spacer
spacer

PDBsum entry 1lop

Go to PDB code: 
Top Page protein ligands links
Isomerase/isomerase inhibitor PDB id
1lop
Jmol
Contents
Protein chain
164 a.a. *
Ligands
SIN-ALA-PRO-ALA-
NIT
Waters ×133
* Residue conservation analysis
HEADER    ISOMERASE/ISOMERASE INHIBITOR           17-JUN-96   1LOP
TITLE     CYCLOPHILIN A COMPLEXED WITH SUCCINYL-ALA-PRO-ALA-P-NITROANILIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYCLOPHILIN A;
COMPND   3 CHAIN: A;
COMPND   4 EC: 5.2.1.8;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: SUCCINYL-ALA-PRO-ALA-P-NITROANILIDE;
COMPND   7 CHAIN: B;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 MOL_ID: 2;
SOURCE   5 SYNTHETIC: YES
KEYWDS    ROTAMASE, ISOMERASE-ISOMERASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.KONNO
REVDAT   4   13-JUL-11 1LOP    1       VERSN
REVDAT   3   25-AUG-09 1LOP    1       SOURCE
REVDAT   2   24-FEB-09 1LOP    1       VERSN
REVDAT   1   23-DEC-96 1LOP    0
JRNL        AUTH   M.KONNO,M.ITO,T.HAYANO,N.TAKAHASHI
JRNL        TITL   THE SUBSTRATE-BINDING SITE IN ESCHERICHIA COLI CYCLOPHILIN A
JRNL        TITL 2 PREFERABLY RECOGNIZES A CIS-PROLINE ISOMER OR A HIGHLY
JRNL        TITL 3 DISTORTED FORM OF THE TRANS ISOMER.
JRNL        REF    J.MOL.BIOL.                   V. 256   897 1996
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   8601841
JRNL        DOI    10.1006/JMBI.1996.0136
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) : 5.00
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)   (%) : 79.0
REMARK   3   NUMBER OF REFLECTIONS             : 12783
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.176
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
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            : 1312
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 133
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.00
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) : 0.15
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) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 2.70
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
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 1LOP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 288
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                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : WEIS
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13690
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 79.0
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.06900
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE ISOMORPHOUS
REMARK 200  REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       33.16500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       20.01500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.11500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       20.01500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.16500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.11500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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    HIS A   5   NE2   HIS A   5   CD2    -0.069
REMARK 500    HIS A   8   NE2   HIS A   8   CD2    -0.067
REMARK 500    HIS A  42   NE2   HIS A  42   CD2    -0.072
REMARK 500    HIS A  92   NE2   HIS A  92   CD2    -0.070
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    ARG A  32   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES
REMARK 500    ARG A  32   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A  43   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG A  80   CG  -  CD  -  NE  ANGL. DEV. = -14.8 DEGREES
REMARK 500    ARG A  80   NE  -  CZ  -  NH1 ANGL. DEV. =   8.0 DEGREES
REMARK 500    ARG A  80   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.5 DEGREES
