spacer
spacer

PDBsum entry 3rdc

Go to PDB code: 
Top Page protein ligands links
Isomerase/isomerase inhibitor PDB id
3rdc
Jmol
Contents
Protein chain
164 a.a.
Ligands
EA4
Waters ×223
HEADER    ISOMERASE/ISOMERASE INHIBITOR           01-APR-11   3RDC
TITLE     HUMAN CYCLOPHILIN D COMPLEXED WITH AN INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE F, MITOCHONDRIAL;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 43-207;
COMPND   5 SYNONYM: PPIASE F, CYCLOPHILIN F, ROTAMASE F;
COMPND   6 EC: 5.2.1.8;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: PPIF, CYP3;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    BETA BARREL, PROLYL CIS/TRANS ISOMERASE, MITOCHONDRIA, INHIBITOR,
KEYWDS   2 ISOMERASE-ISOMERASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.COLLIANDRE,H.AHMED-BELKACEM,Y.BESSIN,J.M.PAWLOTSKY,J.F.GUICHOU
REVDAT   1   21-MAR-12 3RDC    0
JRNL        AUTH   L.COLLIANDRE,H.AHMED-BELKACEM,Y.BESSIN,J.M.PAWLOTSKY,
JRNL        AUTH 2 J.F.GUICHOU
JRNL        TITL   RATIONAL DESIGN OF SMALL-MOLECULE INHIBITORS OF HUMAN
JRNL        TITL 2 CYCLOPHILINS AND HCV REPLICATION
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.94 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.4.0062
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.79
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0
REMARK   3   NUMBER OF REFLECTIONS             : 10358
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208
REMARK   3   R VALUE            (WORKING SET) : 0.205
REMARK   3   FREE R VALUE                     : 0.270
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 529
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.94
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 672
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.66
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1860
REMARK   3   BIN FREE R VALUE SET COUNT          : 37
REMARK   3   BIN FREE R VALUE                    : 0.3400
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1232
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 18
REMARK   3   SOLVENT ATOMS            : 223
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.29
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.58000
REMARK   3    B22 (A**2) : -0.58000
REMARK   3    B33 (A**2) : 1.15000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.232
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.201
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.130
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.259
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.908
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.853
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1277 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):   865 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1721 ; 1.063 ; 1.962
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2102 ; 0.809 ; 3.003
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   163 ; 5.879 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    51 ;33.292 ;24.510
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   208 ;10.362 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;12.106 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   186 ; 0.063 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1439 ; 0.004 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   256 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   810 ; 0.349 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   345 ; 0.084 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1301 ; 0.605 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   467 ; 0.970 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   420 ; 1.477 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3RDC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064791.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.3
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : YALE MIRROR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10358
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.200
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 9.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5
REMARK 200  DATA REDUNDANCY                : 4.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.05900
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.99
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.18800
REMARK 200   FOR SHELL         : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 2BIT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 36.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG4000, PH 7.3, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4
REMARK 290       7555   Y,X,-Z
REMARK 290       8555   -Y,-X,-Z+1/2
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   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.49750
