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PDBsum entry 3da2

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3da2
Jmol
Contents
Protein chain
262 a.a.
Ligands
4MD ×2
Metals
_ZN ×2
_CL ×2
Waters ×435
HEADER    LYASE                                   28-MAY-08   3DA2
TITLE     X-RAY STRUCTURE OF HUMAN CARBONIC ANHYDRASE 13 IN COMPLEX WITH
TITLE    2 INHIBITOR
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 13;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE XIII, CARBONATE DEHYDRATASE XIII, CA-
COMPND   5 XIII;
COMPND   6 EC: 4.2.1.1;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_TAXID: 9606;
SOURCE   4 GENE: CA13;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS    CARBONIC ANHYDRASE, SULFONAMIDE, SGC, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS   2 GENOMICS CONSORTIUM, LYASE, METAL-BINDING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    E.S.PILKA,S.S.PICAUD,W.W.YUE,O.N.F.KING,J.E.BRAY,P.FILIPPAKOPOULOS,
AUTHOR   2 A.K.ROOS,A.C.W.PIKE,F.VON DELFT,C.H.ARROWSMITH,M.WIKSTROM,
AUTHOR   3 A.M.EDWARDS,C.BOUNTRA,U.OPPERMANN,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR   4 (SGC)
REVDAT   3   13-JUL-11 3DA2    1       VERSN
REVDAT   2   24-FEB-09 3DA2    1       VERSN
REVDAT   1   15-JUL-08 3DA2    0
JRNL        AUTH   E.S.PILKA,S.S.PICAUD,W.W.YUE,O.N.F.KING,J.E.BRAY,
JRNL        AUTH 2 P.FILIPPAKOPOULOS,A.K.ROOS,A.C.W.PIKE,F.VON DELFT,
JRNL        AUTH 3 C.H.ARROWSMITH,M.WIKSTROM,A.M.EDWARDS,C.BOUNTRA,U.OPPERMANN
JRNL        TITL   X-RAY STRUCTURE OF HUMAN CARBONIC ANHYDRASE 13 IN COMPLEX
JRNL        TITL 2 WITH INHIBITOR.
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.4.0066
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) : 2.05
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0
REMARK   3   NUMBER OF REFLECTIONS             : 32583
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) : 0.162
REMARK   3   R VALUE            (WORKING SET) : 0.159
REMARK   3   FREE R VALUE                     : 0.221
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1734
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) : 2.05
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2359
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2050
REMARK   3   BIN FREE R VALUE SET COUNT          : 121
REMARK   3   BIN FREE R VALUE                    : 0.2950
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4063
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 50
REMARK   3   SOLVENT ATOMS            : 435
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) : 18.18
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.42000
REMARK   3    B22 (A**2) : 0.77000
REMARK   3    B33 (A**2) : -0.51000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.18000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.188
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.173
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.131
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.160
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4267 ; 0.013 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  2840 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5834 ; 1.523 ; 1.955
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6912 ; 0.918 ; 3.001
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   525 ;14.167 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   188 ;29.481 ;24.149
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   654 ;13.488 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;18.502 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   628 ; 0.089 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4778 ; 0.006 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):   846 ; 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):  2621 ; 2.176 ; 3.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1042 ; 0.628 ; 3.000
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4247 ; 3.411 ; 5.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1646 ; 5.499 ; 7.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1587 ; 7.239 ;11.000
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  : 8
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     1        A     6
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6740  30.8910  13.7670
REMARK   3    T TENSOR
REMARK   3      T11:   0.4662 T22:   0.2214
REMARK   3      T33:   0.3492 T12:   0.1191
REMARK   3      T13:   0.0256 T23:  -0.0049
REMARK   3    L TENSOR
REMARK   3      L11:  18.6081 L22:   7.9689
REMARK   3      L33:   1.0181 L12:   3.9647
REMARK   3      L13:  -4.0828 L23:   0.0636
REMARK   3    S TENSOR
REMARK   3      S11:   0.0414 S12:  -0.4526 S13:   0.5128
REMARK   3      S21:   0.0732 S22:  -0.1866 S23:   0.3975
