.246
1.00 74.95
ANISOU 1013
0.123 -32.707
1.00 70.03
ANISOU 1014
0.223 -33.801
1.00 82.59
ANISOU 1015
0.780 -35.111
1.00 92.21
ANISOU 1016
OE1 GLN A 147
1.171 -35.190
1.00 94.10
ANISOU 1017
OE1 GLN A 147
NE2 GLN A 147
0.809 -36.146
1.00 93.23
ANISOU 1018
NE2 GLN A 147
0.973 -30.209
1.00 65.64
ANISOU 1019
1.707 -29.747
1.00 64.29
ANISOU 1020
3.094 -29.232
1.00 64.79
ANISOU 1021
3.357 -28.891
1.00 67.49
ANISOU 1022
0.924 -28.635
1.00 67.60
ANISOU 1023
0.748 -27.115
1.00 70.26
ANISOU 1024
3.980 -29.183
1.00 62.61
ANISOU 1025
5.125 -28.295
1.00 49.23
ANISOU 1026
4.695 -26.996
1.00 52.33
ANISOU 1027
4.725 -26.849
1.00 55.66
ANISOU 1028
6.377 -28.882
1.00 60.00
ANISOU 1029
7.565 -27.902
1.00 63.32
ANISOU 1030
OD1 ASN A 149
7.558 -26.851
1.00 49.30
ANISOU 1031
OD1 ASN A 149
ND2 ASN A 149
8.607 -28.267
1.00 69.55
ANISOU 1032
ND2 ASN A 149
4.285 -26.057
1.00 57.81
ANISOU 1033
3.737 -24.788
1.00 53.82
ANISOU 1034
4.649 -24.121
1.00 54.21
ANISOU 1035
4.179 -23.531
1.00 53.64
ANISOU 1036
3.521 -23.854
1.00 48.50
ANISOU 1037
2.968 -22.518
1.00 46.06
ANISOU 1038
CD1 PHE A 150
1.604 -22.342
1.00 55.00
ANISOU 1039
CD1 PHE A 150
CD2 PHE A 150
3.814 -21.447
1.00 39.50
ANISOU 1040
CD2 PHE A 150
CE1 PHE A 150
1.091 -21.107
1.00 42.55
ANISOU 1041
CE1 PHE A 150
CE2 PHE A 150
3.320 -20.212
1.00 46.08
ANISOU 1042
CE2 PHE A 150
1.952 -20.043
1.00 49.60
ANISOU 1043
5.954 -24.197
1.00 50.75
ANISOU 1044
6.886 -23.524
1.00 55.09
ANISOU 1045
6.796 -24.125
1.00 44.19
ANISOU 1046
6.723 -23.400
1.00 56.36
ANISOU 1047
8.331 -23.604
1.00 58.33
ANISOU 1048
OG1 THR A 151
8.391 -23.115
1.00 60.56
ANISOU 1049
OG1 THR A 151
CG2 THR A 151
9.253 -22.762
1.00 57.16
ANISOU 1050
CG2 THR A 151
6.774 -25.447
1.00 50.06
ANISOU 1051
6.777 -26.107
1.00 59.73
ANISOU 1052
5.370 -26.173
1.00 64.37
ANISOU 1053
5.201 -26.083
1.00 68.02
ANISOU 1054
7.386 -27.510
1.00 69.63
ANISOU 1055
7.572 -28.293
1.00 84.69
ANISOU 1056
8.904 -28.009
1.00 89.27
ANISOU 1057
OE1 GLU A 152
9.750 -27.260
1.00 85.76
ANISOU 1058
OE1 GLU A 152
OE2 GLU A 152
9.110 -28.564
1.00 88.27
ANISOU 1059
OE2 GLU A 152
4.363 -26.271
1.00 58.62
ANISOU 1060
2.987 -26.563
1.00 50.89
ANISOU 1061
2.145 -25.311
1.00 48.56
ANISOU 1062
1.162 -25.348
1.00 62.25
ANISOU 1063
2.298 -27.441
1.00 59.41
ANISOU 1064
2.934 -28.809
1.00 69.06
ANISOU 1065
OD1 ASP A 153
3.563 -29.270
1.00 74.02
ANISOU 1066
OD1 ASP A 153
OD2 ASP A 153
2.811 -29.418
1.00 70.16
ANISOU 1067
OD2 ASP A 153
2.524 -24.195
1.00 49.48
ANISOU 1068
1.770 -22.958
1.00 51.74
ANISOU 1069
2.669 -21.781
1.00 51.42
ANISOU 1070
2.480 -21.112
1.00 52.17
ANISOU 1071
0.884 -22.611
1.00 50.33
ANISOU 1072
0.048 -21.361
1.00 54.27
ANISOU 1073
CD1 TYR A 154
0.584 -20.091
1.00 54.98
ANISOU 1074
CD1 TYR A 154
CD2 TYR A 154
-1.268 -21.449
1.00 56.26
ANISOU 1075
CD2 TYR A 154
CE1 TYR A 154
-0.160 -18.951
1.00 58.05
ANISOU 1076
CE1 TYR A 154
CE2 TYR A 154
-2.027 -20.320
1.00 60.12
ANISOU 1077
CE2 TYR A 154
-1.465 -19.071
1.00 60.36
ANISOU 1078
-2.212 -17.939
1.00 57.39
ANISOU 1079
3.642 -21.523
1.00 49.83
ANISOU 1080
4.429 -20.295
1.00 51.79
ANISOU 1081
5.119 -20.152
1.00 54.93
ANISOU 1082
5.138 -19.052
1.00 51.54
ANISOU 1083
5.474 -20.225
1.00 48.77
ANISOU 1084
5.653 -21.256
1.00 50.36
ANISOU 1085
6.377 -21.224
1.00 50.00
ANISOU 1086
5.453 -21.143
1.00 53.83
ANISOU 1087
5.676 -20.295
1.00 53.41
ANISOU 1088
7.320 -22.446
