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PDBsum entry 4fru

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Isomerase PDB id
4fru
Jmol
Contents
Protein chain
185 a.a.
Ligands
ME2
PEG
Metals
_ZN ×2
Waters ×283
HEADER    ISOMERASE                               26-JUN-12   4FRU
TITLE     CRYSTAL STRUCTURE OF HORSE WILD-TYPE CYCLOPHILIN B
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CYCLOPHILIN B;
COMPND   5 EC: 5.2.1.8;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE   3 ORGANISM_COMMON: DOMESTIC HORSE,EQUINE;
SOURCE   4 ORGANISM_TAXID: 9796;
SOURCE   5 GENE: PPIB;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30B(+)
KEYWDS    CYCLOPHILIN-TYPE PPIASE, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE;
KEYWDS   2 CHAPERONE; FOLDASE, P3H1-CRTAP-CYPB COMPLEX; LH1 BINDING,
KEYWDS   3 ENDOPLASMIC RETICULUM, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.P.BOUDKO,Y.ISHIKAWA,H.P.BACHINGER
REVDAT   3   13-MAR-13 4FRU    1       REMARK
REVDAT   2   09-JAN-13 4FRU    1       JRNL
REVDAT   1   14-NOV-12 4FRU    0
JRNL        AUTH   S.P.BOUDKO,Y.ISHIKAWA,T.F.LERCH,J.NIX,M.S.CHAPMAN,
JRNL        AUTH 2 H.P.BACHINGER
JRNL        TITL   CRYSTAL STRUCTURES OF WILD-TYPE AND MUTATED CYCLOPHILIN B
JRNL        TITL 2 THAT CAUSES HYPERELASTOSIS CUTIS IN THE AMERICAN QUARTER
JRNL        TITL 3 HORSE.
JRNL        REF    BMC RES NOTES                 V.   5   626 2012
JRNL        REFN                   ESSN 1756-0500
JRNL        PMID   23137129
JRNL        DOI    10.1186/1756-0500-5-626
REMARK   2
REMARK   2 RESOLUTION.    1.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.42
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.2
REMARK   3   NUMBER OF REFLECTIONS             : 62351
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.117
REMARK   3   R VALUE            (WORKING SET) : 0.116
REMARK   3   FREE R VALUE                     : 0.139
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070
REMARK   3   FREE R VALUE TEST SET COUNT      : 3161
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 16.4181 -  3.1214    1.00     2958   145  0.1391 0.1483
REMARK   3     2  3.1214 -  2.4803    1.00     2885   155  0.1301 0.1545
REMARK   3     3  2.4803 -  2.1676    1.00     2858   154  0.1085 0.1301
REMARK   3     4  2.1676 -  1.9697    1.00     2894   129  0.0980 0.1152
REMARK   3     5  1.9697 -  1.8288    1.00     2873   151  0.0964 0.1241
REMARK   3     6  1.8288 -  1.7211    1.00     2857   169  0.0920 0.1072
REMARK   3     7  1.7211 -  1.6349    1.00     2837   139  0.0898 0.1072
REMARK   3     8  1.6349 -  1.5638    1.00     2843   153  0.0874 0.1139
REMARK   3     9  1.5638 -  1.5037    1.00     2846   169  0.0856 0.1285
REMARK   3    10  1.5037 -  1.4518    1.00     2838   163  0.0884 0.1099
REMARK   3    11  1.4518 -  1.4064    1.00     2831   165  0.0881 0.1287
REMARK   3    12  1.4064 -  1.3663    1.00     2815   179  0.0913 0.1182
REMARK   3    13  1.3663 -  1.3303    1.00     2871   147  0.0970 0.1294
REMARK   3    14  1.3303 -  1.2979    1.00     2863   115  0.0996 0.1353
REMARK   3    15  1.2979 -  1.2684    1.00     2824   142  0.1072 0.1293
REMARK   3    16  1.2684 -  1.2414    0.97     2781   163  0.1223 0.1674
REMARK   3    17  1.2414 -  1.2166    0.92     2605   147  0.1346 0.1912
REMARK   3    18  1.2166 -  1.1936    0.86     2410   148  0.1455 0.1733
REMARK   3    19  1.1936 -  1.1723    0.77     2212   104  0.1609 0.1925
REMARK   3    20  1.1723 -  1.1524    0.68     1897    95  0.1658 0.2102
REMARK   3    21  1.1524 -  1.1339    0.59     1695    92  0.1764 0.2159
REMARK   3    22  1.1339 -  1.1164    0.52     1449    81  0.1919 0.1995
REMARK   3    23  1.1164 -  1.1000    0.43     1248    56  0.2130 0.1861
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11
REMARK   3   SHRINKAGE RADIUS   : 0.90
REMARK   3   K_SOL              : NULL