REMARK   3      S31:  -1.2646 S32:  -0.1375 S33:   0.1451
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 :   A     7        A    59
REMARK   3    ORIGIN FOR THE GROUP (A):   6.6720  10.9410  16.2480
REMARK   3    T TENSOR
REMARK   3      T11:   0.0181 T22:   0.0508
REMARK   3      T33:  -0.0306 T12:  -0.0465
REMARK   3      T13:  -0.0327 T23:  -0.0160
REMARK   3    L TENSOR
REMARK   3      L11:   3.8443 L22:   1.9168
REMARK   3      L33:   2.5560 L12:  -0.1638
REMARK   3      L13:  -0.2163 L23:  -0.0023
REMARK   3    S TENSOR
REMARK   3      S11:   0.1093 S12:   0.1659 S13:  -0.1741
REMARK   3      S21:   0.0400 S22:  -0.2882 S23:  -0.0267
REMARK   3      S31:   0.0299 S32:  -0.1025 S33:   0.1788
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A    60        A   181
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7570  11.3970  21.4280
REMARK   3    T TENSOR
REMARK   3      T11:   0.0531 T22:   0.1799
REMARK   3      T33:   0.0030 T12:  -0.0635
REMARK   3      T13:   0.0261 T23:  -0.0390
REMARK   3    L TENSOR
REMARK   3      L11:   3.0672 L22:   1.3056
REMARK   3      L33:   3.3144 L12:  -0.6292
REMARK   3      L13:  -0.0557 L23:  -0.0062
REMARK   3    S TENSOR
REMARK   3      S11:   0.0168 S12:  -0.0040 S13:  -0.1774
REMARK   3      S21:   0.2409 S22:  -0.1459 S23:   0.2642
REMARK   3      S31:   0.0435 S32:  -0.6714 S33:   0.1291
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   182        A   261
REMARK   3    ORIGIN FOR THE GROUP (A):   0.1550   9.2300  14.7980
REMARK   3    T TENSOR
REMARK   3      T11:   0.0217 T22:   0.1297
REMARK   3      T33:  -0.0212 T12:  -0.0405
REMARK   3      T13:   0.0071 T23:  -0.0601
REMARK   3    L TENSOR
REMARK   3      L11:   3.8271 L22:   1.8905
REMARK   3      L33:   2.7166 L12:  -0.5577
REMARK   3      L13:  -0.1010 L23:   0.2021
REMARK   3    S TENSOR
REMARK   3      S11:   0.1153 S12:   0.3215 S13:  -0.2702
REMARK   3      S21:   0.0887 S22:  -0.2439 S23:   0.2081
REMARK   3      S31:   0.1058 S32:  -0.4317 S33:   0.1287
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     6        B    45
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8520 -20.1360  19.6390
REMARK   3    T TENSOR
REMARK   3      T11:   0.1187 T22:   0.0538
REMARK   3      T33:   0.0333 T12:  -0.0406
REMARK   3      T13:  -0.0155 T23:   0.0461
REMARK   3    L TENSOR
REMARK   3      L11:   2.5074 L22:   2.4529
REMARK   3      L33:   2.6110 L12:   0.6620
REMARK   3      L13:   0.0004 L23:  -0.3772
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0635 S12:  -0.2553 S13:  -0.4538
REMARK   3      S21:   0.1386 S22:   0.1519 S23:  -0.0114
REMARK   3      S31:   0.4568 S32:  -0.0983 S33:  -0.0884
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B    46        B   155
REMARK   3    ORIGIN FOR THE GROUP (A):  33.6900  -4.5550  14.9510
REMARK   3    T TENSOR
REMARK   3      T11:   0.0474 T22:   0.0391
REMARK   3      T33:  -0.0037 T12:  -0.0365
REMARK   3      T13:   0.0250 T23:   0.0058
REMARK   3    L TENSOR
REMARK   3      L11:   1.9185 L22:   2.9345
REMARK   3      L33:   2.2103 L12:   0.0695
REMARK   3      L13:   0.0885 L23:  -0.5462
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0682 S12:  -0.0209 S13:   0.1681
REMARK   3      S21:  -0.0463 S22:   0.2301 S23:   0.0369
REMARK   3      S31:  -0.1706 S32:  -0.0624 S33:  -0.1619
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   156        B   180
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0460   5.6600  27.6840
REMARK   3    T TENSOR
REMARK   3      T11:   0.3605 T22:   0.1521
REMARK   3      T33:   0.0580 T12:   0.1129
REMARK   3      T13:   0.0483 T23:  -0.0625
REMARK   3    L TENSOR
REMARK   3      L11:   3.6479 L22:   2.9722
REMARK   3      L33:   1.4562 L12:  -2.2877
REMARK   3      L13:   1.5165 L23:  -1.1897
REMARK   3    S TENSOR
REMARK   3      S11:  -0.2925 S12:  -0.1760 S13:   0.4024
REMARK   3      S21:   0.7678 S22:   0.3106 S23:   0.0363
REMARK   3      S31:  -0.7645 S32:  -0.2812 S33:  -0.0180
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   181        B   261
REMARK   3    ORIGIN FOR THE GROUP (A):  36.4480  -9.1440  20.9300
REMARK   3    T TENSOR
REMARK   3      T11:   0.0460 T22:   0.0323
REMARK   3      T33:  -0.0272 T12:  -0.0032
REMARK   3      T13:   0.0000 T23:  -0.0058
REMARK   3    L TENSOR
REMARK   3      L11:   2.0489 L22:   2.5676
REMARK   3      L33:   2.6097 L12:   0.2621
REMARK   3      L13:   0.2870 L23:  -0.3758
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0814 S12:  -0.1764 S13:   0.0223
REMARK   3      S21:   0.1646 S22:   0.1604 S23:  -0.0946
REMARK   3      S31:  -0.0790 S32:  -0.0061 S33:  -0.0789
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 3DA2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-08.
