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PDBsum entry 3fe4

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3fe4
Jmol
Contents
Protein chain
244 a.a.
Ligands
GOL ×2
Metals
_MG ×2
Waters ×429
HEADER    LYASE                                   27-NOV-08   3FE4
TITLE     CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE VI
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 6;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: CARBONIC ANHYDRASE VI, UNP RESIDUES 21-290;
COMPND   5 SYNONYM: CARBONIC ANHYDRASE VI, CA-VI, CARBONATE DEHYDRATASE VI,
COMPND   6 SECRETED CARBONIC ANHYDRASE, SALIVARY CARBONIC ANHYDRASE;
COMPND   7 EC: 4.2.1.1;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: CA6;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF
KEYWDS    CARBONIC ANHYDRASE, SECRETION, METAL BINDING, STRUCTURAL GENOMICS,
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC, GLYCOPROTEIN, LYASE, METAL-
KEYWDS   3 BINDING, SECRETED
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.S.PILKA,G.KOCHAN,E.KRYSZTOFINSKA,J.MUNIZ,W.W.YUE,A.K.ROOS,F.VON
AUTHOR   2 DELFT,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,C.BOUNTRA,U.OPPERMANN,
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT   4   27-NOV-13 3FE4    1       JRNL
REVDAT   3   13-JUL-11 3FE4    1       VERSN
REVDAT   2   10-FEB-09 3FE4    1       ATOM
REVDAT   1   16-DEC-08 3FE4    0
JRNL        AUTH   E.S.PILKA,G.KOCHAN,U.OPPERMANN,W.W.YUE
JRNL        TITL   CRYSTAL STRUCTURE OF THE SECRETORY ISOZYME OF MAMMALIAN
JRNL        TITL 2 CARBONIC ANHYDRASES CA VI: IMPLICATIONS FOR BIOLOGICAL
JRNL        TITL 3 ASSEMBLY AND INHIBITOR DEVELOPMENT
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 419   485 2012
JRNL        REFN                   ISSN 0006-291X
JRNL        PMID   22366092
JRNL        DOI    10.1016/J.BBRC.2012.02.038
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0055
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) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.27
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2
REMARK   3   NUMBER OF REFLECTIONS             : 41862
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) : 0.179
REMARK   3   R VALUE            (WORKING SET) : 0.177
REMARK   3   FREE R VALUE                     : 0.235
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2223
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) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2947
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.53
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2660
REMARK   3   BIN FREE R VALUE SET COUNT          : 171
REMARK   3   BIN FREE R VALUE                    : 0.3310
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3866
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 14
REMARK   3   SOLVENT ATOMS            : 427
REMARK   3
REMARK   3  B VALUES.
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.52
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.13000
REMARK   3    B22 (A**2) : -2.00000
REMARK   3    B33 (A**2) : 0.88000
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): 0.144
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.147
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.328
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4029 ; 0.016 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  2592 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5513 ; 1.562 ; 1.919
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6313 ; 0.930 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   497 ; 6.765 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   195 ;35.393 ;23.692
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   595 ;13.876 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;17.365 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   601 ; 0.103 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4537 ; 0.008 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   835 ; 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):  2457 ; 2.795 ; 3.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   984 ; 0.816 ; 3.000
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3987 ; 4.267 ; 5.000
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1572 ; 6.292 ; 7.000
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1520 ; 8.448 ;11.000
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL
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  : 2
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    32        A   279
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0292  53.7498 111.0246
REMARK   3    T TENSOR
REMARK   3      T11:   0.0268 T22:   0.0405
REMARK   3      T33:   0.0766 T12:   0.0032
REMARK   3      T13:  -0.0209 T23:  -0.0131
REMARK   3    L TENSOR
REMARK   3      L11:   0.5745 L22:   1.6332
REMARK   3      L33:   0.7634 L12:   0.0059
REMARK   3      L13:   0.1629 L23:  -0.0945
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0312 S12:   0.0092 S13:   0.0297
REMARK   3      S21:   0.1967 S22:   0.0068 S23:  -0.2097
REMARK   3      S31:  -0.0068 S32:   0.0670 S33:   0.0244
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    33        B   280
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8503  53.3444  82.0705
REMARK   3    T TENSOR
REMARK   3      T11:   0.0711 T22:   0.0314
REMARK   3      T33:   0.0142 T12:  -0.0036
REMARK   3      T13:  -0.0098 T23:  -0.0017
REMARK   3    L TENSOR
REMARK   3      L11:   0.6291 L22:   1.6176
REMARK   3      L33:   0.9441 L12:   0.0356
REMARK   3      L13:   0.1331 L23:  -0.0273
REMARK   3    S TENSOR
REMARK   3      S11:   0.0034 S12:   0.0648 S13:   0.0545
REMARK   3      S21:  -0.3117 S22:   0.0235 S23:   0.0354
REMARK   3      S31:   0.1028 S32:   0.0513 S33:  -0.0268
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.00
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 3FE4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-DEC-08.