1.00 57.01
ANISOU 1089
8.566 -22.378
1.00 63.00
ANISOU 1090
9.430 -23.646
1.00 77.09
ANISOU 1091
OE1 GLU A 156
9.177 -24.522
1.00 77.04
ANISOU 1092
OE1 GLU A 156
OE2 GLU A 156
10.357 -23.770
1.00 81.60
ANISOU 1093
OE2 GLU A 156
4.420 -22.016
1.00 54.32
ANISOU 1094
3.611 -21.933
1.00 51.72
ANISOU 1095
2.660 -20.717
1.00 58.14
ANISOU 1096
2.201 -20.385
1.00 56.67
ANISOU 1097
2.801 -23.242
1.00 48.35
ANISOU 1098
2.716 -23.608
1.00 55.79
ANISOU 1099
4.066 -23.201
1.00 52.21
ANISOU 1100
2.371 -20.056
1.00 57.51
ANISOU 1101
1.403 -18.958
1.00 56.21
ANISOU 1102
1.911 -17.720
1.00 57.29
ANISOU 1103
1.257 -17.296
1.00 56.27
ANISOU 1104
1.029 -18.612
1.00 57.14
ANISOU 1105
0.029 -17.499
1.00 59.24
ANISOU 1106
CD1 PHE A 158
-1.211 -17.568
1.00 55.87
ANISOU 1107
CD1 PHE A 158
CD2 PHE A 158
0.344 -16.373
1.00 56.61
ANISOU 1108
CD2 PHE A 158
CE1 PHE A 158
-2.127 -16.543
1.00 58.81
ANISOU 1109
CE1 PHE A 158
CE2 PHE A 158
-0.567 -15.341
1.00 46.06
ANISOU 1110
CE2 PHE A 158
-1.811 -15.434
1.00 54.90
ANISOU 1111
3.079 -17.147
1.00 49.97
ANISOU 1112
3.550 -15.975
1.00 50.86
ANISOU 1113
3.952 -16.255
1.00 47.70
ANISOU 1114
3.831 -15.371
1.00 43.72
ANISOU 1115
4.776 -15.513
1.00 40.47
ANISOU 1116
5.240 -16.716
1.00 45.76
ANISOU 1117
3.987 -17.446
1.00 53.72
ANISOU 1118
4.430 -17.457
1.00 46.78
ANISOU 1119
4.815 -17.771
1.00 47.77
ANISOU 1120
3.545 -17.917
1.00 52.29
ANISOU 1121
3.520 -17.488
1.00 55.69
ANISOU 1122
5.696 -19.035
1.00 52.79
ANISOU 1123
CG1 ILE A 160
6.063 -19.364
1.00 68.25
ANISOU 1124
CG1 ILE A 160
CG2 ILE A 160
5.002 -20.220
1.00 58.08
ANISOU 1125
CG2 ILE A 160
CD1 ILE A 160
6.911 -18.304
1.00 69.51
ANISOU 1126
CD1 ILE A 160
2.492 -18.510
1.00 48.92
ANISOU 1127
1.199 -18.552
1.00 52.29
ANISOU 1128
0.590 -17.138
1.00 49.58
ANISOU 1129
-0.042 -16.814
1.00 46.66
ANISOU 1130
0.237 -19.484
1.00 56.33
ANISOU 1131
0.304 -20.964
1.00 61.87
ANISOU 1132
-0.413 -21.842
1.00 68.90
ANISOU 1133
-0.541 -23.248
1.00 84.11
ANISOU 1134
0.444 -24.145
1.00 88.57
ANISOU 1135
NH1 ARG A 161
1.653 -23.794
1.00 89.78
ANISOU 1136
NH1 ARG A 161
NH2 ARG A 161
0.222 -25.398
1.00 93.79
ANISOU 1137
NH2 ARG A 161
0.813 -16.275
1.00 50.02
ANISOU 1138
0.313 -14.894
1.00 54.88
ANISOU 1139
0.996 -14.136
1.00 53.54
ANISOU 1140
0.354 -13.355
1.00 55.53
ANISOU 1141
0.527 -14.119
1.00 54.95
ANISOU 1142
CG1 ILE A 162
-0.442 -14.607
1.00 53.08
ANISOU 1143
CG1 ILE A 162
CG2 ILE A 162
0.362 -12.603
1.00 55.51
ANISOU 1144
CG2 ILE A 162
CD1 ILE A 162
0.003 -14.250
1.00 55.59
ANISOU 1145
CD1 ILE A 162
2.291 -14.393
1.00 47.32
ANISOU 1146
3.012 -13.781
1.00 48.09
ANISOU 1147
2.484 -14.271
1.00 45.01
ANISOU 1148
2.335 -13.471
1.00 46.53
ANISOU 1149
4.517 -14.057
1.00 56.56
ANISOU 1150
5.279 -13.459
1.00 57.97
ANISOU 1151
CD1 PHE A 163
5.623 -12.103
1.00 52.31
ANISOU 1152
CD1 PHE A 163
CD2 PHE A 163
5.575 -14.220
1.00 59.86
ANISOU 1153
CD2 PHE A 163
CE1 PHE A 163
6.296 -11.520
1.00 47.18
ANISOU 1154
CE1 PHE A 163
CE2 PHE A 163
6.238 -13.654
1.00 57.91
ANISOU 1155
CE2 PHE A 163
6.607 -12.300
1.00 52.67
ANISOU 1156
2.225 -15.567
1.00 47.79
ANISOU 1157
1.669 -16.097
1.00 53.58
ANISOU 1158
0.386 -15.352
1.00 59.63
ANISOU 1159
0.143 -14.960
1.00 56.73
ANISOU 1160
1.359 -17.584
1.00 61.48
ANISOU 1161
2.392 -18.447
1.00 64.93
ANISOU 1162
3.722 -19.064
1.00 81.79
ANISOU 1163
2.787 -19.860
1.00 62.64
ANISOU 1164
-0.438 -15.177