REMARK   3   B_SOL              : NULL
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.070
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 11.540
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 4.20
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  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.007           1521
REMARK   3   ANGLE     :  1.301           2041
REMARK   3   CHIRALITY :  0.078            218
REMARK   3   PLANARITY :  0.006            260
REMARK   3   DIHEDRAL  : 11.819            588
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 4FRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073276.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-10
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : ALS
REMARK 200  BEAMLINE                       : 4.2.2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.827
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL
REMARK 200  OPTICS                         : ROSENBAUM-ROCK MONOCHROMATOR 1:
REMARK 200                                   HIGH-RESOLUTION DOUBLE-CRYSTAL
REMARK 200                                   SAGITTAL FOCUSING, ROSENBAUM-ROCK
REMARK 200                                   MONOCHROMATOR 2: DOUBLE CRYSTAL,
REMARK 200                                   ROSENBAUM-ROCK VERTICAL FOCUSING
REMARK 200                                   MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : NOIR-1
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62397
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 16.420
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.4
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : 0.07800
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.16
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.27200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1CYN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 10MM ZNCL2, 10% GLYCEROL,
REMARK 280  28% PEG MME 550, PH 7.2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 295.0K
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       32.44000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.03500
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       32.44000
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.03500
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: MONOMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH A 492  LIES ON A SPECIAL POSITION.
REMARK 375      HOH A 554  LIES ON A SPECIAL POSITION.
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   3    CG   CD   CE   NZ
REMARK 470     LYS A   4    CE   NZ
REMARK 470     LYS A  34    CE   NZ
REMARK 470     ARG A 157    NE   CZ   NH1  NH2
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  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   HZ1  LYS A    59     O    HOH A   486              1.58
REMARK 500   O    HOH A   487     O    HOH A   540              1.98
REMARK 500   O    HOH A   491     O    HOH A   537              2.06
REMARK 500   O    HOH A   550     O    HOH A   563              2.08
REMARK 500   O    HOH A   455     O    HOH A   456              2.08
REMARK 500   O    HOH A   523     O    HOH A   538              2.10
REMARK 500   O    HOH A   482     O    HOH A   520              2.15
REMARK 500   O    HOH A   523     O    HOH A   553              2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    HOH A   526     O    HOH A   526     2656     1.84
REMARK 500   O    HOH A   540     O    HOH A   545     2656     1.97
REMARK 500   O    HOH A   483     O    HOH A   485     3545     2.05
REMARK 500   O    HOH A   540     O    HOH A   555     3555     2.15
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  67      -74.72   -142.77
REMARK 500    PHE A 136       -2.53   -140.75
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 427        DISTANCE =  5.11 ANGSTROMS
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     PEG A  204
