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PDBsum entry 3i6c

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Isomerase PDB id
3i6c
Jmol
Contents
Protein chain
113 a.a.
Ligands
GIA ×3
Waters ×166
HEADER    ISOMERASE                               06-JUL-09   3I6C
TITLE     STRUCTURE-BASED DESIGN OF NOVEL PIN1 INHIBITORS (II)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-
COMPND   3 INTERACTING 1;
COMPND   4 CHAIN: A, B;
COMPND   5 FRAGMENT: UNP RESIDUES 45-163;
COMPND   6 SYNONYM: ROTAMASE PIN1, PPIASE PIN1;
COMPND   7 EC: 5.2.1.8;
COMPND   8 ENGINEERED: YES;
COMPND   9 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: PIN1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    SBDD, SMALL MOLECULE, PPIASE, CELL CYCLE, ISOMERASE,
KEYWDS   2 NUCLEUS, PHOSPHOPROTEIN, ROTAMASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.E.GREASLEY,R.A.FERRE
REVDAT   1   21-APR-10 3I6C    0
JRNL        AUTH   L.DONG,J.MARAKOVITS,X.HOU,C.GUO,S.GREASLEY,
JRNL        AUTH 2 E.DAGOSTINO,R.FERRE,M.C.JOHNSON,E.KRAYNOV,
JRNL        AUTH 3 J.THOMSON,V.PATHAK,B.W.MURRAY
JRNL        TITL   STRUCTURE-BASED DESIGN OF NOVEL HUMAN PIN1
JRNL        TITL 2 INHIBITORS (II).
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  20  2210 2010
JRNL        REFN                   ISSN 0960-894X
JRNL        PMID   20207139
JRNL        DOI    10.1016/J.BMCL.2010.02.033
REMARK   2
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.2
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.164
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.214
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.300
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2634
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 50063
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.152
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.200
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.200
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 2208
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 42647
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 1756
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 58
REMARK   3   SOLVENT ATOMS      : 166
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1999.00
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 4
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 18012
REMARK   3   NUMBER OF RESTRAINTS                     : 22438
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.011
REMARK   3   ANGLE DISTANCES                      (A) : 0.029
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.031
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.057
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.071
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.019
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.040
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.088
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3I6C COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB054019.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-JAN-02
REMARK 200  TEMPERATURE           (KELVIN) : 93
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 5.0.1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52797
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : 2.900
REMARK 200  R MERGE                    (I) : 0.06400
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.32
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.46800
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: ARP/WARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.9M NA
REMARK 280  CITRATE, 5MM TCEP, 100MM HEPES, PH 8.0, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 286K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,Y,-Z
REMARK 290       3555   X+1/2,Y+1/2,Z
REMARK 290       4555   -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   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        0.00000
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       58.98350
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       18.32400
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       58.98350
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       18.32400
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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: 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 350
REMARK 350 BIOMOLECULE: 2
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: B
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     GLY A    41
REMARK 465     SER A    42
REMARK 465     HIS A    43
REMARK 465     MET A    44
REMARK 465     GLY A    45
REMARK 465     LYS A    46
REMARK 465     ASN A    47
REMARK 465     GLY A    48
REMARK 465     GLN A    49
REMARK 465     GLY A    50
REMARK 465     GLY B    41
REMARK 465     SER B    42
REMARK 465     HIS B    43
REMARK 465     MET B    44
REMARK 465     GLY B    45
REMARK 465     LYS B    46
REMARK 465     ASN B    47
REMARK 465     GLY B    48
REMARK 465     GLN B    49
REMARK 465     GLY B    50
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     ARG A  68    NE   CZ   NH1  NH2
REMARK 470     ARG A  69    NE   CZ   NH1  NH2