1.00 60.55
ANISOU 1165
-1.683 -14.439
1.00 61.97
ANISOU 1166
-1.461 -13.023
1.00 58.75
ANISOU 1167
-2.042 -12.612
1.00 75.35
ANISOU 1168
-2.386 -14.378
1.00 55.38
ANISOU 1169
-3.627 -13.494
1.00 62.96
ANISOU 1170
CD1 LEU A 165
-4.732 -14.227
1.00 63.58
ANISOU 1171
CD1 LEU A 165
CD2 LEU A 165
-4.082 -13.083
1.00 64.55
ANISOU 1172
CD2 LEU A 165
-0.609 -12.293
1.00 62.98
ANISOU 1173
-0.253 -10.935
1.00 62.05
ANISOU 1174
0.320 -10.859
1.00 54.57
ANISOU 1175
1.00 56.94
ANISOU 1176
0.755 -10.408
1.00 67.87
ANISOU 1177
1.00 75.23
ANISOU 1178
CD1 LEU A 166
1.00 77.11
ANISOU 1179
CD1 LEU A 166
CD2 LEU A 166
1.00 74.87
ANISOU 1180
CD2 LEU A 166
1.132 -11.843
1.00 60.56
ANISOU 1181
1.831 -11.814
1.00 62.28
ANISOU 1182
1.078 -12.551
1.00 63.29
ANISOU 1183
1.554 -12.630
1.00 67.86
ANISOU 1184
3.243 -12.412
1.00 53.56
ANISOU 1185
-0.098 -13.076
1.00 65.05
ANISOU 1186
-0.913 -13.777
1.00 52.19
ANISOU 1187
-0.193 -14.980
1.00 53.51
ANISOU 1188
-0.189 -15.190
1.00 58.42
ANISOU 1189
0.425 -15.779
1.00 68.33
ANISOU 1190
1.123 -16.982
1.00 63.91
ANISOU 1191
0.229 -18.172
1.00 70.15
ANISOU 1192
-0.516 -18.140
1.00 72.65
ANISOU 1193
2.478 -17.119
1.00 61.88
ANISOU 1194
3.548 -16.079
1.00 61.35
ANISOU 1195
CD1 LEU A 169
4.787 -16.191
1.00 47.05
ANISOU 1196
CD1 LEU A 169
CD2 LEU A 169
3.936 -16.272
1.00 62.28
ANISOU 1197
CD2 LEU A 169
0.300 -19.229
1.00 75.97
ANISOU 1198
-0.606 -20.378
1.00 79.57
ANISOU 1199
-0.240 -21.258
1.00 80.81
ANISOU 1200
0.944 -21.353
1.00 76.30
ANISOU 1201
-0.424 -21.127
1.00 80.16
ANISOU 1202
0.966 -20.814
1.00 76.71
ANISOU 1203
1.221 -19.396
1.00 75.25
ANISOU 1204
-1.234 -21.868
1.00 90.01
ANISOU 1205
-1.001 -22.681
1.00 96.98
ANISOU 1206
-0.011 -23.846
1.00 95.31
ANISOU 1207
0.614 -24.248
1.00 98.40
ANISOU 1208
-2.334 -23.244
1.00105.74
ANISOU 1209
-3.171 -22.275
1.00110.32
ANISOU 1210
-4.330 -22.964
1.00115.86
ANISOU 1211
OE1 GLU A 171
-4.606 -24.150
1.00121.02
ANISOU 1212
OE1 GLU A 171
OE2 GLU A 171
-4.973 -22.316
1.00114.42
ANISOU 1213
OE2 GLU A 171
0.159 -24.367
1.00 91.10
ANISOU 1214
1.012 -25.544
1.00 93.50
ANISOU 1215
2.500 -25.205
1.00 89.68
ANISOU 1216
3.341 -26.095
1.00 82.88
ANISOU 1217
0.597 -26.313
1.00102.32
ANISOU 1218
0.933 -25.627
1.00106.57
ANISOU 1219
-0.258 -24.902
1.00113.29
ANISOU 1220
OE1 GLU A 172
-1.038 -24.308
1.00113.02
ANISOU 1221
OE1 GLU A 172
OE2 GLU A 172
-0.418 -24.931
1.00118.02
ANISOU 1222
OE2 GLU A 172
2.833 -23.926
1.00 90.52
ANISOU 1223
4.223 -23.517
1.00 87.80
ANISOU 1224
4.889 -23.465
1.00 82.43
ANISOU 1225
6.104 -23.287
1.00 79.19
ANISOU 1226
4.325 -22.140
1.00 90.26
ANISOU 1227
4.348 -22.220
1.00 98.67
ANISOU 1228
OD1 ASP A 173
4.640 -23.303
1.00104.19
ANISOU 1229
OD1 ASP A 173
OD2 ASP A 173
4.090 -21.179
1.00 96.17
ANISOU 1230
OD2 ASP A 173
4.102 -23.642
1.00 85.35
ANISOU 1231
4.620 -23.466
1.00 90.71
ANISOU 1232
5.816 -24.361
1.00 88.92
ANISOU 1233
6.837 -23.850
1.00 88.68
ANISOU 1234
3.520 -23.685
1.00 99.08
ANISOU 1235
CG1 ILE A 174
2.333 -22.760
1.00102.46
ANISOU 1236
CG1 ILE A 174
CG2 ILE A 174
4.084 -23.450
1.00 97.81
ANISOU 1237
CG2 ILE A 174
CD1 ILE A 174
1.172 -22.987
1.00102.97
ANISOU 1238
CD1 ILE A 174
5.704 -25.688
1.00 85.03
ANISOU 1239
6.800 -26.539
1.00 84.16
ANISOU 1240
8.135 -26.180
1.00 87.68
ANISOU 1241
9.183 -26.349
1.00 89.08
ANISOU 1242
6.354 -27.953
1.00 82.31
ANISOU 1243
5.380 -27.755
