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PDBsum entry 3oim

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Lyase PDB id
3oim
Jmol
Contents
Protein chain
258 a.a.
Ligands
VZ5
GOL
DMS
Metals
_ZN
Waters ×336
HEADER    LYASE                                   19-AUG-10   3OIM
TITLE     HUMAN CARBONIC ANHYDRASE II BOUND BY 2-ETHYLESTRADIOL 3-O-SULFAMATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONIC ANHYDRASE II, CA-II, CARBONATE DEHYDRATASE II,
COMPND   5 CARBONIC ANHYDRASE C, CAC;
COMPND   6 EC: 4.2.1.1;
COMPND   7 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: CA2;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    2-ETHYLESTRONE, ESTRADIOL, SULFAMATE, MIXED ALPHA-BETA, CARBON
KEYWDS   2 DIOXIDE/BICARBONATE CONVERSION, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.H.SIPPEL,B.A.STANDER,A.H.ROBBINS,C.K.TU,M.AGBANDJE-MCKENNA,
AUTHOR   2 D.N.SILVERMAN,A.M.JOUBERT,R.MCKENNA
REVDAT   1   06-JUL-11 3OIM    0
JRNL        AUTH   K.H.SIPPEL,B.A.STANDER,A.H.ROBBINS,C.K.TU,
JRNL        AUTH 2 M.AGBANDJE-MCKENNA,D.N.SILVERMAN,A.M.JOUBERT,R.MCKENNA
JRNL        TITL   CHARACTERIZATION OF CARBONIC ANHYDRASE ISOZYME SPECIFIC
JRNL        TITL 2 INHIBITION BY SULFAMATED 2-ETHYLESTRA COMPOUNDS
JRNL        REF    LETT.DRUG DES.DISCOVERY       V.   8       2011
JRNL        REFN                   ISSN 1570-1808
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   G.E.COZIER,M.P.LEESE,M.D.LLOYD,M.D.BAKER,N.THIYAGARAJAN,
REMARK   1  AUTH 2 K.R.ACHARYA,B.V.POTTER
REMARK   1  TITL   STRUCTURES OF HUMAN CARBONIC ANHYDRASE II/INHIBITOR
REMARK   1  TITL 2 COMPLEXES REVEAL A SECOND BINDING SITE FOR STEROIDAL AND
REMARK   1  TITL 3 NONSTEROIDAL INHIBITORS.
REMARK   1  REF    BIOCHEMISTRY                  V.  49  3464 2010
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1  PMID   20297840
REMARK   1  DOI    10.1021/BI902178W
REMARK   1 REFERENCE 2
REMARK   1  AUTH   C.GENIS,K.H.SIPPEL,N.CASE,W.CAO,B.S.AVVARU,L.J.TARTAGLIA,
REMARK   1  AUTH 2 L.GOVINDASAMY,C.TU,M.AGBANDJE-MCKENNA,D.N.SILVERMAN,
REMARK   1  AUTH 3 C.J.ROSSER,R.MCKENNA
REMARK   1  TITL   DESIGN OF A CARBONIC ANHYDRASE IX ACTIVE-SITE MIMIC TO
REMARK   1  TITL 2 SCREEN INHIBITORS FOR POSSIBLE ANTICANCER PROPERTIES.
REMARK   1  REF    BIOCHEMISTRY                  V.  48  1322 2009
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1  PMID   19170619
REMARK   1  DOI    10.1021/BI802035F
REMARK   2
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.3_467)
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) : 1.45
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.76
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.2
REMARK   3   NUMBER OF REFLECTIONS             : 39564
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.146
REMARK   3   R VALUE            (WORKING SET) : 0.144
REMARK   3   FREE R VALUE                     : 0.170
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020
REMARK   3   FREE R VALUE TEST SET COUNT      : 1985
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 23.7657 -  3.4910    0.99     2959   161  0.1422 0.1422
REMARK   3     2  3.4910 -  2.7723    0.99     2885   158  0.1258 0.1527
REMARK   3     3  2.7723 -  2.4222    0.99     2854   153  0.1237 0.1744
REMARK   3     4  2.4222 -  2.2010    0.98     2835   154  0.1229 0.1381
REMARK   3     5  2.2010 -  2.0433    0.97     2786   135  0.1312 0.1617
REMARK   3     6  2.0433 -  1.9229    0.96     2759   153  0.1308 0.1804
REMARK   3     7  1.9229 -  1.8266    0.94     2727   143  0.1240 0.1507
REMARK   3     8  1.8266 -  1.7471    0.94     2682   142  0.1260 0.1766
REMARK   3     9  1.7471 -  1.6799    0.94     2674   137  0.1300 0.1975
REMARK   3    10  1.6799 -  1.6219    0.93     2677   139  0.1657 0.1718
REMARK   3    11  1.6219 -  1.5712    0.92     2629   144  0.2158 0.3028
REMARK   3    12  1.5712 -  1.5263    0.91     2595   137  0.2928 0.3216
REMARK   3    13  1.5263 -  1.4861    0.89     2557   136  0.3773 0.3746