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       28.22250
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       28.22250
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       21.74875
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       28.22250
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       28.22250
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       65.24625
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       28.22250
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       28.22250
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       21.74875
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       28.22250
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       28.22250
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       65.24625
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       43.49750
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   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
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     MET A    42
REMARK 465     SER A    43
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  ATOMS
REMARK 470     LYS A  57    CD   CE   NZ
REMARK 470     ARG A 193    CD   NE   CZ   NH1  NH2
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        PSI       PHI
REMARK 500    PHE A 102      -77.55   -149.19
REMARK 500    THR A 161       64.24   -115.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EA4 A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R49   RELATED DB: PDB
REMARK 900 RELATED ID: 3R4G   RELATED DB: PDB
REMARK 900 RELATED ID: 3R54   RELATED DB: PDB
REMARK 900 RELATED ID: 3R56   RELATED DB: PDB
REMARK 900 RELATED ID: 3R57   RELATED DB: PDB
REMARK 900 RELATED ID: 3R59   RELATED DB: PDB
REMARK 900 RELATED ID: 3RCF   RELATED DB: PDB
REMARK 900 RELATED ID: 3RCG   RELATED DB: PDB
REMARK 900 RELATED ID: 3RCI   RELATED DB: PDB
REMARK 900 RELATED ID: 3RCK   RELATED DB: PDB
REMARK 900 RELATED ID: 3RCL   RELATED DB: PDB
REMARK 900 RELATED ID: 3RD9   RELATED DB: PDB
REMARK 900 RELATED ID: 3RDA   RELATED DB: PDB
REMARK 900 RELATED ID: 3RDB   RELATED DB: PDB
REMARK 900 RELATED ID: 3RDD   RELATED DB: PDB
DBREF  3RDC A   43   207  UNP    P30405   PPIF_HUMAN      43    207
SEQADV 3RDC MET A   42  UNP  P30405              INITIATING METHIONINE
SEQADV 3RDC ILE A  175  UNP  P30405    LYS   175 ENGINEERED MUTATION
SEQRES   1 A  166  MET SER GLY ASN PRO LEU VAL TYR LEU ASP VAL ASP ALA
SEQRES   2 A  166  ASN GLY LYS PRO LEU GLY ARG VAL VAL LEU GLU LEU LYS
SEQRES   3 A  166  ALA ASP VAL VAL PRO LYS THR ALA GLU ASN PHE ARG ALA
SEQRES   4 A  166  LEU CYS THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER
SEQRES   5 A  166  THR PHE HIS ARG VAL ILE PRO SER PHE MET CYS GLN ALA
SEQRES   6 A  166  GLY ASP PHE THR ASN HIS ASN GLY THR GLY GLY LYS SER
SEQRES   7 A  166  ILE TYR GLY SER ARG PHE PRO ASP GLU ASN PHE THR LEU
SEQRES   8 A  166  LYS HIS VAL GLY PRO GLY VAL LEU SER MET ALA ASN ALA
SEQRES   9 A  166  GLY PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR
SEQRES  10 A  166  ILE LYS THR ASP TRP LEU ASP GLY LYS HIS VAL VAL PHE
SEQRES  11 A  166  GLY HIS VAL ILE GLU GLY MET ASP VAL VAL LYS LYS ILE
SEQRES  12 A  166  GLU SER PHE GLY SER LYS SER GLY ARG THR SER LYS LYS
SEQRES  13 A  166  ILE VAL ILE THR ASP CYS GLY GLN LEU SER
HET    EA4  A   1      18
HETNAM     EA4 ETHYL N-[(4-AMINOBENZYL)CARBAMOYL]GLYCINATE
FORMUL   2  EA4    C12 H17 N3 O3
FORMUL   3  HOH   *223(H2 O)
HELIX    1   1 VAL A   71  GLY A   84  1                                  14
HELIX    2   2 THR A  161  ASP A  165  5                                   5
HELIX    3   3 GLY A  177  PHE A  187  1                                  11
SHEET    1   A 8 PHE A  95  ILE A  99  0
SHEET    2   A 8 MET A 103  ALA A 106 -1  O  GLN A 105   N  ARG A  97
SHEET    3   A 8 PHE A 154  CYS A 157 -1  O  PHE A 154   N  ALA A 106
SHEET    4   A 8 VAL A 139  MET A 142 -1  N  SER A 141   O  PHE A 155
SHEET    5   A 8 VAL A 170  GLU A 176 -1  O  GLY A 172   N  LEU A 140
SHEET    6   A 8 LYS A  57  LEU A  66 -1  N  VAL A  63   O  GLU A 176
SHEET    7   A 8 LEU A  47  ALA A  54 -1  N  VAL A  52   O  LEU A  59
SHEET    8   A 8 ILE A 198  GLN A 205 -1  O  ASP A 202   N  ASP A  51
SITE     1 AC1 14 ARG A  97  GLN A 105  GLY A 114  ARG A 124
SITE     2 AC1 14 ALA A 143  ASN A 144  THR A 149  GLY A 151
SITE     3 AC1 14 GLN A 153  PHE A 155  HIS A 168  HOH A 283
SITE     4 AC1 14 HOH A 303  HOH A 315
CRYST1   56.445   56.445   86.995  90.00  90.00  90.00 P 41 21 2     8
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.017716  0.000000  0.000000        0.00000
SCALE2      0.000000  0.017716  0.000000        0.00000
SCALE3      0.000000  0.000000  0.011495        0.00000
      
PROCHECK
Go to PROCHECK summary
 References