1.00 85.62
ANISOU 1244
4.684 -26.470
1.00 84.05
ANISOU 1245
8.095 -25.672
1.00 89.67
ANISOU 1246
9.314 -25.206
1.00 91.23
ANISOU 1247
9.812 -23.927
1.00 86.43
ANISOU 1248
10.993 -23.820
1.00 86.35
ANISOU 1249
9.087 -24.975
1.00 97.56
ANISOU 1250
10.334 -24.622
1.00 99.82
ANISOU 1251
ND1 HIS A 176
11.478 -25.388
1.00101.84
ANISOU 1252
ND1 HIS A 176
CD2 HIS A 176
10.624 -23.579
1.00101.06
ANISOU 1253
CD2 HIS A 176
CE1 HIS A 176
12.417 -24.836
1.00100.56
ANISOU 1254
CE1 HIS A 176
NE2 HIS A 176
11.924 -23.738
1.00101.00
ANISOU 1255
NE2 HIS A 176
8.904 -22.971
1.00 81.24
ANISOU 1256
9.246 -21.701
1.00 75.64
ANISOU 1257
9.688 -21.926
1.00 68.64
ANISOU 1258
10.682 -21.344
1.00 60.40
ANISOU 1259
8.059 -20.744
1.00 75.84
ANISOU 1260
8.272 -19.559
1.00 74.13
ANISOU 1261
CD1 LEU A 177
8.392 -20.070
1.00 75.20
ANISOU 1262
CD1 LEU A 177
CD2 LEU A 177
7.143 -18.538
1.00 74.33
ANISOU 1263
CD2 LEU A 177
8.937 -22.774
1.00 73.32
ANISOU 1264
9.284 -23.178
1.00 78.15
ANISOU 1265
10.710 -23.702
1.00 76.75
ANISOU 1266
11.499 -23.323
1.00 71.28
ANISOU 1267
8.322 -24.250
1.00 82.22
ANISOU 1268
8.683 -24.759
1.00 83.91
ANISOU 1269
7.730 -25.843
1.00 90.12
ANISOU 1270
8.138 -26.318
1.00 88.81
ANISOU 1271
8.190 -25.175
1.00 84.70
ANISOU 1272
11.033 -24.552
1.00 82.73
ANISOU 1273
12.367 -25.125
1.00 86.42
ANISOU 1274
13.436 -24.058
1.00 81.21
ANISOU 1275
14.460 -24.066
1.00 79.85
ANISOU 1276
12.440 -26.138
1.00 99.50
ANISOU 1277
13.852 -26.622
1.00107.49
ANISOU 1278
CD1 TYR A 179
14.492 -27.460
1.00110.51
ANISOU 1279
CD1 TYR A 179
CD2 TYR A 179
14.553 -26.221
1.00111.36
ANISOU 1280
CD2 TYR A 179
CE1 TYR A 179
15.787 -27.898
1.00114.22
ANISOU 1281
CE1 TYR A 179
CE2 TYR A 179
15.851 -26.652
1.00115.06
ANISOU 1282
CE2 TYR A 179
16.462 -27.491
1.00115.67
ANISOU 1283
17.751 -27.923
1.00115.72
ANISOU 1284
13.195 -23.126
1.00 75.42
ANISOU 1285
14.215 -22.126
1.00 72.39
ANISOU 1286
14.457 -21.153
1.00 70.97
ANISOU 1287
15.605 -20.772
1.00 69.47
ANISOU 1288
13.852 -21.352
1.00 69.72
ANISOU 1289
14.136 -22.117
1.00 73.14
ANISOU 1290
CD1 LEU A 180
13.820 -21.266
1.00 74.98
ANISOU 1291
CD1 LEU A 180
CD2 LEU A 180
15.597 -22.533
1.00 72.48
ANISOU 1292
CD2 LEU A 180
13.389 -20.749
1.00 74.79
ANISOU 1293
13.515 -19.786
1.00 69.14
ANISOU 1294
14.270 -20.420
1.00 70.58
ANISOU 1295
15.122 -19.779
1.00 62.86
ANISOU 1296
12.139 -19.274
1.00 63.37
ANISOU 1297
OG1 THR A 181
11.274 -20.378
1.00 69.54
ANISOU 1298
OG1 THR A 181
CG2 THR A 181
11.511 -18.451
1.00 64.70
ANISOU 1299
CG2 THR A 181
13.957 -21.684
1.00 79.92
ANISOU 1300
14.635 -22.423
1.00 86.97
ANISOU 1301
16.155 -22.474
1.00 90.48
ANISOU 1302
16.921 -22.346
1.00 91.99
ANISOU 1303
14.066 -23.843
1.00 93.09
ANISOU 1304
12.658 -23.871
1.00 98.60
ANISOU 1305
OD1 ASP A 182
11.980 -22.820
1.00102.03
ANISOU 1306
OD1 ASP A 182
OD2 ASP A 182
12.221 -24.947
1.00 99.49
ANISOU 1307
OD2 ASP A 182
16.584 -22.617
1.00 90.69
ANISOU 1308
18.009 -22.723
1.00 86.65
ANISOU 1309
18.754 -21.413
1.00 87.50
ANISOU 1310
19.983 -21.386
1.00 90.78
ANISOU 1311
18.197 -23.187
1.00 91.83
ANISOU 1312
17.472 -24.469
1.00 99.42
ANISOU 1313
17.791 -25.576
1.00104.65
ANISOU 1314
OE1 GLN A 183
18.946 -25.774
1.00105.59
ANISOU 1315
OE1 GLN A 183
NE2 GLN A 183
16.763 -26.303
1.00108.58
ANISOU 1316
NE2 GLN A 183
18.004 -20.323
1.00 88.77
ANISOU 1317
18.581 -19.025
1.00 91.17
ANISOU 1318
18.692 -18.898