REMARK 100 THE RCSB ID CODE IS RCSB050476.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X10SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99988
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : OSMIC
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41862
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.400
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3
REMARK 200  DATA REDUNDANCY                : 3.400
REMARK 200  R MERGE                    (I) : 0.08400
REMARK 200  R SYM                      (I) : 0.05200
REMARK 200   FOR THE DATA SET  : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.56500
REMARK 200  R SYM FOR SHELL            (I) : 0.36700
REMARK 200   FOR SHELL         : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1RJ5, 1JCZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 43.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16M MGCL2, 0.08M TRIS PH 8.5, 16% W/
REMARK 280  V PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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       25.82500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.72050
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.02400
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.72050
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.82500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.02400
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     MET A    20
REMARK 465     SER A    21
REMARK 465     ASP A    22
REMARK 465     TRP A    23
REMARK 465     THR A    24
REMARK 465     TYR A    25
REMARK 465     SER A    26
REMARK 465     GLU A    27
REMARK 465     GLY A    28
REMARK 465     ALA A    29
REMARK 465     LEU A    30
REMARK 465     ASP A    31
REMARK 465     ALA A   117
REMARK 465     SER A   118
REMARK 465     SER A   119
REMARK 465     GLU A   120
REMARK 465     ASN A   280
REMARK 465     GLN A   281
REMARK 465     GLU A   282
REMARK 465     TYR A   283
REMARK 465     THR A   284
REMARK 465     LEU A   285
REMARK 465     GLY A   286
REMARK 465     SER A   287
REMARK 465     GLU A   288
REMARK 465     PHE A   289
REMARK 465     GLN A   290
REMARK 465     ALA A   291
REMARK 465     GLU A   292
REMARK 465     ASN A   293
REMARK 465     LEU A   294
REMARK 465     TYR A   295
REMARK 465     PHE A   296
REMARK 465     GLN A   297
REMARK 465     MET B    20
REMARK 465     SER B    21
REMARK 465     ASP B    22
REMARK 465     TRP B    23
REMARK 465     THR B    24
REMARK 465     TYR B    25
REMARK 465     SER B    26
REMARK 465     GLU B    27
REMARK 465     GLY B    28
REMARK 465     ALA B    29
REMARK 465     LEU B    30
REMARK 465     ASP B    31
REMARK 465     GLU B    32
REMARK 465     ALA B   117
REMARK 465     SER B   118
REMARK 465     SER B   119
REMARK 465     GLN B   281
REMARK 465     GLU B   282
REMARK 465     TYR B   283
REMARK 465     THR B   284
REMARK 465     LEU B   285
REMARK 465     GLY B   286
REMARK 465     SER B   287
REMARK 465     GLU B   288
REMARK 465     PHE B   289
REMARK 465     GLN B   290
REMARK 465     ALA B   291
REMARK 465     GLU B   292
REMARK 465     ASN B   293
REMARK 465     LEU B   294
REMARK 465     TYR B   295
REMARK 465     PHE B   296
REMARK 465     GLN B   297
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     HIS A  34    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS A  56    CD   CE   NZ
REMARK 470     LYS A  64    CE   NZ