REMARK 100 THE RCSB ID CODE IS RCSB047781.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.0
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) : 1.00001
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
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   : 32583
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.520
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.09600
REMARK 200  R SYM                      (I) : 0.05700
REMARK 200   FOR THE DATA SET  : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.62100
REMARK 200  R SYM FOR SHELL            (I) : 0.37200
REMARK 200   FOR SHELL         : 2.300
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 ENTRIES 1AZM,1ZH9,1FLJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 47.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M (NH4)2H(CITRATE),
REMARK 280  PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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       76.81850
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.56900
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       76.81850
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.56900
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     SER B     0
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     ARG B     3
REMARK 465     LEU B     4
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   3    NE   CZ   NH1  NH2
REMARK 470     LYS A  18    NZ
REMARK 470     LYS A  40    CE   NZ
REMARK 470     ARG A  46    NE   CZ   NH1  NH2
REMARK 470     LYS A  77    CE   NZ
REMARK 470     GLN A 159    CG   CD   OE1  NE2
REMARK 470     LYS A 214    CG   CD   CE   NZ
REMARK 470     GLU A 235    CG   CD   OE1  OE2
REMARK 470     LYS B  18    NZ
REMARK 470     PHE B  20    CG   CD1  CD2  CE1  CE2  CZ
REMARK 470     LYS B  37    CD   CE   NZ
REMARK 470     LYS B  40    CD   CE   NZ
REMARK 470     ARG B  46    NE   CZ   NH1  NH2
REMARK 470     LYS B  77    CE   NZ
REMARK 470     GLU B 153    CG   CD   OE1  OE2
REMARK 470     LYS B 160    CG   CD   CE   NZ
REMARK 470     LYS B 173    CD   CE   NZ
REMARK 470     LYS B 214    CE   NZ
REMARK 470     GLN B 222    CD   OE1  NE2
REMARK 470     GLU B 237    CG   CD   OE1  OE2
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   O    ARG B    46     O    HOH B   701              2.02
REMARK 500   O    HOH A   505     O    HOH B   685              2.03
REMARK 500   O    HOH A   430     O    HOH A   523              2.08
REMARK 500   ND2  ASN B   179     O    HOH B   577              2.12
REMARK 500   O    ASP B   181     O    HOH B   697              2.14
REMARK 500   CD2  LEU A    48     O    HOH A   588              2.15
REMARK 500   O    HOH B   608     O    HOH B   665              2.16
REMARK 500   OG   SER B    63     O    HOH B   612              2.17
REMARK 500   O    HOH A   405     O    HOH A   571              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    SER A   5       42.56   -103.81
REMARK 500    ASN A  76       40.28    -98.76
REMARK 500    LEU A 204       27.08     87.96
REMARK 500    ASN A 245       47.46   -149.72
REMARK 500    LYS B  58      -38.97   -131.97
REMARK 500    ARG B  92      -50.66   -126.86
REMARK 500    HIS B 104       68.68   -152.59
REMARK 500    LEU B 204       24.13     80.41