REMARK 500    TRP A 118   CD1 -  CG  -  CD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    TRP A 118   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 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        PSI       PHI
REMARK 500    PHE A  48      -76.59   -139.61
REMARK 500    ARG A  87     -169.73   -163.34
REMARK 500    HIS A  92       44.77   -101.90
REMARK 500    THR A  95      -85.13   -120.19
REMARK 500    ASN A 105       76.06   -110.18
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 A 377        DISTANCE =  7.13 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUCCINYL-ALA-PRO-ALA
REMARK 800  -P-NITROANILIDE
DBREF  1LOP A    1   164  UNP    P23869   PPIB_ECOLI       1    164
DBREF  1LOP B    0     4  PDB    1LOP     1LOP             0      4
SEQADV 1LOP GLU A  132  UNP  P23869    VAL   132 CONFLICT
SEQRES   1 A  164  MET VAL THR PHE HIS THR ASN HIS GLY ASP ILE VAL ILE
SEQRES   2 A  164  LYS THR PHE ASP ASP LYS ALA PRO GLU THR VAL LYS ASN
SEQRES   3 A  164  PHE LEU ASP TYR CYS ARG GLU GLY PHE TYR ASN ASN THR
SEQRES   4 A  164  ILE PHE HIS ARG VAL ILE ASN GLY PHE MET ILE GLN GLY
SEQRES   5 A  164  GLY GLY PHE GLU PRO GLY MET LYS GLN LYS ALA THR LYS
SEQRES   6 A  164  GLU PRO ILE LYS ASN GLU ALA ASN ASN GLY LEU LYS ASN
SEQRES   7 A  164  THR ARG GLY THR LEU ALA MET ALA ARG THR GLN ALA PRO
SEQRES   8 A  164  HIS SER ALA THR ALA GLN PHE PHE ILE ASN VAL VAL ASP
SEQRES   9 A  164  ASN ASP PHE LEU ASN PHE SER GLY GLU SER LEU GLN GLY
SEQRES  10 A  164  TRP GLY TYR CYS VAL PHE ALA GLU VAL VAL ASP GLY MET
SEQRES  11 A  164  ASP GLU VAL ASP LYS ILE LYS GLY VAL ALA THR GLY ARG
SEQRES  12 A  164  SER GLY MET HIS GLN ASP VAL PRO LYS GLU ASP VAL ILE
SEQRES  13 A  164  ILE GLU SER VAL THR VAL SER GLU
SEQRES   1 B    5  SIN ALA PRO ALA NIT
HET    SIN  B   0       7
HET    NIT  B   4      11
HETNAM     SIN SUCCINIC ACID
HETNAM     NIT 4-NITROANILINE
HETSYN     NIT PARANITROANILINE
FORMUL   2  SIN    C4 H6 O4
FORMUL   2  NIT    C6 H6 N2 O2
FORMUL   3  HOH   *133(H2 O)
HELIX    1  H1 PHE A   16  ALA A   20  5                                   5
HELIX    2  H2 PRO A   21  GLU A   33  1                                  13
HELIX    3  H3 ASN A  105  LEU A  108  5                                   4
HELIX    4  H4 GLY A  129  LYS A  137  1                                   9
SHEET    1   A 9 MET A   1  HIS A   5  0
SHEET    2   A 9 ASP A  10  THR A  15 -1  N  ILE A  13   O  VAL A   2
SHEET    3   A 9 CYS A 121  ASP A 128 -1  N  ASP A 128   O  VAL A  12
SHEET    4   A 9 GLY A  81  ALA A  86 -1  N  LEU A  83   O  PHE A 123
SHEET    5   A 9 GLN A  97  VAL A 102 -1  N  PHE A  99   O  ALA A  84
SHEET    6   A 9 MET A  49  GLY A  52 -1  N  GLY A  52   O  PHE A  98
SHEET    7   A 9 ASN A  38  VAL A  44 -1
SHEET    8   A 9 VAL A 155  SER A 163 -1
SHEET    9   A 9 MET A   1  HIS A   5 -1  N  HIS A   5   O  GLU A 158
SHEET    1   B 2 GLY A 142  ARG A 143  0
SHEET    2   B 2 GLN A 148  ASP A 149 -1
LINK         C4  SIN B   0                 N   ALA B   1     1555   1555  1.32
LINK         N1  NIT B   4                 C   ALA B   3     1555   1555  1.34
CISPEP   1 ALA B    1    PRO B    2          0         1.25
SITE     1 AC1 19 ARG A  43  ILE A  45  PHE A  48  MET A  49
SITE     2 AC1 19 ALA A  86  ARG A  87  THR A  88  ALA A  90
SITE     3 AC1 19 HIS A  92  SER A  93  PHE A  99  ASP A 106
SITE     4 AC1 19 PHE A 107  TYR A 120  HOH A 277  HOH B 299
SITE     5 AC1 19 HOH B 349  HOH B 354  HOH B 355
CRYST1   66.330   68.230   40.030  90.00  90.00  90.00 P 21 21 21    4
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      0.015076  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014656  0.000000        0.00000
SCALE3      0.000000  0.000000  0.024981        0.00000
      
PROCHECK
Go to PROCHECK summary
 References