REMARK   3    14  1.4861 -  1.4500    0.69     1960    93  0.4885 0.4988
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 0.60
REMARK   3   SHRINKAGE RADIUS   : 0.41
REMARK   3   K_SOL              : 0.48
REMARK   3   B_SOL              : 62.40
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.650
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.28340
REMARK   3    B22 (A**2) : -1.43730
REMARK   3    B33 (A**2) : 1.15390
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.87850
REMARK   3    B23 (A**2) : 0.00000
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      :  0.013           2374
REMARK   3   ANGLE     :  1.697           3264
REMARK   3   CHIRALITY :  0.091            339
REMARK   3   PLANARITY :  0.011            429
REMARK   3   DIHEDRAL  : 13.636            917
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 5
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (chain A and resid 3:9)
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1353  -4.5125  10.6682
REMARK   3    T TENSOR
REMARK   3      T11:   0.1605 T22:   0.2381
REMARK   3      T33:   0.2929 T12:  -0.0095
REMARK   3      T13:   0.0583 T23:   0.0112
REMARK   3    L TENSOR
REMARK   3      L11:   0.0620 L22:   0.0170
REMARK   3      L33:   0.0703 L12:   0.0031
REMARK   3      L13:  -0.0050 L23:  -0.0005
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0189 S12:   0.1334 S13:  -0.2261
REMARK   3      S21:  -0.1915 S22:  -0.1443 S23:  -0.7730
REMARK   3      S31:   0.0223 S32:   0.4171 S33:  -0.0001
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (chain A and resid 10:45)
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9835  -2.8642  27.4936
REMARK   3    T TENSOR
REMARK   3      T11:   0.1178 T22:   0.1547
REMARK   3      T33:   0.1140 T12:   0.0201
REMARK   3      T13:   0.0127 T23:   0.0047
REMARK   3    L TENSOR
REMARK   3      L11:   0.5254 L22:   0.8620
REMARK   3      L33:   0.7795 L12:   0.0733
REMARK   3      L13:   0.5382 L23:  -0.3254
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1227 S12:  -0.2665 S13:  -0.0474
REMARK   3      S21:   0.1265 S22:   0.0901 S23:  -0.0644
REMARK   3      S31:  -0.0202 S32:   0.0289 S33:  -0.0001
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: (chain A and resid 46:87)
REMARK   3    ORIGIN FOR THE GROUP (A): -16.6978   6.7738  12.8420
REMARK   3    T TENSOR
REMARK   3      T11:   0.1830 T22:   0.1466
REMARK   3      T33:   0.1849 T12:   0.0070
REMARK   3      T13:  -0.0114 T23:   0.0101
REMARK   3    L TENSOR
REMARK   3      L11:   0.1535 L22:   0.3305
REMARK   3      L33:   0.3424 L12:   0.1137
REMARK   3      L13:   0.1286 L23:  -0.0420
REMARK   3    S TENSOR
REMARK   3      S11:   0.0593 S12:  -0.0139 S13:   0.1256
REMARK   3      S21:  -0.1038 S22:  -0.0078 S23:   0.0882
REMARK   3      S31:  -0.1727 S32:  -0.0484 S33:  -0.0001
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: (chain A and resid 88:251)
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2029  -3.6191  13.3621
REMARK   3    T TENSOR
REMARK   3      T11:   0.0989 T22:   0.0918
REMARK   3      T33:   0.0986 T12:  -0.0059
REMARK   3      T13:  -0.0021 T23:   0.0063
REMARK   3    L TENSOR
REMARK   3      L11:   0.7102 L22:   0.7665
REMARK   3      L33:   0.9773 L12:  -0.0540
REMARK   3      L13:   0.0928 L23:   0.1399
REMARK   3    S TENSOR
REMARK   3      S11:   0.0027 S12:   0.0289 S13:  -0.0271
REMARK   3      S21:  -0.1182 S22:   0.0146 S23:   0.0224
REMARK   3      S31:  -0.0056 S32:   0.0278 S33:   0.0000
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: (chain A and resid 252:261)
REMARK   3    ORIGIN FOR THE GROUP (A): -11.5222  -3.6266  34.6733
REMARK   3    T TENSOR
REMARK   3      T11:   0.1739 T22:   0.2777
REMARK   3      T33:   0.1512 T12:   0.0027
REMARK   3      T13:   0.0141 T23:  -0.0010
REMARK   3    L TENSOR
REMARK   3      L11:   0.0442 L22:   0.1119
REMARK   3      L33:   0.0837 L12:  -0.0611
REMARK   3      L13:   0.0223 L23:  -0.0026