REMARK 500    ASN B 245       42.62   -143.04
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 A  203     LEU A  204                  136.51
REMARK 500 PRO B   31     ILE B   32                  143.83
REMARK 500 PRO B  203     LEU B  204                  140.76
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 499        DISTANCE =  5.59 ANGSTROMS
REMARK 525    HOH B 639        DISTANCE =  7.52 ANGSTROMS
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 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  97   NE2
REMARK 620 2 HIS A 120   ND1  98.2
REMARK 620 3 4MD A 401   S1B 138.6  98.8
REMARK 620 4 4MD A 401   N1K 116.5 117.5  24.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 301  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 4MD B 401   S1B
REMARK 620 2 4MD B 401   N1K  37.4
REMARK 620 N                    1
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4MD A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4MD B 401
DBREF  3DA2 A    1   261  UNP    Q8N1Q1   CAH13_HUMAN      1    261
DBREF  3DA2 B    1   261  UNP    Q8N1Q1   CAH13_HUMAN      1    261
SEQADV 3DA2 SER A    0  UNP  Q8N1Q1              EXPRESSION TAG
SEQADV 3DA2 SER B    0  UNP  Q8N1Q1              EXPRESSION TAG
SEQRES   1 A  262  SER MET SER ARG LEU SER TRP GLY TYR ARG GLU HIS ASN
SEQRES   2 A  262  GLY PRO ILE HIS TRP LYS GLU PHE PHE PRO ILE ALA ASP
SEQRES   3 A  262  GLY ASP GLN GLN SER PRO ILE GLU ILE LYS THR LYS GLU
SEQRES   4 A  262  VAL LYS TYR ASP SER SER LEU ARG PRO LEU SER ILE LYS
SEQRES   5 A  262  TYR ASP PRO SER SER ALA LYS ILE ILE SER ASN SER GLY
SEQRES   6 A  262  HIS SER PHE ASN VAL ASP PHE ASP ASP THR GLU ASN LYS
SEQRES   7 A  262  SER VAL LEU ARG GLY GLY PRO LEU THR GLY SER TYR ARG
SEQRES   8 A  262  LEU ARG GLN VAL HIS LEU HIS TRP GLY SER ALA ASP ASP
SEQRES   9 A  262  HIS GLY SER GLU HIS ILE VAL ASP GLY VAL SER TYR ALA
SEQRES  10 A  262  ALA GLU LEU HIS VAL VAL HIS TRP ASN SER ASP LYS TYR
SEQRES  11 A  262  PRO SER PHE VAL GLU ALA ALA HIS GLU PRO ASP GLY LEU
SEQRES  12 A  262  ALA VAL LEU GLY VAL PHE LEU GLN ILE GLY GLU PRO ASN
SEQRES  13 A  262  SER GLN LEU GLN LYS ILE THR ASP THR LEU ASP SER ILE
SEQRES  14 A  262  LYS GLU LYS GLY LYS GLN THR ARG PHE THR ASN PHE ASP
SEQRES  15 A  262  LEU LEU SER LEU LEU PRO PRO SER TRP ASP TYR TRP THR
SEQRES  16 A  262  TYR PRO GLY SER LEU THR VAL PRO PRO LEU LEU GLU SER
SEQRES  17 A  262  VAL THR TRP ILE VAL LEU LYS GLN PRO ILE ASN ILE SER
SEQRES  18 A  262  SER GLN GLN LEU ALA LYS PHE ARG SER LEU LEU CYS THR
SEQRES  19 A  262  ALA GLU GLY GLU ALA ALA ALA PHE LEU VAL SER ASN HIS
SEQRES  20 A  262  ARG PRO PRO GLN PRO LEU LYS GLY ARG LYS VAL ARG ALA
SEQRES  21 A  262  SER PHE
SEQRES   1 B  262  SER MET SER ARG LEU SER TRP GLY TYR ARG GLU HIS ASN
SEQRES   2 B  262  GLY PRO ILE HIS TRP LYS GLU PHE PHE PRO ILE ALA ASP
SEQRES   3 B  262  GLY ASP GLN GLN SER PRO ILE GLU ILE LYS THR LYS GLU
SEQRES   4 B  262  VAL LYS TYR ASP SER SER LEU ARG PRO LEU SER ILE LYS
SEQRES   5 B  262  TYR ASP PRO SER SER ALA LYS ILE ILE SER ASN SER GLY
SEQRES   6 B  262  HIS SER PHE ASN VAL ASP PHE ASP ASP THR GLU ASN LYS
SEQRES   7 B  262  SER VAL LEU ARG GLY GLY PRO LEU THR GLY SER TYR ARG
SEQRES   8 B  262  LEU ARG GLN VAL HIS LEU HIS TRP GLY SER ALA ASP ASP