1.00 95.49
ANISOU 1319
19.382 -18.014
1.00 96.67
ANISOU 1320
17.755 -17.904
1.00 89.98
ANISOU 1321
17.553 -18.135
1.00 89.43
ANISOU 1322
16.603 -16.893
1.00 92.39
ANISOU 1323
17.820 -15.584
1.00 73.43
ANISOU 1324
17.991 -19.787
1.00 97.77
ANISOU 1325
17.960 -19.804
1.00 96.93
ANISOU 1326
18.617 -21.100
1.00 92.51
ANISOU 1327
18.954 -21.187
1.00 89.93
ANISOU 1328
16.506 -19.663
1.00 94.75
ANISOU 1329
OG1 THR A 185
15.909 -18.498
1.00 91.14
ANISOU 1330
OG1 THR A 185
CG2 THR A 185
16.456 -19.538
1.00 92.96
ANISOU 1331
CG2 THR A 185
18.816 -22.091
1.00 90.75
ANISOU 1332
19.379 -23.393
1.00 81.40
ANISOU 1333
20.682 -23.667
1.00 75.86
ANISOU 1334
21.509 -22.768
1.00 71.65
ANISOU 1335
18.380 -24.526
1.00 76.53
ANISOU 1336
20.855 -27.203
1.00 80.19
ANISOU 1337
20.630 -28.342
1.00 86.79
ANISOU 1338
21.827 -28.720
1.00 99.13
ANISOU 1339
22.639 -29.559
1.00102.69
ANISOU 1340
21.947 -28.097
1.00105.34
ANISOU 1341
22.903 -28.535
1.00113.71
ANISOU 1342
23.031 -27.498
1.00113.83
ANISOU 1343
23.009 -27.841
1.00120.52
ANISOU 1344
22.472 -29.872
1.00121.92
ANISOU 1345
21.143 -29.803
1.00123.87
ANISOU 1346
23.186 -26.236
1.00104.99
ANISOU 1347
23.082 -25.145
1.00 93.12
ANISOU 1348
23.612 -23.848
1.00 82.73
ANISOU 1349
23.277 -23.493
1.00 80.55
ANISOU 1350
21.618 -24.989
1.00 89.07
ANISOU 1351
21.332 -23.840
1.00 90.80
ANISOU 1352
19.602 -23.833
1.00115.09
ANISOU 1353
19.460 -25.464
1.00109.57
ANISOU 1354
24.455 -23.148
1.00 75.38
ANISOU 1355
25.018 -21.888
1.00 67.88
ANISOU 1356
23.923 -20.847
1.00 63.86
ANISOU 1357
22.834 -20.996
1.00 66.96
ANISOU 1358
26.079 -21.339
1.00 74.96
ANISOU 1359
OG1 THR A 192
26.820 -22.426
1.00 84.17
ANISOU 1360
OG1 THR A 192
CG2 THR A 192
27.027 -20.381
1.00 70.96
ANISOU 1361
CG2 THR A 192
24.198 -19.798
1.00 55.16
ANISOU 1362
23.239 -18.725
1.00 55.22
ANISOU 1363
23.047 -18.010
1.00 57.97
ANISOU 1364
21.932 -17.603
1.00 47.69
ANISOU 1365
23.665 -17.722
1.00 56.13
ANISOU 1366
22.621 -16.691
1.00 66.71
ANISOU 1367
CD1 PHE A 193
21.627 -16.934
1.00 74.95
ANISOU 1368
CD1 PHE A 193
CD2 PHE A 193
22.589 -15.505
1.00 64.48
ANISOU 1369
CD2 PHE A 193
CE1 PHE A 193
20.644 -15.997
1.00 71.48
ANISOU 1370
CE1 PHE A 193
CE2 PHE A 193
21.611 -14.564
1.00 61.91
ANISOU 1371
CE2 PHE A 193
20.637 -14.811
1.00 68.19
ANISOU 1372
24.159 -17.795
1.00 51.90
ANISOU 1373
24.132 -17.157
1.00 50.30
ANISOU 1374
23.316 -17.994
1.00 52.48
ANISOU 1375
22.519 -17.458
1.00 58.20
ANISOU 1376
25.557 -16.964
1.00 51.82
ANISOU 1377
23.518 -19.311
1.00 48.65
ANISOU 1378
22.783 -20.246
1.00 51.82
ANISOU 1379
21.285 -20.201
1.00 52.16
ANISOU 1380
20.458 -20.245
1.00 57.23
ANISOU 1381
23.312 -21.664
1.00 59.67
ANISOU 1382
24.512 -21.976
1.00 69.13
ANISOU 1383
25.068 -23.366
1.00 72.68
ANISOU 1384
OE1 GLU A 195
25.402 -24.053
1.00 64.82
ANISOU 1385
OE1 GLU A 195
OE2 GLU A 195
25.204 -23.745
1.00 73.61
ANISOU 1386
OE2 GLU A 195
20.938 -20.138
1.00 47.90
ANISOU 1387
19.540 -20.113
1.00 49.42
ANISOU 1388
18.889 -18.805
1.00 53.06
ANISOU 1389
17.730 -18.782
1.00 54.36
ANISOU 1390
19.399 -20.311
1.00 53.62
ANISOU 1391
19.628 -17.708
1.00 50.78
ANISOU 1392
19.086 -16.414
1.00 59.59
ANISOU 1393
18.814 -16.378
1.00 59.07
ANISOU 1394
17.807 -15.828
1.00 49.33
ANISOU 1395
20.044 -15.296
1.00 66.27
ANISOU 1396
19.451 -13.914
1.00 69.88
ANISOU 1397
20.395 -12.864
1.00 77.30
ANISOU 1398
21.686 -12.765