REMARK 470     GLU A  77    CD   OE1  OE2
REMARK 470     LYS A 147    CE   NZ
REMARK 470     GLU A 167    CG   CD   OE1  OE2
REMARK 470     LYS A 169    CG   CD   CE   NZ
REMARK 470     ASN A 170    CG   OD1  ND2
REMARK 470     ARG A 207    CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 210    CD   OE1  NE2
REMARK 470     ARG A 255    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 257    CG   CD   CE   NZ
REMARK 470     HIS A 260    CG   ND1  CD2  CE1  NE2
REMARK 470     ASN A 261    CG   OD1  ND2
REMARK 470     ASP A 262    CG   OD1  OD2
REMARK 470     HIS B  34    CG   ND1  CD2  CE1  NE2
REMARK 470     LYS B  56    CE   NZ
REMARK 470     LYS B  64    CG   CD   CE   NZ
REMARK 470     GLU B 120    CG   CD   OE1  OE2
REMARK 470     GLU B 167    CG   CD   OE1  OE2
REMARK 470     LYS B 169    NZ
REMARK 470     ASN B 170    CG   OD1  ND2
REMARK 470     ARG B 207    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG B 255    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B 257    CG   CD   CE   NZ
REMARK 470     ASN B 261    CG   OD1  ND2
REMARK 470     ASP B 262    CG   OD1  OD2
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   NH1  ARG A    46     O    HOH A   360              1.93
REMARK 500   OD2  ASP A   203     C1   GOL A   911              1.99
REMARK 500   NH1  ARG B    46     O    HOH B   348              2.08
REMARK 500   O    HOH B   342     O    HOH B   374              2.15
REMARK 500   OD2  ASP B   200     C3   GOL B   910              2.19
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    LYS A  64     -137.31   -109.88
REMARK 500    SER A 122       24.76   -143.68
REMARK 500    LYS A 169     -103.35   -154.87
REMARK 500    HIS A 260       79.50   -152.09
REMARK 500    ASN A 270     -119.36     61.11
REMARK 500    LYS B  64     -131.03   -108.46
REMARK 500    LYS B 169     -103.85   -160.61
REMARK 500    GLU B 226       57.95    -94.81
REMARK 500    ASN B 270     -118.54     57.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 PRO B  279     ASN B  280                  127.13
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 346        DISTANCE =  5.19 ANGSTROMS
REMARK 525    HOH A 455        DISTANCE =  5.68 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE 6-COORDINATED ION IN THE ACTIVE SITE (LINK RECORD BELOW) HAS
REMARK 600 BEEN IDENTIFIED AS MAGNESIUM FROM THE CRYSTALLISATION CONDITION.
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                              MG A 901  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 111   NE2
REMARK 620 2 HIS A 113   NE2  96.0
REMARK 620 3 HIS A 138   ND1 104.6  93.4
REMARK 620 4 HOH A 374   O    89.6 167.5  96.0
REMARK 620 5 HOH A 370   O    85.8  88.4 169.2  80.8
REMARK 620 6 HOH A 371   O   160.8  91.3  92.6  80.1  76.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG B 902  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 111   NE2
REMARK 620 2 HIS B 113   NE2  97.7
REMARK 620 3 HIS B 138   ND1 104.4  89.2
REMARK 620 4 HOH B 375   O    92.7 169.1  91.4
REMARK 620 5 HOH B 352   O   163.4  90.7  89.9  78.4
REMARK 620 6 HOH B 376   O    85.8  91.1 169.6  86.4  79.7
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 911
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 910
DBREF  3FE4 A   21   290  UNP    P23280   CAH6_HUMAN      21    290
DBREF  3FE4 B   21   290  UNP    P23280   CAH6_HUMAN      21    290
