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PDBsum entry 1vai

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Top Page protein ligands Protein-protein interface(s) links
Isomerase PDB id
1vai
Jmol
Contents
Protein chains
166 a.a. *
Ligands
ACE-ALA-ALA-PRO-
ALA-MCM
Waters ×197
* Residue conservation analysis
HEADER    ISOMERASE                               17-FEB-04   1VAI
TITLE     STRUCTURE OF E. COLI CYCLOPHILIN B K163T MUTANT BOUND TO N-
TITLE    2 ACETYL-ALA-ALA-PRO-ALA-7-AMINO-4-METHYLCOUMARIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYCLOPHILIN B;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: PPIASE A, ROTAMASE A, CYCLOPHILIN A;
COMPND   5 EC: 5.2.1.8;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: (ACE)AAPA(MCM);
COMPND  10 CHAIN: C;
COMPND  11 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PATRP EPPIA;
SOURCE   9 MOL_ID: 2;
SOURCE  10 SYNTHETIC: YES;
SOURCE  11 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
KEYWDS    BETA BARREL, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.KONNO,Y.SANO,K.OKUDAIRA,Y.KAWAGUCHI,Y.YAMAGISHI-OHMORI,
AUTHOR   2 S.FUSHINOBU,H.MATSUZAWA
REVDAT   2   24-FEB-09 1VAI    1       VERSN
REVDAT   1   21-SEP-04 1VAI    0
JRNL        AUTH   M.KONNO,Y.SANO,K.OKUDAIRA,Y.KAWAGUCHI,
JRNL        AUTH 2 Y.YAMAGISHI-OHMORI,S.FUSHINOBU,H.MATSUZAWA
JRNL        TITL   ESCHERICHIA COLI CYCLOPHILIN B BINDS A HIGHLY
JRNL        TITL 2 DISTORTED FORM OF TRANS-PROLYL PEPTIDE ISOMER
JRNL        REF    EUR.J.BIOCHEM.                V. 271  3794 2004
JRNL        REFN                   ISSN 0014-2956
JRNL        PMID   15355356
JRNL        DOI    10.1111/J.1432-1033.2004.04321.X
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 34891
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.188
REMARK   3   FREE R VALUE                     : 0.229
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 3469
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2518
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 197
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.38
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.75
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1VAI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-04.
REMARK 100 THE RCSB ID CODE IS RCSB006407.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-98
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-6A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : WEISSENBERG
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35961
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.09000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.37100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1V9T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, PH 8.0, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.44000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       18.72000
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 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   2    CG   CD   CE   NZ
REMARK 470     ASP A   4    CG   OD1  OD2
REMARK 470     GLN A  65    CG   CD   OE1  NE2
REMARK 470     LYS A  68    CG   CD   CE   NZ
REMARK 470     LYS B   2    CG   CD   CE   NZ
REMARK 470     GLN B  23    CG   CD   OE1  NE2
REMARK 470     GLN B  30    CG   CD   OE1  NE2