1.00 82.58
ANISOU 1399
22.504 -11.592
1.00 87.05
ANISOU 1400
19.717 -16.976
1.00 43.94
ANISOU 1401
19.615 -16.957
1.00 46.26
ANISOU 1402
18.436 -17.833
1.00 58.90
ANISOU 1403
17.660 -17.445
1.00 56.98
ANISOU 1404
20.940 -17.421
1.00 48.36
ANISOU 1405
20.923 -17.655
1.00 59.29
ANISOU 1406
20.827 -16.370
1.00 67.93
ANISOU 1407
OE1 GLU A 198
20.607 -15.259
1.00 60.30
ANISOU 1408
OE1 GLU A 198
OE2 GLU A 198
20.994 -16.485
1.00 68.18
ANISOU 1409
OE2 GLU A 198
18.263 -18.978
1.00 52.19
ANISOU 1410
17.131 -19.845
1.00 58.20
ANISOU 1411
15.825 -19.115
1.00 55.83
ANISOU 1412
14.859 -19.224
1.00 57.58
ANISOU 1413
17.207 -21.140
1.00 55.55
ANISOU 1414
15.789 -18.364
1.00 46.96
ANISOU 1415
14.596 -17.579
1.00 48.63
ANISOU 1416
14.375 -16.494
1.00 52.17
ANISOU 1417
13.238 -16.254
1.00 50.70
ANISOU 1418
14.676 -16.967
1.00 43.18
ANISOU 1419
13.504 -16.041
1.00 48.50
ANISOU 1420
CD1 LEU A 200
12.191 -16.797
1.00 53.46
ANISOU 1421
CD1 LEU A 200
CD2 LEU A 200
13.649 -15.523
1.00 51.79
ANISOU 1422
CD2 LEU A 200
15.457 -15.844
1.00 53.45
ANISOU 1423
15.358 -14.840
1.00 55.05
ANISOU 1424
14.859 -15.499
1.00 58.48
ANISOU 1425
13.938 -14.992
1.00 54.40
ANISOU 1426
16.709 -14.162
1.00 48.33
ANISOU 1427
17.137 -13.183
1.00 43.51
ANISOU 1428
CD1 TYR A 201
16.228 -12.673
1.00 40.15
ANISOU 1429
CD1 TYR A 201
CD2 TYR A 201
18.473 -12.801
1.00 53.58
ANISOU 1430
CD2 TYR A 201
CE1 TYR A 201
16.626 -11.783
1.00 42.38
ANISOU 1431
CE1 TYR A 201
CE2 TYR A 201
18.885 -11.910
1.00 44.04
ANISOU 1432
CE2 TYR A 201
17.959 -11.413
1.00 46.36
ANISOU 1433
18.362 -10.534
1.00 53.31
ANISOU 1434
15.426 -16.660
1.00 55.53
ANISOU 1435
15.095 -17.335
1.00 57.19
ANISOU 1436
13.641 -17.824
1.00 59.37
ANISOU 1437
13.086 -18.083
1.00 62.89
ANISOU 1438
16.046 -18.519
1.00 57.42
ANISOU 1439
17.396 -18.091
1.00 57.19
ANISOU 1440
OD1 ASP A 202
17.558 -16.911
1.00 58.19
ANISOU 1441
OD1 ASP A 202
OD2 ASP A 202
18.278 -18.972
1.00 66.91
ANISOU 1442
OD2 ASP A 202
13.041 -17.994
1.00 63.01
ANISOU 1443
11.621 -18.329
1.00 64.37
ANISOU 1444
10.728 -17.102
1.00 62.66
ANISOU 1445
9.656 -17.212
1.00 63.93
ANISOU 1446
11.300 -18.918
1.00 62.89
ANISOU 1447
9.822 -19.032
1.00 63.90
ANISOU 1448
CD1 TYR A 203
9.097 -20.139
1.00 61.81
ANISOU 1449
CD1 TYR A 203
CD2 TYR A 203
9.152 -18.036
1.00 58.72
ANISOU 1450
CD2 TYR A 203
CE1 TYR A 203
7.740 -20.241
1.00 69.98
ANISOU 1451
CE1 TYR A 203
CE2 TYR A 203
7.796 -18.124
1.00 60.40
ANISOU 1452
CE2 TYR A 203
7.094 -19.231
1.00 72.14
ANISOU 1453
5.739 -19.310
1.00 72.59
ANISOU 1454
11.185 -15.932
1.00 56.13
ANISOU 1455
10.401 -14.704
1.00 48.80
ANISOU 1456
10.430 -14.051
1.00 57.55
ANISOU 1457
9.406 -13.532
1.00 60.07
ANISOU 1458
10.880 -13.702
1.00 45.70
ANISOU 1459
10.611 -14.059
1.00 53.38
ANISOU 1460
CD1 LEU A 204
11.457 -13.220
1.00 43.33
ANISOU 1461
CD1 LEU A 204
CD2 LEU A 204
9.132 -13.886
1.00 52.12
ANISOU 1462
CD2 LEU A 204
11.582 -14.085
1.00 57.02
ANISOU 1463
11.761 -13.303
1.00 59.11
ANISOU 1464
10.769 -13.639
1.00 61.11
ANISOU 1465
10.286 -12.725
1.00 65.44
ANISOU 1466
13.202 -13.443
1.00 82.40
ANISOU 1467
CG1 ILE A 205
14.259 -13.214
1.00 86.16
ANISOU 1468
CG1 ILE A 205
CG2 ILE A 205
13.445 -12.416
1.00 84.19
ANISOU 1469
CG2 ILE A 205
CD1 ILE A 205
15.647 -13.705
1.00 91.13
ANISOU 1470
CD1 ILE A 205
10.442 -14.933
1.00 65.14
ANISOU 1471
9.444 -15.200
1.00 64.38
ANISOU 1472