SEQRES   9 B  262  HIS GLY SER GLU HIS ILE VAL ASP GLY VAL SER TYR ALA
SEQRES  10 B  262  ALA GLU LEU HIS VAL VAL HIS TRP ASN SER ASP LYS TYR
SEQRES  11 B  262  PRO SER PHE VAL GLU ALA ALA HIS GLU PRO ASP GLY LEU
SEQRES  12 B  262  ALA VAL LEU GLY VAL PHE LEU GLN ILE GLY GLU PRO ASN
SEQRES  13 B  262  SER GLN LEU GLN LYS ILE THR ASP THR LEU ASP SER ILE
SEQRES  14 B  262  LYS GLU LYS GLY LYS GLN THR ARG PHE THR ASN PHE ASP
SEQRES  15 B  262  LEU LEU SER LEU LEU PRO PRO SER TRP ASP TYR TRP THR
SEQRES  16 B  262  TYR PRO GLY SER LEU THR VAL PRO PRO LEU LEU GLU SER
SEQRES  17 B  262  VAL THR TRP ILE VAL LEU LYS GLN PRO ILE ASN ILE SER
SEQRES  18 B  262  SER GLN GLN LEU ALA LYS PHE ARG SER LEU LEU CYS THR
SEQRES  19 B  262  ALA GLU GLY GLU ALA ALA ALA PHE LEU VAL SER ASN HIS
SEQRES  20 B  262  ARG PRO PRO GLN PRO LEU LYS GLY ARG LYS VAL ARG ALA
SEQRES  21 B  262  SER PHE
HET     ZN  A 301       1
HET     ZN  B 301       1
HET     CL  B 302       1
HET     CL  B 303       1
HET    4MD  A 401      23
HET    4MD  B 401      23
HETNAM      ZN ZINC ION
HETNAM      CL CHLORIDE ION
HETNAM     4MD N-(4-CHLOROBENZYL)-N-METHYLBENZENE-1,4-DISULFONAMIDE
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5   CL    2(CL 1-)
FORMUL   7  4MD    2(C14 H15 CL N2 O4 S2)
FORMUL   9  HOH   *435(H2 O)
HELIX    1   1 GLY A   13  LYS A   18  1                                   6
HELIX    2   2 GLU A   19  PHE A   20  5                                   2
HELIX    3   3 PHE A   21  GLY A   26  5                                   6
HELIX    4   4 LYS A   35  VAL A   39  5                                   5
HELIX    5   5 ASP A   53  SER A   55  5                                   3
HELIX    6   6 SER A  131  ALA A  136  1                                   6
HELIX    7   7 LEU A  158  ASP A  163  1                                   6
HELIX    8   8 ASP A  181  LEU A  186  1                                   6
HELIX    9   9 SER A  220  SER A  229  1                                  10
HELIX   10  10 GLY B   13  PHE B   20  5                                   8
HELIX   11  11 PHE B   21  GLY B   26  5                                   6
HELIX   12  12 LYS B   35  VAL B   39  5                                   5
HELIX   13  13 ASP B   53  SER B   55  5                                   3
HELIX   14  14 SER B  131  HIS B  137  1                                   7
HELIX   15  15 GLN B  157  ASP B  163  1                                   7
HELIX   16  16 THR B  164  LYS B  169  5                                   6
HELIX   17  17 ASP B  181  LEU B  186  5                                   6
HELIX   18  18 SER B  220  ARG B  228  1                                   9
SHEET    1   A 2 GLU A  33  ILE A  34  0
SHEET    2   A 2 ILE A 109  VAL A 110  1  O  ILE A 109   N  ILE A  34
SHEET    1   B10 LYS A  40  TYR A  41  0
SHEET    2   B10 ARG A 258  ALA A 259  1  O  ALA A 259   N  LYS A  40
SHEET    3   B10 TYR A 192  GLY A 197 -1  N  THR A 194   O  ARG A 258
SHEET    4   B10 VAL A 208  LEU A 213 -1  O  VAL A 208   N  GLY A 197
SHEET    5   B10 LEU A 142  ILE A 151  1  N  GLY A 146   O  LEU A 213
SHEET    6   B10 ALA A 117  ASN A 125 -1  N  LEU A 119   O  VAL A 147
SHEET    7   B10 TYR A  89  TRP A  98 -1  N  GLN A  93   O  VAL A 122