REMARK 470     GLN B  63    CG   CD   OE1  NE2
REMARK 470     GLN B  65    CG   CD   OE1  NE2
REMARK 470     LYS B  68    CG   CD   CE   NZ
REMARK 470     LYS B  74    CG   CD   CE   NZ
REMARK 470     GLN B 117    CG   CD   OE1  NE2
REMARK 470     ARG B 118    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP B 119    CG   OD1  OD2
REMARK 470     LYS B 137    CG   CD   CE   NZ
REMARK 470     VAL B 146    CG1  CG2
REMARK 470     GLN B 150    CG   CD   OE1  NE2
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    ASP A   4      -59.49    162.37
REMARK 500    PHE A  53      -78.65   -135.89
REMARK 500    THR A  93     -157.40   -103.71
REMARK 500    THR A 100      -95.22   -127.86
REMARK 500    ASN A 110       73.15   -107.89
REMARK 500    LYS B   2       17.33     50.32
REMARK 500    ASP B   4      -66.30   -140.56
REMARK 500    PHE B  53      -76.50   -125.05
REMARK 500    ASP B  97       45.05   -107.36
REMARK 500    THR B 100      -90.89   -127.50
REMARK 500    ASN B 110       69.42   -101.43
REMARK 500    ALA C   3       88.65    179.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B 199        DISTANCE =  5.62 ANGSTROMS
REMARK 525    HOH B 211        DISTANCE =  5.59 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE C 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V9T   RELATED DB: PDB
REMARK 900 CYCLOPHILIN B K163T MUTANT BOUND TO SUCCINYL-ALA-PRO-ALA-P-
REMARK 900 NITROANILIDE
REMARK 900 RELATED ID: 1J2A   RELATED DB: PDB
REMARK 900 CYCLOPHILIN B K163T MUTANT
DBREF  1VAI A    1   166  UNP    P20752   PPIA_ECOLI      25    190
DBREF  1VAI B    1   166  UNP    P20752   PPIA_ECOLI      25    190
DBREF  1VAI C    1     6  PDB    1VAI     1VAI             1      6
SEQADV 1VAI THR A  163  UNP  P20752    LYS   187 ENGINEERED
SEQADV 1VAI THR B  163  UNP  P20752    LYS   187 ENGINEERED
SEQRES   1 A  166  ALA LYS GLY ASP PRO HIS VAL LEU LEU THR THR SER ALA
SEQRES   2 A  166  GLY ASN ILE GLU LEU GLU LEU ASP LYS GLN LYS ALA PRO
SEQRES   3 A  166  VAL SER VAL GLN ASN PHE VAL ASP TYR VAL ASN SER GLY
SEQRES   4 A  166  PHE TYR ASN ASN THR THR PHE HIS ARG VAL ILE PRO GLY
SEQRES   5 A  166  PHE MET ILE GLN GLY GLY GLY PHE THR GLU GLN MET GLN
SEQRES   6 A  166  GLN LYS LYS PRO ASN PRO PRO ILE LYS ASN GLU ALA ASP
SEQRES   7 A  166  ASN GLY LEU ARG ASN THR ARG GLY THR ILE ALA MET ALA
SEQRES   8 A  166  ARG THR ALA ASP LYS ASP SER ALA THR SER GLN PHE PHE
SEQRES   9 A  166  ILE ASN VAL ALA ASP ASN ALA PHE LEU ASP HIS GLY GLN
SEQRES  10 A  166  ARG ASP PHE GLY TYR ALA VAL PHE GLY LYS VAL VAL LYS
SEQRES  11 A  166  GLY MET ASP VAL ALA ASP LYS ILE SER GLN VAL PRO THR
SEQRES  12 A  166  HIS ASP VAL GLY PRO TYR GLN ASN VAL PRO SER LYS PRO
SEQRES  13 A  166  VAL VAL ILE LEU SER ALA THR VAL LEU PRO
SEQRES   1 B  166  ALA LYS GLY ASP PRO HIS VAL LEU LEU THR THR SER ALA
SEQRES   2 B  166  GLY ASN ILE GLU LEU GLU LEU ASP LYS GLN LYS ALA PRO
SEQRES   3 B  166  VAL SER VAL GLN ASN PHE VAL ASP TYR VAL ASN SER GLY
SEQRES   4 B  166  PHE TYR ASN ASN THR THR PHE HIS ARG VAL ILE PRO GLY
SEQRES   5 B  166  PHE MET ILE GLN GLY GLY GLY PHE THR GLU GLN MET GLN
SEQRES   6 B  166  GLN LYS LYS PRO ASN PRO PRO ILE LYS ASN GLU ALA ASP
SEQRES   7 B  166  ASN GLY LEU ARG ASN THR ARG GLY THR ILE ALA MET ALA