REMARK   3    S TENSOR
REMARK   3      S11:   0.0451 S12:  -0.6772 S13:  -0.0222
REMARK   3      S21:   0.2243 S22:   0.0798 S23:   0.0169
REMARK   3      S31:   0.0386 S32:  -0.0556 S33:   0.0001
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: INDIVIDUAL COORDINATE, INDIVIDUAL
REMARK   3  ISOTROPIC ADP, TLS, OCCUPANCY, HYDROGEN WRITING
REMARK   4
REMARK   4 3OIM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB061162.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 05-JUN-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : OSMIC MIRROR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39564
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.2
REMARK 200  DATA REDUNDANCY                : 4.400
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.04500
REMARK 200   FOR THE DATA SET  : 29.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.26800
REMARK 200   FOR SHELL         : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.REFINE: 1.6.3_467)
REMARK 200 STARTING MODEL: PDB ENTRY 2ILI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 40.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM CITRATE, 100 MM TRIS, 7.5
REMARK 280  MM 2-ETHYLESTRADIOL 3-O-SULFAMATE, PH 8.0, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       20.62000
REMARK 290   SMTRY3   2  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 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 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     1
REMARK 465     SER A     2
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    ASN A  11       11.72   -140.35
REMARK 500    ARG A  27       55.32   -144.35
REMARK 500    ALA A  65     -174.03   -171.40
REMARK 500    LYS A 111       -2.87     73.54
REMARK 500    PHE A 176       73.13   -155.67
REMARK 500    ASN A 244       46.14    -93.48
REMARK 500    LYS A 252     -136.13     56.88
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 373        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH A 509        DISTANCE =  5.33 ANGSTROMS
REMARK 525    HOH A 524        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH A 558        DISTANCE =  5.70 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 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VZ5 A 263   N1
REMARK 620 2 HIS A  94   NE2 114.1
REMARK 620 3 HIS A  96   NE2 110.3 105.6
REMARK 620 4 HIS A 119   ND1 116.9 109.9  98.4
REMARK 620 N                    1     2     3
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 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VZ5 A 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 265
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OIK   RELATED DB: PDB
REMARK 900 RELATED ID: 3OIL   RELATED DB: PDB
REMARK 900 RELATED ID: 3OKU   RELATED DB: PDB
REMARK 900 RELATED ID: 3OKV   RELATED DB: PDB
DBREF  3OIM A    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQRES   1 A  260  MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN GLY PRO
SEQRES   2 A  260  GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA LYS GLY GLU
SEQRES   3 A  260  ARG GLN SER PRO VAL ASP ILE ASP THR HIS THR ALA LYS
SEQRES   4 A  260  TYR ASP PRO SER LEU LYS PRO LEU SER VAL SER TYR ASP
SEQRES   5 A  260  GLN ALA THR SER LEU ARG ILE LEU ASN ASN GLY HIS ALA
SEQRES   6 A  260  PHE ASN VAL GLU PHE ASP ASP SER GLN ASP LYS ALA VAL
SEQRES   7 A  260  LEU LYS GLY GLY PRO LEU ASP GLY THR TYR ARG LEU ILE
SEQRES   8 A  260  GLN PHE HIS PHE HIS TRP GLY SER LEU ASP GLY GLN GLY
SEQRES   9 A  260  SER GLU HIS THR VAL ASP LYS LYS LYS TYR ALA ALA GLU
SEQRES  10 A  260  LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY ASP PHE
SEQRES  11 A  260  GLY LYS ALA VAL GLN GLN PRO ASP GLY LEU ALA VAL LEU
SEQRES  12 A  260  GLY ILE PHE LEU LYS VAL GLY SER ALA LYS PRO GLY LEU
SEQRES  13 A  260  GLN LYS VAL VAL ASP VAL LEU ASP SER ILE LYS THR LYS
SEQRES  14 A  260  GLY LYS SER ALA ASP PHE THR ASN PHE ASP PRO ARG GLY
SEQRES  15 A  260  LEU LEU PRO GLU SER LEU ASP TYR TRP THR TYR PRO GLY