SHEET    8   B10 PHE A  67  PHE A  71 -1  N  PHE A  71   O  ARG A  92
SHEET    9   B10 ALA A  57  ASN A  62 -1  N  LYS A  58   O  ASP A  70
SHEET   10   B10 GLN A 174  ARG A 176 -1  O  THR A 175   N  ILE A  60
SHEET    1   C 6 LEU A  48  LYS A  51  0
SHEET    2   C 6 VAL A  79  GLY A  82 -1  O  ARG A  81   N  SER A  49
SHEET    3   C 6 TYR A  89  TRP A  98 -1  O  TYR A  89   N  LEU A  80
SHEET    4   C 6 ALA A 117  ASN A 125 -1  O  VAL A 122   N  GLN A  93
SHEET    5   C 6 LEU A 142  ILE A 151 -1  O  VAL A 147   N  LEU A 119
SHEET    6   C 6 ILE A 217  ILE A 219  1  O  ILE A 217   N  GLN A 150
SHEET    1   D 2 GLU B  33  ILE B  34  0
SHEET    2   D 2 ILE B 109  VAL B 110  1  O  ILE B 109   N  ILE B  34
SHEET    1   E10 LYS B  40  TYR B  41  0
SHEET    2   E10 ARG B 258  ALA B 259  1  O  ALA B 259   N  LYS B  40
SHEET    3   E10 TYR B 192  GLY B 197 -1  N  THR B 194   O  ARG B 258
SHEET    4   E10 VAL B 208  LEU B 213 -1  O  VAL B 208   N  GLY B 197
SHEET    5   E10 LEU B 142  ILE B 151  1  N  GLY B 146   O  ILE B 211
SHEET    6   E10 ALA B 117  ASN B 125 -1  N  LEU B 119   O  VAL B 147
SHEET    7   E10 TYR B  89  TRP B  98 -1  N  GLN B  93   O  VAL B 122
SHEET    8   E10 PHE B  67  PHE B  71 -1  N  PHE B  71   O  ARG B  92
SHEET    9   E10 ALA B  57  ASN B  62 -1  N  ILE B  59   O  ASP B  70
SHEET   10   E10 GLN B 174  ARG B 176 -1  O  THR B 175   N  ILE B  60
SHEET    1   F 6 LEU B  48  LYS B  51  0
SHEET    2   F 6 VAL B  79  GLY B  82 -1  O  ARG B  81   N  SER B  49
SHEET    3   F 6 TYR B  89  TRP B  98 -1  O  TYR B  89   N  LEU B  80
SHEET    4   F 6 ALA B 117  ASN B 125 -1  O  VAL B 122   N  GLN B  93
SHEET    5   F 6 LEU B 142  ILE B 151 -1  O  VAL B 147   N  LEU B 119
SHEET    6   F 6 ILE B 217  ILE B 219  1  O  ILE B 217   N  GLN B 150
LINK         NE2 HIS A  97                ZN    ZN A 301     1555   1555  2.36
LINK         ND1 HIS A 120                ZN    ZN A 301     1555   1555  2.18
LINK        ZN    ZN A 301                 S1B 4MD A 401     1555   1555  2.83
LINK        ZN    ZN B 301                 S1B 4MD B 401     1555   1555  2.58
LINK        ZN    ZN A 301                 N1K 4MD A 401     1555   1555  1.43
LINK        ZN    ZN B 301                 N1K 4MD B 401     1555   1555  1.53
CISPEP   1 SER A   30    PRO A   31          0         0.45
CISPEP   2 PRO A  202    PRO A  203          0         6.90
CISPEP   3 SER B   30    PRO B   31          0         2.70
CISPEP   4 PRO B  202    PRO B  203          0        13.88
SITE     1 AC1  3 HIS A  95  HIS A  97  HIS A 120
SITE     1 AC2  3 HIS B  95  HIS B  97  HIS B 120
SITE     1 AC3  1 ARG B  90
SITE     1 AC4  2 ALA B 259  PHE B 261
SITE     1 AC5  9 GLN A  93  HIS A  95  HIS A  97  HIS A 120
SITE     2 AC5  9 PHE A 132  ALA A 136  HIS A 137  LEU A 199
SITE     3 AC5  9 THR A 200
SITE     1 AC6 11 GLN B  93  HIS B  95  HIS B  97  HIS B 120
SITE     2 AC6 11 PHE B 132  ALA B 136  HIS B 137  LEU B 199
SITE     3 AC6 11 THR B 200  PRO B 203  TRP B 210
CRYST1  153.637   45.138   87.938  90.00 116.28  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      0.006509  0.000000  0.003214        0.00000
SCALE2      0.000000  0.022155  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012682        0.00000
      
PROCHECK
Go to PROCHECK summary
 References