8.069 -14.614
1.00 60.20
ANISOU 1473
7.346 -14.151
1.00 61.99
ANISOU 1474
9.382 -16.730
1.00 68.74
ANISOU 1475
10.709 -17.183
1.00 69.40
ANISOU 1476
11.058 -16.180
1.00 60.56
ANISOU 1477
7.707 -14.671
1.00 57.86
ANISOU 1478
6.435 -14.155
1.00 57.13
ANISOU 1479
6.369 -12.635
1.00 56.07
ANISOU 1480
5.342 -12.067
1.00 56.60
ANISOU 1481
6.209 -14.563
1.00 57.39
ANISOU 1482
CG1 ILE A 207
6.266 -16.086
1.00 63.69
ANISOU 1483
CG1 ILE A 207
CG2 ILE A 207
4.872 -14.044
1.00 54.74
ANISOU 1484
CG2 ILE A 207
CD1 ILE A 207
6.157 -16.566
1.00 66.17
ANISOU 1485
CD1 ILE A 207
7.482 -11.983
1.00 60.25
ANISOU 1486
7.563 -10.535
1.00 57.91
ANISOU 1487
7.365 -10.096
1.00 62.32
ANISOU 1488
1.00 55.30
ANISOU 1489
8.900 -10.020
1.00 55.59
ANISOU 1490
CG1 ILE A 208
8.885 -10.061
1.00 47.54
ANISOU 1491
CG1 ILE A 208
CG2 ILE A 208
1.00 50.13
ANISOU 1492
CG2 ILE A 208
CD1 ILE A 208
1.00 50.44
ANISOU 1493
CD1 ILE A 208
8.030 -10.788
1.00 57.23
ANISOU 1494
7.988 -10.421
1.00 67.61
ANISOU 1495
6.580 -10.603
1.00 75.76
ANISOU 1496
1.00 77.02
ANISOU 1497
9.004 -11.252
1.00 74.79
ANISOU 1498
10.444 -10.885
1.00 80.27
ANISOU 1499
11.474 -11.692
1.00 92.74
ANISOU 1500
OE1 GLU A 209
11.112 -12.742
1.00 91.84
ANISOU 1501
OE1 GLU A 209
OE2 GLU A 209
12.660 -11.286
1.00 98.82
ANISOU 1502
OE2 GLU A 209
5.892 -11.665
1.00 76.98
ANISOU 1503
4.508 -11.941
1.00 77.46
ANISOU 1504
3.513 -10.888
1.00 71.78
ANISOU 1505
2.598 -10.465
1.00 73.51
ANISOU 1506
4.093 -13.347
1.00 83.02
ANISOU 1507
2.608 -13.646
1.00 89.74
ANISOU 1508
2.041 -13.691
1.00106.64
ANISOU 1509
OE1 GLN A 210
2.777 -13.793
1.00114.93
ANISOU 1510
OE1 GLN A 210
NE2 GLN A 210
0.717 -13.620
1.00111.85
ANISOU 1511
NE2 GLN A 210
3.704 -10.454
1.00 63.53
ANISOU 1512
1.00 64.19
ANISOU 1513
1.00 64.52
ANISOU 1514
1.00 65.16
ANISOU 1515
1.00 63.48
ANISOU 1516
2.230 -11.140
1.00 69.65
ANISOU 1517
1.873 -11.330
1.00 70.05
ANISOU 1518
1.514 -12.729
1.00 72.35
ANISOU 1519
1.213 -13.269
1.00 69.72
ANISOU 1520
NH1 ARG A 211
1.193 -12.518
1.00 53.12
ANISOU 1521
NH1 ARG A 211
NH2 ARG A 211
0.904 -14.557
1.00 69.18
ANISOU 1522
NH2 ARG A 211
1.00 63.65
ANISOU 1523
1.00 73.84
ANISOU 1524
1.00 85.80
ANISOU 1525
1.00 96.93
ANISOU 1526
1.00 74.37
ANISOU 1527
1.00 79.94
ANISOU 1528
1.00 82.86
ANISOU 1529
1.00 84.22
ANISOU 1530
1.00 88.00
ANISOU 1531
NH1 ARG A 212
1.00 88.92
ANISOU 1532
NH1 ARG A 212
NH2 ARG A 212
1.00 77.92
ANISOU 1533
NH2 ARG A 212
1.00 92.39
ANISOU 1534
1.00105.58
ANISOU 1535
1.00110.60
ANISOU 1536
1.00112.68
ANISOU 1537
1.00110.04
ANISOU 1538
1.00109.45
ANISOU 1539
1.00112.31
ANISOU 1540
OE1 GLN A 213
1.00114.70
ANISOU 1541
OE1 GLN A 213
NE2 GLN A 213
1.00115.35
ANISOU 1542
NE2 GLN A 213
1.00109.62
ANISOU 1543
1.00105.91
ANISOU 1544
1.00101.00
ANISOU 1545
1.00 98.57
ANISOU 1546
1.00111.25
ANISOU 1547
1.00109.04
ANISOU 1548
1.00101.09
ANISOU 1549
1.00 96.40
ANISOU 1550
1.00 89.28
ANISOU 1551
1.00 98.34
ANISOU 1552
1.00 97.33
ANISOU 1553
1.00100.69
ANISOU 1554
1.00104.40
ANISOU 1555
1.00 96.12
ANISOU 1556
1.00 94.06
ANISOU 1557
1.00100.26
ANISOU 1558
1.00 94.06
ANISOU 1559
1.00 88.97
ANISOU 1560
1.00 84.16
ANISOU 1561
1.00 83.89
ANISOU 1562
1.00 80.50
ANISOU 1563
1.00 75.72
ANISOU 1564
1.00 71.08
ANISOU 1565
1.00 66.80
ANISOU 1566
1.00 78.43
ANISOU 1567
OG1 THR A 217
1.00 86.36
ANISOU 1568
OG1 THR A 217
CG2 THR A 217
1.00 77.39
ANISOU 1569
CG2 THR A 217