REMARK 470     ARG A 142    NE   CZ   NH1  NH2
REMARK 470     GLU B  76    CD   OE1  OE2
REMARK 470     GLN B  94    CG   CD   OE1  NE2
REMARK 470     GLN B 131    CG   CD   OE1  NE2
REMARK 470     LYS B 132    CD   CE   NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU B  51   CD    GLU B  51   OE2     0.066
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   ATM2   ATM3
REMARK 500    PHE A 103   CB  -  CG  -  CD1 ANGL. DEV. =   6.3 DEGREES
REMARK 500    PHE B 103   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    PHE B 103   CB  -  CG  -  CD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     GIA A  301
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GIA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GIA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GIA B 302
DBREF  3I6C A   45   163  UNP    Q13526   PIN1_HUMAN      45    163
DBREF  3I6C B   45   163  UNP    Q13526   PIN1_HUMAN      45    163
SEQADV 3I6C GLY A   41  UNP  Q13526              EXPRESSION TAG
SEQADV 3I6C SER A   42  UNP  Q13526              EXPRESSION TAG
SEQADV 3I6C HIS A   43  UNP  Q13526              EXPRESSION TAG
SEQADV 3I6C MET A   44  UNP  Q13526              EXPRESSION TAG
SEQADV 3I6C GLN A   77  UNP  Q13526    LYS    77 ENGINEERED
SEQADV 3I6C GLN A   82  UNP  Q13526    LYS    82 ENGINEERED
SEQADV 3I6C GLY B   41  UNP  Q13526              EXPRESSION TAG
SEQADV 3I6C SER B   42  UNP  Q13526              EXPRESSION TAG
SEQADV 3I6C HIS B   43  UNP  Q13526              EXPRESSION TAG
SEQADV 3I6C MET B   44  UNP  Q13526              EXPRESSION TAG
SEQADV 3I6C GLN B   77  UNP  Q13526    LYS    77 ENGINEERED
SEQADV 3I6C GLN B   82  UNP  Q13526    LYS    82 ENGINEERED
SEQRES   1 A  123  GLY SER HIS MET GLY LYS ASN GLY GLN GLY GLU PRO ALA
SEQRES   2 A  123  ARG VAL ARG CYS SER HIS LEU LEU VAL LYS HIS SER GLN
SEQRES   3 A  123  SER ARG ARG PRO SER SER TRP ARG GLN GLU GLN ILE THR
SEQRES   4 A  123  ARG THR GLN GLU GLU ALA LEU GLU LEU ILE ASN GLY TYR
SEQRES   5 A  123  ILE GLN LYS ILE LYS SER GLY GLU GLU ASP PHE GLU SER
SEQRES   6 A  123  LEU ALA SER GLN PHE SER ASP CYS SER SER ALA LYS ALA
SEQRES   7 A  123  ARG GLY ASP LEU GLY ALA PHE SER ARG GLY GLN MET GLN
SEQRES   8 A  123  LYS PRO PHE GLU ASP ALA SER PHE ALA LEU ARG THR GLY
SEQRES   9 A  123  GLU MET SER GLY PRO VAL PHE THR ASP SER GLY ILE HIS
SEQRES  10 A  123  ILE ILE LEU ARG THR GLU
SEQRES   1 B  123  GLY SER HIS MET GLY LYS ASN GLY GLN GLY GLU PRO ALA
SEQRES   2 B  123  ARG VAL ARG CYS SER HIS LEU LEU VAL LYS HIS SER GLN
SEQRES   3 B  123  SER ARG ARG PRO SER SER TRP ARG GLN GLU GLN ILE THR
SEQRES   4 B  123  ARG THR GLN GLU GLU ALA LEU GLU LEU ILE ASN GLY TYR
SEQRES   5 B  123  ILE GLN LYS ILE LYS SER GLY GLU GLU ASP PHE GLU SER
SEQRES   6 B  123  LEU ALA SER GLN PHE SER ASP CYS SER SER ALA LYS ALA
SEQRES   7 B  123  ARG GLY ASP LEU GLY ALA PHE SER ARG GLY GLN MET GLN
SEQRES   8 B  123  LYS PRO PHE GLU ASP ALA SER PHE ALA LEU ARG THR GLY
SEQRES   9 B  123  GLU MET SER GLY PRO VAL PHE THR ASP SER GLY ILE HIS
SEQRES  10 B  123  ILE ILE LEU ARG THR GLU
HET    GIA  A 301       8
HET    GIA  A 303      25
HET    GIA  B 302      25
HETNAM     GIA 3-FLUORO-N-(NAPHTHALEN-2-YLCARBONYL)-D-PHENYLALANINE
FORMUL   3  GIA    3(C20 H16 F N O3)
FORMUL   6  HOH   *166(H2 O)
HELIX    1   1 THR A   81  GLY A   99  1                                  19
HELIX    2   2 ASP A  102  SER A  111  1                                  10
HELIX    3   3 CYS A  113  ARG A  119  5                                   7
HELIX    4   4 GLN A  131  LEU A  141  1                                  11
HELIX    5   5 THR B   81  SER B   98  1                                  18
HELIX    6   6 ASP B  102  SER B  111  1                                  10
HELIX    7   7 CYS B  113  ARG B  119  5                                   7
HELIX    8   8 GLN B  131  ALA B  140  1                                  10
SHEET    1   A 4 ASP A 121  SER A 126  0
SHEET    2   A 4 ARG A  54  VAL A  62 -1  N  CYS A  57   O  LEU A 122
SHEET    3   A 4 GLY A 155  GLU A 163 -1  O  ILE A 156   N  VAL A  62
SHEET    4   A 4 VAL A 150  THR A 152 -1  N  VAL A 150   O  HIS A 157
SHEET    1   B 4 ASP B 121  PHE B 125  0
SHEET    2   B 4 VAL B  55  VAL B  62 -1  N  VAL B  55   O  PHE B 125
SHEET    3   B 4 GLY B 155  GLU B 163 -1  O  ILE B 156   N  VAL B  62
SHEET    4   B 4 VAL B 150  THR B 152 -1  N  VAL B 150   O  HIS B 157
SITE     1 AC1  5 HIS A  59  GLN A 131  PHE A 134  SER A 154
SITE     2 AC1  5 HIS A 157
SITE     1 AC2 11 HOH A  38  ARG A  74  GLN A  75  ARG A  80
SITE     2 AC2 11 LEU A  88  PHE A 110  HOH A 168  GLN B  82
SITE     3 AC2 11 GLU B  83  LEU B  86  PHE B 151
SITE     1 AC3 11 HIS B  59  LEU B  61  LYS B  63  ARG B  68
SITE     2 AC3 11 CYS B 113  SER B 114  LEU B 122  PHE B 134
SITE     3 AC3 11 SER B 154  HOH B 171  HOH B 199
CRYST1  117.967   36.648   51.293  90.00 100.99  90.00 C 1 2 1       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      0.008477  0.000000  0.001646        0.00000
SCALE2      0.000000  0.027287  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019860        0.00000
      
PROCHECK
Go to PROCHECK summary
 References