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                              ZN A 202  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  21   OD2
REMARK 620 2 HOH A 320   O    97.6
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 201  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 472   O
REMARK 620 2 HIS A 133   NE2 110.9
REMARK 620 3 HOH A 476   O    83.0  91.8
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ME2 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 204
DBREF  4FRU A    1   183  UNP    A5YBL8   A5YBL8_HORSE    34    216
SEQADV 4FRU ALA A   -1  UNP  A5YBL8              EXPRESSION TAG
SEQADV 4FRU MET A    0  UNP  A5YBL8              EXPRESSION TAG
SEQRES   1 A  185  ALA MET ASP GLU LYS LYS LYS GLY PRO LYS VAL THR VAL
SEQRES   2 A  185  LYS VAL TYR PHE ASP LEU ARG ILE GLY ASP GLU ASP ILE
SEQRES   3 A  185  GLY ARG VAL VAL ILE GLY LEU PHE GLY LYS THR VAL PRO
SEQRES   4 A  185  LYS THR VAL ASP ASN PHE VAL ALA LEU ALA THR GLY GLU
SEQRES   5 A  185  LYS GLY PHE GLY TYR LYS ASP SER LYS PHE HIS ARG VAL
SEQRES   6 A  185  ILE LYS ASP PHE MET ILE GLN GLY GLY ASP PHE THR ARG
SEQRES   7 A  185  GLY ASP GLY THR GLY GLY LYS SER ILE TYR GLY GLU ARG
SEQRES   8 A  185  PHE PRO ASP GLU ASN PHE LYS LEU LYS HIS TYR GLY PRO
SEQRES   9 A  185  GLY TRP VAL SER MET ALA ASN ALA GLY LYS ASP THR ASN
SEQRES  10 A  185  GLY SER GLN PHE PHE ILE THR THR VAL LYS THR ALA TRP
SEQRES  11 A  185  LEU ASP GLY LYS HIS VAL VAL PHE GLY LYS VAL LEU GLU
SEQRES  12 A  185  GLY MET GLU VAL VAL ARG LYS VAL GLU THR THR LYS THR
SEQRES  13 A  185  ASP GLY ARG ASP LYS PRO LEU LYS ASP VAL THR ILE ALA
SEQRES  14 A  185  ASP CYS GLY LYS ILE GLU VAL GLU LYS PRO PHE ALA ILE
SEQRES  15 A  185  ALA LYS GLU
HET     ZN  A 201       1
HET     ZN  A 202       1
HET    ME2  A 203      20
HET    PEG  A 204      11
HETNAM      ZN ZINC ION
HETNAM     ME2 1-ETHOXY-2-(2-METHOXYETHOXY)ETHANE
HETNAM     PEG DI(HYDROXYETHYL)ETHER
FORMUL   2   ZN    2(ZN 2+)
FORMUL   4  ME2    C7 H16 O3
FORMUL   5  PEG    C4 H10 O3
FORMUL   6  HOH   *283(H2 O)
HELIX    1   1 ASP A    1  LYS A    3  5                                   3
HELIX    2   2 VAL A   36  GLY A   49  1                                  14
HELIX    3   3 THR A  126  ASP A  130  5                                   5
HELIX    4   4 GLY A  142  THR A  151  1                                  10
SHEET    1   A 8 ARG A  62  ILE A  64  0
SHEET    2   A 8 MET A  68  GLY A  71 -1  O  GLN A  70   N  ARG A  62
SHEET    3   A 8 PHE A 119  THR A 122 -1  O  ILE A 121   N  ILE A  69
SHEET    4   A 8 TRP A 104  MET A 107 -1  N  TRP A 104   O  THR A 122
SHEET    5   A 8 VAL A 135  GLU A 141 -1  O  GLY A 137   N  VAL A 105
SHEET    6   A 8 GLU A  22  LEU A  31 -1  N  VAL A  28   O  LEU A 140
SHEET    7   A 8 LYS A   5  ILE A  19 -1  N  VAL A  13   O  ILE A  29
SHEET    8   A 8 VAL A 164  ALA A 181 -1  O  PHE A 178   N  VAL A   9
LINK         OD2 ASP A  21                ZN    ZN A 202     1555   1555  1.94
LINK        ZN    ZN A 202                 O   HOH A 320     1555   1555  1.99
LINK        ZN    ZN A 201                 O   HOH A 472     1555   1555  2.00
LINK         NE2 HIS A 133                ZN    ZN A 201     1555   1555  2.03
LINK        ZN    ZN A 201                 O   HOH A 476     1555   1555  2.23
SITE     1 AC1  4 ALA A  -1  HIS A 133  HOH A 472  HOH A 476
SITE     1 AC2  4 ASP A  21  ASP A  57  GLU A  88  HOH A 320
SITE     1 AC3  4 ILE A  19  GLY A  20  ASP A  21  LYS A 162
SITE     1 AC4  3 ASP A  57  ARG A  89  LYS A 162
CRYST1   64.880   44.070   60.570  90.00  95.20  90.00 C 1 2 1       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      0.015413  0.000000  0.001403        0.00000
SCALE2      0.000000  0.022691  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016578        0.00000
      
PROCHECK
Go to PROCHECK summary
 References