SEQADV 3FE4 MET A   20  UNP  P23280              INITIATING METHIONINE
SEQADV 3FE4 ALA A  291  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 GLU A  292  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 ASN A  293  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 LEU A  294  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 TYR A  295  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 PHE A  296  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 GLN A  297  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 MET B   20  UNP  P23280              INITIATING METHIONINE
SEQADV 3FE4 ALA B  291  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 GLU B  292  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 ASN B  293  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 LEU B  294  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 TYR B  295  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 PHE B  296  UNP  P23280              EXPRESSION TAG
SEQADV 3FE4 GLN B  297  UNP  P23280              EXPRESSION TAG
SEQRES   1 A  278  MET SER ASP TRP THR TYR SER GLU GLY ALA LEU ASP GLU
SEQRES   2 A  278  ALA HIS TRP PRO GLN HIS TYR PRO ALA CYS GLY GLY GLN
SEQRES   3 A  278  ARG GLN SER PRO ILE ASN LEU GLN ARG THR LYS VAL ARG
SEQRES   4 A  278  TYR ASN PRO SER LEU LYS GLY LEU ASN MET THR GLY TYR
SEQRES   5 A  278  GLU THR GLN ALA GLY GLU PHE PRO MET VAL ASN ASN GLY
SEQRES   6 A  278  HIS THR VAL GLN ILE SER LEU PRO SER THR MET ARG MET
SEQRES   7 A  278  THR VAL ALA ASP GLY THR VAL TYR ILE ALA GLN GLN MET
SEQRES   8 A  278  HIS PHE HIS TRP GLY GLY ALA SER SER GLU ILE SER GLY
SEQRES   9 A  278  SER GLU HIS THR VAL ASP GLY ILE ARG HIS VAL ILE GLU
SEQRES  10 A  278  ILE HIS ILE VAL HIS TYR ASN SER LYS TYR LYS SER TYR
SEQRES  11 A  278  ASP ILE ALA GLN ASP ALA PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 A  278  ALA ALA PHE VAL GLU VAL LYS ASN TYR PRO GLU ASN THR
SEQRES  13 A  278  TYR TYR SER ASN PHE ILE SER HIS LEU ALA ASN ILE LYS
SEQRES  14 A  278  TYR PRO GLY GLN ARG THR THR LEU THR GLY LEU ASP VAL
SEQRES  15 A  278  GLN ASP MET LEU PRO ARG ASN LEU GLN HIS TYR TYR THR
SEQRES  16 A  278  TYR HIS GLY SER LEU THR THR PRO PRO CYS THR GLU ASN
SEQRES  17 A  278  VAL HIS TRP PHE VAL LEU ALA ASP PHE VAL LYS LEU SER
SEQRES  18 A  278  ARG THR GLN VAL TRP LYS LEU GLU ASN SER LEU LEU ASP
SEQRES  19 A  278  HIS ARG ASN LYS THR ILE HIS ASN ASP TYR ARG ARG THR
SEQRES  20 A  278  GLN PRO LEU ASN HIS ARG VAL VAL GLU SER ASN PHE PRO
SEQRES  21 A  278  ASN GLN GLU TYR THR LEU GLY SER GLU PHE GLN ALA GLU
SEQRES  22 A  278  ASN LEU TYR PHE GLN
SEQRES   1 B  278  MET SER ASP TRP THR TYR SER GLU GLY ALA LEU ASP GLU
SEQRES   2 B  278  ALA HIS TRP PRO GLN HIS TYR PRO ALA CYS GLY GLY GLN
SEQRES   3 B  278  ARG GLN SER PRO ILE ASN LEU GLN ARG THR LYS VAL ARG
SEQRES   4 B  278  TYR ASN PRO SER LEU LYS GLY LEU ASN MET THR GLY TYR
SEQRES   5 B  278  GLU THR GLN ALA GLY GLU PHE PRO MET VAL ASN ASN GLY
SEQRES   6 B  278  HIS THR VAL GLN ILE SER LEU PRO SER THR MET ARG MET
SEQRES   7 B  278  THR VAL ALA ASP GLY THR VAL TYR ILE ALA GLN GLN MET
SEQRES   8 B  278  HIS PHE HIS TRP GLY GLY ALA SER SER GLU ILE SER GLY
SEQRES   9 B  278  SER GLU HIS THR VAL ASP GLY ILE ARG HIS VAL ILE GLU
SEQRES  10 B  278  ILE HIS ILE VAL HIS TYR ASN SER LYS TYR LYS SER TYR