1.00 67.01
ANISOU 1570
1.00 62.62
ANISOU 1571
1.00 54.09
ANISOU 1572
1.00 50.51
ANISOU 1573
1.00 67.18
ANISOU 1574
1.00 71.92
ANISOU 1575
OD1 ASP A 218
1.00 72.18
ANISOU 1576
OD1 ASP A 218
OD2 ASP A 218
0.923 -10.262
1.00 77.24
ANISOU 1577
OD2 ASP A 218
1.00 48.65
ANISOU 1578
1.00 48.74
ANISOU 1579
1.00 51.52
ANISOU 1580
1.00 50.47
ANISOU 1581
1.00 60.82
ANISOU 1582
1.00 51.75
ANISOU 1583
1.00 47.09
ANISOU 1584
1.00 53.92
ANISOU 1585
1.00 52.60
ANISOU 1586
4.351 -10.230
1.00 55.43
ANISOU 1587
CG1 ILE A 220
4.991 -11.039
1.00 56.61
ANISOU 1588
CG1 ILE A 220
CG2 ILE A 220
5.170 -10.403
1.00 47.82
ANISOU 1589
CG2 ILE A 220
CD1 ILE A 220
5.003 -12.536
1.00 59.61
ANISOU 1590
CD1 ILE A 220
1.00 52.49
ANISOU 1591
1.00 54.74
ANISOU 1592
1.00 49.25
ANISOU 1593
1.00 49.40
ANISOU 1594
1.00 53.65
ANISOU 1595
1.00 56.90
ANISOU 1596
1.00 45.75
ANISOU 1597
1.00 57.01
ANISOU 1598
1.00 54.86
ANISOU 1599
1.00 50.23
ANISOU 1600
1.00 52.26
ANISOU 1601
CG1 ILE A 222
1.00 64.13
ANISOU 1602
CG1 ILE A 222
CG2 ILE A 222
1.00 52.53
ANISOU 1603
CG2 ILE A 222
CD1 ILE A 222
1.00 72.04
ANISOU 1604
CD1 ILE A 222
1.00 46.73
ANISOU 1605
1.00 43.84
ANISOU 1606
1.00 45.10
ANISOU 1607
1.00 53.22
ANISOU 1608
1.00 46.40
ANISOU 1609
CG1 VAL A 223
1.00 45.36
ANISOU 1610
CG1 VAL A 223
CG2 VAL A 223
1.00 43.52
ANISOU 1611
CG2 VAL A 223
1.00 45.26
ANISOU 1612
1.00 48.37
ANISOU 1613
1.00 54.28
ANISOU 1614
1.00 56.88
ANISOU 1615
1.00 51.71
ANISOU 1616
1.00 48.21
ANISOU 1617
1.00 51.85
ANISOU 1618
1.00 57.10
ANISOU 1619
1.00 59.48
ANISOU 1620
1.00 50.59
ANISOU 1621
1.00 65.63
ANISOU 1622
OD1 ASN A 225
1.00 72.27
ANISOU 1623
OD1 ASN A 225
ND2 ASN A 225
1.00 63.32
ANISOU 1624
ND2 ASN A 225
1.00 48.73
ANISOU 1625
1.00 50.66
ANISOU 1626
1.00 48.06
ANISOU 1627
1.00 50.19
ANISOU 1628
1.00 53.44
ANISOU 1629
1.00 49.90
ANISOU 1630
1.00 45.89
ANISOU 1631
1.00 46.01
ANISOU 1632
1.00 51.22
ANISOU 1633
1.00 59.79
ANISOU 1634
1.00 66.66
ANISOU 1635
OE1 GLN A 227
1.00 64.41
ANISOU 1636
OE1 GLN A 227
NE2 GLN A 227
1.00 65.73
ANISOU 1637
NE2 GLN A 227
1.00 51.09
ANISOU 1638
1.00 49.63
ANISOU 1639
1.00 51.10
ANISOU 1640
1.00 52.05
ANISOU 1641
1.00 46.90
ANISOU 1642
CG1 VAL A 228
1.00 47.23
ANISOU 1643
CG1 VAL A 228
CG2 VAL A 228
1.00 49.77
ANISOU 1644
CG2 VAL A 228
1.00 48.23
ANISOU 1645
1.00 44.93
ANISOU 1646
1.00 47.41
ANISOU 1647
1.00 52.68
ANISOU 1648
1.00 49.36
ANISOU 1649
1.00 52.62
ANISOU 1650
OD1 ASN A 229
1.00 58.35
ANISOU 1651
OD1 ASN A 229
ND2 ASN A 229
1.00 51.32
ANISOU 1652
ND2 ASN A 229
1.00 47.44
ANISOU 1653
1.00 49.83
ANISOU 1654
1.00 51.37
ANISOU 1655
1.00 53.56
ANISOU 1656
1.00 50.44
ANISOU 1657
1.00 64.89
ANISOU 1658
1.00 50.67
ANISOU 1659
1.00 48.29
ANISOU 1660
1.00 53.40
ANISOU 1661
1.00 51.40
ANISOU 1662
1.00 50.25
ANISOU 1663
1.00 51.32
ANISOU 1664
1.00 57.84
ANISOU 1665
NH1 ARG A 231
1.00 62.37
ANISOU 1666
NH1 ARG A 231
NH2 ARG A 231
1.00 60.68
ANISOU 1667
NH2 ARG A 231
1.00 54.33
ANISOU 1668
1.00 51.03
ANISOU 1669
1.00 51.57
ANISOU 1670
1.00 51.03
ANISOU 1671
1.00 53.61
ANISOU 1672
1.00 56.00
ANISOU 1673
1.00 58.90
ANISOU 1674
1.00 47.06
ANISOU 1675
1.00 45.91
ANISOU 1676
1.00 54.45
ANISOU 1677
1.00 49.74
ANISOU 1678
1.00 51.24
ANISOU 1679
CG1 ILE A 233
1.00 47.80
ANISOU 1680
CG1 ILE A 233
CG2 ILE A 233
1.00 49.48
ANISOU 1681
CG2 ILE A 233
CD1 ILE A 233
1.00 47.61
ANISOU 1682
CD1 ILE A 233
1.00 56.5}