SEQRES   8 B  166  ARG THR ALA ASP LYS ASP SER ALA THR SER GLN PHE PHE
SEQRES   9 B  166  ILE ASN VAL ALA ASP ASN ALA PHE LEU ASP HIS GLY GLN
SEQRES  10 B  166  ARG ASP PHE GLY TYR ALA VAL PHE GLY LYS VAL VAL LYS
SEQRES  11 B  166  GLY MET ASP VAL ALA ASP LYS ILE SER GLN VAL PRO THR
SEQRES  12 B  166  HIS ASP VAL GLY PRO TYR GLN ASN VAL PRO SER LYS PRO
SEQRES  13 B  166  VAL VAL ILE LEU SER ALA THR VAL LEU PRO
SEQRES   1 C    6  ACE ALA ALA PRO ALA MCM
HET    ACE  C   1       3
HET    MCM  C   6      13
HETNAM     ACE ACETYL GROUP
HETNAM     MCM 7-AMINO-4-METHYL-CHROMEN-2-ONE
HETSYN     MCM 7-AMINO-4-METHYLCOUMARIN
FORMUL   3  ACE    C2 H4 O
FORMUL   3  MCM    C10 H9 N O2
FORMUL   4  HOH   *197(H2 O)
HELIX    1   1 ALA A   25  SER A   38  1                                  14
HELIX    2   2 GLU A   76  GLY A   80  5                                   5
HELIX    3   3 ASN A  110  ASP A  114  5                                   5
HELIX    4   4 GLY A  131  GLN A  140  1                                  10
HELIX    5   5 ALA B   25  SER B   38  1                                  14
HELIX    6   6 GLU B   76  GLY B   80  5                                   5
HELIX    7   7 ASN B  110  ASP B  114  5                                   5
HELIX    8   8 GLY B  131  GLN B  140  1                                  10
SHEET    1   A 9 THR A  44  THR A  45  0
SHEET    2   A 9 VAL A 158  VAL A 164 -1  O  ILE A 159   N  THR A  44
SHEET    3   A 9 HIS A   6  THR A  11 -1  N  THR A  10   O  SER A 161
SHEET    4   A 9 GLY A  14  LEU A  20 -1  O  ILE A  16   N  LEU A   9
SHEET    5   A 9 VAL A 124  LYS A 130 -1  O  LYS A 130   N  GLU A  17
SHEET    6   A 9 THR A  87  MET A  90 -1  N  ILE A  88   O  PHE A 125
SHEET    7   A 9 PHE A 103  ASN A 106 -1  O  PHE A 104   N  ALA A  89
SHEET    8   A 9 MET A  54  GLY A  57 -1  N  GLY A  57   O  PHE A 103
SHEET    9   A 9 ARG A  48  ILE A  50 -1  N  ARG A  48   O  GLN A  56
SHEET    1   B 2 THR A 143  VAL A 146  0
SHEET    2   B 2 TYR A 149  PRO A 153 -1  O  TYR A 149   N  VAL A 146
SHEET    1   C 9 THR B  44  THR B  45  0
SHEET    2   C 9 VAL B 158  VAL B 164 -1  O  ILE B 159   N  THR B  44
SHEET    3   C 9 HIS B   6  THR B  11 -1  N  LEU B   8   O  THR B 163
SHEET    4   C 9 GLY B  14  LEU B  20 -1  O  LEU B  18   N  VAL B   7
SHEET    5   C 9 VAL B 124  LYS B 130 -1  O  LYS B 130   N  GLU B  17
SHEET    6   C 9 THR B  87  MET B  90 -1  N  ILE B  88   O  PHE B 125
SHEET    7   C 9 PHE B 103  ASN B 106 -1  O  PHE B 104   N  ALA B  89
SHEET    8   C 9 MET B  54  GLY B  57 -1  N  GLY B  57   O  PHE B 103
SHEET    9   C 9 ARG B  48  ILE B  50 -1  N  ARG B  48   O  GLN B  56
SHEET    1   D 2 THR B 143  VAL B 146  0
SHEET    2   D 2 TYR B 149  PRO B 153 -1  O  TYR B 149   N  VAL B 146
LINK         C   ACE C   1                 N   ALA C   2     1555   1555  1.34
LINK         C   ALA C   5                 N   MCM C   6     1555   1555  1.35
SITE     1 AC1  3 GLN B 102  HOH B 169  HOH B 193
CRYST1   78.730   78.730   56.160  90.00  90.00 120.00 P 32          6
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      0.012702  0.007333  0.000000        0.00000
SCALE2      0.000000  0.014667  0.000000        0.00000
SCALE3      0.000000  0.000000  0.017806        0.00000
      
PROCHECK
Go to PROCHECK summary
 References