SEQRES  11 B  278  ASP ILE ALA GLN ASP ALA PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 B  278  ALA ALA PHE VAL GLU VAL LYS ASN TYR PRO GLU ASN THR
SEQRES  13 B  278  TYR TYR SER ASN PHE ILE SER HIS LEU ALA ASN ILE LYS
SEQRES  14 B  278  TYR PRO GLY GLN ARG THR THR LEU THR GLY LEU ASP VAL
SEQRES  15 B  278  GLN ASP MET LEU PRO ARG ASN LEU GLN HIS TYR TYR THR
SEQRES  16 B  278  TYR HIS GLY SER LEU THR THR PRO PRO CYS THR GLU ASN
SEQRES  17 B  278  VAL HIS TRP PHE VAL LEU ALA ASP PHE VAL LYS LEU SER
SEQRES  18 B  278  ARG THR GLN VAL TRP LYS LEU GLU ASN SER LEU LEU ASP
SEQRES  19 B  278  HIS ARG ASN LYS THR ILE HIS ASN ASP TYR ARG ARG THR
SEQRES  20 B  278  GLN PRO LEU ASN HIS ARG VAL VAL GLU SER ASN PHE PRO
SEQRES  21 B  278  ASN GLN GLU TYR THR LEU GLY SER GLU PHE GLN ALA GLU
SEQRES  22 B  278  ASN LEU TYR PHE GLN
HET     MG  A 901       1
HET    GOL  A 911       6
HET     MG  B 902       1
HET    GOL  B 910       6
HETNAM      MG MAGNESIUM ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3   MG    2(MG 2+)
FORMUL   4  GOL    2(C3 H8 O3)
FORMUL   7  HOH   *427(H2 O)
HELIX    1   1 HIS A   34  TYR A   39  1                                   6
HELIX    2   2 PRO A   40  GLY A   44  5                                   5
HELIX    3   3 GLN A   53  VAL A   57  5                                   5
HELIX    4   4 SER A  148  GLN A  153  1                                   6
HELIX    5   5 ASN A  174  TYR A  176  5                                   3
HELIX    6   6 TYR A  177  LEU A  184  1                                   8
HELIX    7   7 ALA A  185  LYS A  188  5                                   4
HELIX    8   8 ASP A  200  LEU A  205  1                                   6
HELIX    9   9 SER A  240  SER A  250  1                                  11
HELIX   10  10 HIS B   34  TYR B   39  1                                   6
HELIX   11  11 PRO B   40  GLY B   44  5                                   5
HELIX   12  12 GLN B   53  VAL B   57  5                                   5
HELIX   13  13 SER B  148  GLN B  153  1                                   6
HELIX   14  14 ASN B  174  TYR B  176  5                                   3
HELIX   15  15 TYR B  177  LEU B  184  1                                   8
HELIX   16  16 ALA B  185  LYS B  188  5                                   4
HELIX   17  17 ASP B  200  LEU B  205  1                                   6
HELIX   18  18 SER B  240  SER B  250  1                                  11
SHEET    1   A 2 ASN A  51  LEU A  52  0
SHEET    2   A 2 THR A 127  VAL A 128  1  O  THR A 127   N  LEU A  52
SHEET    1   B10 ARG A  58  TYR A  59  0
SHEET    2   B10 GLU A 275  SER A 276  1  O  SER A 276   N  ARG A  58
SHEET    3   B10 TYR A 212  GLY A 217 -1  N  THR A 214   O  GLU A 275
SHEET    4   B10 VAL A 228  LEU A 233 -1  O  VAL A 228   N  GLY A 217
SHEET    5   B10 LEU A 159  GLU A 167  1  N  ALA A 163   O  PHE A 231
SHEET    6   B10 ILE A 135  ASN A 143 -1  N  ILE A 137   O  ALA A 164
SHEET    7   B10 VAL A 104  TRP A 114 -1  N  ILE A 106   O  TYR A 142
SHEET    8   B10 VAL A  87  SER A  90 -1  N  ILE A  89   O  MET A 110
SHEET    9   B10 GLN A  74  ASN A  82 -1  N  VAL A  81   O  GLN A  88
SHEET   10   B10 ARG A 193  LEU A 199 -1  O  THR A 194   N  MET A  80
SHEET    1   C 6 MET A  68  THR A  69  0
SHEET    2   C 6 ARG A  96  THR A  98 -1  O  ARG A  96   N  THR A  69
SHEET    3   C 6 VAL A 104  TRP A 114 -1  O  TYR A 105   N  MET A  97