SEQRES  16 A  260  SER LEU THR THR PRO PRO LEU LEU GLU CYS VAL THR TRP
SEQRES  17 A  260  ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER GLU GLN
SEQRES  18 A  260  VAL LEU LYS PHE ARG LYS LEU ASN PHE ASN GLY GLU GLY
SEQRES  19 A  260  GLU PRO GLU GLU LEU MET VAL ASP ASN TRP ARG PRO ALA
SEQRES  20 A  260  GLN PRO LEU LYS ASN ARG GLN ILE LYS ALA SER PHE LYS
HET     ZN  A 262       1
HET    VZ5  A 263      26
HET    GOL  A 264       6
HET    DMS  A 265       4
HETNAM      ZN ZINC ION
HETNAM     VZ5 (14BETA,17ALPHA)-2-ETHYL-17-HYDROXYESTRA-1(10),2,4-
HETNAM   2 VZ5  TRIEN-3-YL SULFAMATE
HETNAM     GOL GLYCEROL
HETNAM     DMS DIMETHYL SULFOXIDE
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2   ZN    ZN 2+
FORMUL   3  VZ5    C20 H29 N O4 S
FORMUL   4  GOL    C3 H8 O3
FORMUL   5  DMS    C2 H6 O S
FORMUL   6  HOH   *303(H2 O)
HELIX    1   1 HIS A   15  ASP A   19  5                                   5
HELIX    2   2 PHE A   20  GLY A   25  5                                   6
HELIX    3   3 LYS A  127  GLY A  129  5                                   3
HELIX    4   4 ASP A  130  VAL A  135  1                                   6
HELIX    5   5 LYS A  154  GLY A  156  5                                   3
HELIX    6   6 LEU A  157  LEU A  164  1                                   8
HELIX    7   7 ASP A  165  LYS A  168  5                                   4
HELIX    8   8 ASP A  180  LEU A  185  5                                   6
HELIX    9   9 SER A  219  ARG A  227  1                                   9
SHEET    1   A 2 ASP A  32  ILE A  33  0
SHEET    2   A 2 THR A 108  VAL A 109  1  O  THR A 108   N  ILE A  33
SHEET    1   B10 LYS A  39  TYR A  40  0
SHEET    2   B10 LYS A 257  ALA A 258  1  O  ALA A 258   N  LYS A  39
SHEET    3   B10 TYR A 191  GLY A 196 -1  N  THR A 193   O  LYS A 257
SHEET    4   B10 VAL A 207  LEU A 212 -1  O  VAL A 207   N  GLY A 196
SHEET    5   B10 LEU A 141  VAL A 150  1  N  GLY A 145   O  ILE A 210
SHEET    6   B10 ALA A 116  ASN A 124 -1  N  LEU A 118   O  ILE A 146
SHEET    7   B10 TYR A  88  TRP A  97 -1  N  HIS A  94   O  HIS A 119
SHEET    8   B10 PHE A  66  PHE A  70 -1  N  VAL A  68   O  PHE A  93
SHEET    9   B10 SER A  56  ASN A  61 -1  N  LEU A  57   O  GLU A  69
SHEET   10   B10 SER A 173  ASP A 175 -1  O  ALA A 174   N  ILE A  59
SHEET    1   C 6 LYS A  45  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  82 -1  O  VAL A  78   N  SER A  50
SHEET    3   C 6 TYR A  88  TRP A  97 -1  O  TYR A  88   N  LEU A  79
SHEET    4   C 6 ALA A 116  ASN A 124 -1  O  HIS A 119   N  HIS A  94
SHEET    5   C 6 LEU A 141  VAL A 150 -1  O  ILE A 146   N  LEU A 118
SHEET    6   C 6 ILE A 216  VAL A 218  1  O  ILE A 216   N  PHE A 147
LINK        ZN    ZN A 262                 N1  VZ5 A 263     1555   1555  1.97
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.01
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.03
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.04
CISPEP   1 SER A   29    PRO A   30          0        -1.45
CISPEP   2 PRO A  201    PRO A  202          0         7.78
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  VZ5 A 263
SITE     1 AC2 13 HIS A  94  HIS A  96  HIS A 119  VAL A 121
SITE     2 AC2 13 PHE A 131  LEU A 141  LEU A 198  THR A 199
SITE     3 AC2 13 THR A 200  PRO A 201   ZN A 262  GOL A 264
SITE     4 AC2 13 HOH A 402
SITE     1 AC3 10 ASN A  62  HIS A  64  ALA A  65  ASN A  67
SITE     2 AC3 10 GLN A  92  HIS A  94  VZ5 A 263  HOH A 293
SITE     3 AC3 10 HOH A 385  HOH A 445
SITE     1 AC4  5 TYR A   7  ASP A 243  TRP A 245  PRO A 247
SITE     2 AC4  5 HOH A 551
CRYST1   42.187   41.240   71.341  90.00 103.95  90.00 P 1 21 1      2
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      0.023704  0.000000  0.005888        0.00000
SCALE2      0.000000  0.024248  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014443        0.00000
      
PROCHECK
Go to PROCHECK summary
 References