SHEET    4   C 6 ILE A 135  ASN A 143 -1  O  TYR A 142   N  ILE A 106
SHEET    5   C 6 LEU A 159  GLU A 167 -1  O  ALA A 164   N  ILE A 137
SHEET    6   C 6 VAL A 237  LYS A 238  1  O  VAL A 237   N  PHE A 165
SHEET    1   D 2 ASN B  51  LEU B  52  0
SHEET    2   D 2 THR B 127  VAL B 128  1  O  THR B 127   N  LEU B  52
SHEET    1   E10 ARG B  58  TYR B  59  0
SHEET    2   E10 GLU B 275  SER B 276  1  O  SER B 276   N  ARG B  58
SHEET    3   E10 TYR B 212  GLY B 217 -1  N  THR B 214   O  GLU B 275
SHEET    4   E10 VAL B 228  LEU B 233 -1  O  VAL B 232   N  TYR B 213
SHEET    5   E10 LEU B 159  GLU B 167  1  N  ALA B 163   O  PHE B 231
SHEET    6   E10 ILE B 135  ASN B 143 -1  N  ILE B 137   O  ALA B 164
SHEET    7   E10 VAL B 104  TRP B 114 -1  N  ILE B 106   O  TYR B 142
SHEET    8   E10 VAL B  87  SER B  90 -1  N  ILE B  89   O  MET B 110
SHEET    9   E10 GLN B  74  ASN B  82 -1  N  PRO B  79   O  SER B  90
SHEET   10   E10 ARG B 193  LEU B 199 -1  O  THR B 194   N  MET B  80
SHEET    1   F 5 ARG B  96  THR B  98  0
SHEET    2   F 5 VAL B 104  TRP B 114 -1  O  TYR B 105   N  MET B  97
SHEET    3   F 5 ILE B 135  ASN B 143 -1  O  TYR B 142   N  ILE B 106
SHEET    4   F 5 LEU B 159  GLU B 167 -1  O  ALA B 164   N  ILE B 137
SHEET    5   F 5 VAL B 237  LYS B 238  1  O  VAL B 237   N  PHE B 165
SSBOND   1 CYS A   42    CYS A  224                          1555   1555  2.08
SSBOND   2 CYS B   42    CYS B  224                          1555   1555  2.08
LINK         NE2 HIS A 111                MG    MG A 901     1555   1555  2.18
LINK         NE2 HIS A 113                MG    MG A 901     1555   1555  2.20
LINK         ND1 HIS A 138                MG    MG A 901     1555   1555  2.15
LINK         NE2 HIS B 111                MG    MG B 902     1555   1555  2.07
LINK         NE2 HIS B 113                MG    MG B 902     1555   1555  2.19
LINK         ND1 HIS B 138                MG    MG B 902     1555   1555  2.20
LINK        MG    MG A 901                 O   HOH A 374     1555   1555  2.22
LINK        MG    MG A 901                 O   HOH A 370     1555   1555  2.01
LINK        MG    MG A 901                 O   HOH A 371     1555   1555  2.23
LINK        MG    MG B 902                 O   HOH B 375     1555   1555  2.22
LINK        MG    MG B 902                 O   HOH B 352     1555   1555  2.17
LINK        MG    MG B 902                 O   HOH B 376     1555   1555  2.07
CISPEP   1 SER A   48    PRO A   49          0        -1.88
CISPEP   2 PRO A  222    PRO A  223          0         7.03
CISPEP   3 SER B   48    PRO B   49          0         2.77
CISPEP   4 PRO B  222    PRO B  223          0        10.83
SITE     1 AC1  6 HIS A 111  HIS A 113  HIS A 138  HOH A 370
SITE     2 AC1  6 HOH A 371  HOH A 374
SITE     1 AC2  8 GLU A  72  THR A  73  TYR A 176  ASP A 200
SITE     2 AC2  8 GLN A 202  ASP A 203  GLU B 173  HOH B 393
SITE     1 AC3  6 HIS B 111  HIS B 113  HIS B 138  HOH B 352
SITE     2 AC3  6 HOH B 375  HOH B 376
SITE     1 AC4  5 GLU A 173  GLU B  72  ASP B 200  GLN B 202
SITE     2 AC4  5 ASP B 203
CRYST1   51.650   80.048  133.441  90.00  90.00  90.00 P 21 21 21    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      0.019361  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012493  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007494        0.00000
      
PROCHECK
Go to PROCHECK summary
 References