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PDBsum entry 3rg4

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Lyase PDB id
3rg4
Jmol
Contents
Protein chain
257 a.a.
Metals
_ZN
Waters ×201
HEADER    LYASE                                   07-APR-11   3RG4
TITLE     CRYSTAL STRUCTURE OF THE W5F MUTANT OF HUMAN CARBONIC ANHYDRASE II
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE C, CAC, CA-II;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: 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: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    ZINC METALLOENZYME, W5F MUTATION, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.F.DOMSIC,A.H.ROBBINS,R.MCKENNA
REVDAT   1   22-FEB-12 3RG4    0
JRNL        AUTH   R.MIKULSKI,J.F.DOMSIC,G.LING,C.TU,A.H.ROBBINS,D.N.SILVERMAN,
JRNL        AUTH 2 R.MCKENNA
JRNL        TITL   STRUCTURE AND CATALYSIS BY CARBONIC ANHYDRASE II: ROLE OF
JRNL        TITL 2 ACTIVE-SITE TRYPTOPHAN 5.
JRNL        REF    ARCH.BIOCHEM.BIOPHYS.         V. 516    97 2011
JRNL        REFN                   ISSN 0003-9861
JRNL        PMID   22001224
JRNL        DOI    10.1016/J.ABB.2011.09.011
REMARK   2
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 1.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.74
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.1
REMARK   3   NUMBER OF REFLECTIONS             : 34955
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.138
REMARK   3   R VALUE            (WORKING SET) : 0.136
REMARK   3   FREE R VALUE                     : 0.166
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1781
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 20.7395 -  3.5217    0.92     2744   151  0.1263 0.1453
REMARK   3     2  3.5217 -  2.7975    0.94     2749   152  0.1343 0.1665
REMARK   3     3  2.7975 -  2.4445    0.94     2731   139  0.1373 0.1667
REMARK   3     4  2.4445 -  2.2213    0.92     2681   146  0.1269 0.1674
REMARK   3     5  2.2213 -  2.0622    0.91     2625   143  0.1275 0.1520
REMARK   3     6  2.0622 -  1.9407    0.90     2610   137  0.1212 0.1391
REMARK   3     7  1.9407 -  1.8436    0.89     2602   119  0.1211 0.1595
REMARK   3     8  1.8436 -  1.7634    0.88     2509   133  0.1292 0.1449
REMARK   3     9  1.7634 -  1.6955    0.86     2475   137  0.1421 0.2021
REMARK   3    10  1.6955 -  1.6370    0.85     2465   129  0.1582 0.2015
REMARK   3    11  1.6370 -  1.5859    0.83     2361   134  0.1683 0.2116
REMARK   3    12  1.5859 -  1.5406    0.82     2363   126  0.2025 0.2490
REMARK   3    13  1.5406 -  1.5000    0.79     2259   135  0.2522 0.2629
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 0.50
REMARK   3   SHRINKAGE RADIUS   : 0.29
REMARK   3   K_SOL              : 0.47
REMARK   3   B_SOL              : 45.82
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.910
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.06
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.84430
REMARK   3    B22 (A**2) : -1.85160
REMARK   3    B33 (A**2) : -3.46490
REMARK   3    B12 (A**2) : -0.00000
REMARK   3    B13 (A**2) : -0.16640
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      :  0.010           2186
REMARK   3   ANGLE     :  1.272           2983
REMARK   3   CHIRALITY :  0.077            313
REMARK   3   PLANARITY :  0.007            390
REMARK   3   DIHEDRAL  : 13.248            808
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 10
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: chain 'A' and (resseq 4:24)
REMARK   3    ORIGIN FOR THE GROUP (A):   8.4179  -2.7074  16.1211
REMARK   3    T TENSOR
REMARK   3      T11:   0.0872 T22:   0.1972
REMARK   3      T33:   0.2285 T12:   0.0036
REMARK   3      T13:   0.0245 T23:  -0.0191
REMARK   3    L TENSOR
REMARK   3      L11:   0.2470 L22:   0.0998
REMARK   3      L33:   0.1390 L12:   0.1474
REMARK   3      L13:   0.0003 L23:  -0.0410
REMARK   3    S TENSOR
REMARK   3      S11:   0.0230 S12:   0.0626 S13:  -0.1946
REMARK   3      S21:   0.0455 S22:  -0.0455 S23:  -0.2225
REMARK   3      S31:   0.1133 S32:   0.1455 S33:  -0.0064
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: chain 'A' and (resseq 25:50)
REMARK   3    ORIGIN FOR THE GROUP (A): -13.1202  -2.8668  31.2630
REMARK   3    T TENSOR
REMARK   3      T11:   0.1359 T22:   0.1839
REMARK   3      T33:   0.0874 T12:   0.0214
REMARK   3      T13:   0.0053 T23:   0.0166
REMARK   3    L TENSOR
REMARK   3      L11:   0.3176 L22:   0.3599
REMARK   3      L33:   0.6405 L12:   0.0213
REMARK   3      L13:   0.2209 L23:   0.0110
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1646 S12:  -0.2828 S13:   0.0092
REMARK   3      S21:   0.1341 S22:   0.1619 S23:  -0.0369
REMARK   3      S31:   0.0303 S32:  -0.0896 S33:   0.0118
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: chain 'A' and (resseq 51:97)
REMARK   3    ORIGIN FOR THE GROUP (A): -14.2601   5.6079  11.6516
REMARK   3    T TENSOR
REMARK   3      T11:   0.1123 T22:   0.0895
REMARK   3      T33:   0.1028 T12:   0.0073
REMARK   3      T13:  -0.0111 T23:   0.0081
REMARK   3    L TENSOR
REMARK   3      L11:   0.4636 L22:   0.4359
REMARK   3      L33:   0.3717 L12:   0.2165
REMARK   3      L13:   0.0428 L23:   0.0401
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0046 S12:   0.0393 S13:   0.0620
REMARK   3      S21:  -0.0868 S22:  -0.0256 S23:   0.0538
REMARK   3      S31:  -0.0648 S32:  -0.0206 S33:   0.0000
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: chain 'A' and (resseq 98:115)
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.7419 -14.5462  19.3898
REMARK   3    T TENSOR
REMARK   3      T11:   0.1280 T22:   0.0801
REMARK   3      T33:   0.1190 T12:   0.0003
REMARK   3      T13:   0.0070 T23:   0.0071
REMARK   3    L TENSOR
REMARK   3      L11:   0.0596 L22:   0.0861
REMARK   3      L33:   0.0671 L12:  -0.0345
REMARK   3      L13:  -0.0127 L23:  -0.0809
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0202 S12:  -0.0337 S13:  -0.0861
REMARK   3      S21:   0.0518 S22:   0.0401 S23:  -0.0112
REMARK   3      S31:   0.1427 S32:   0.0573 S33:  -0.0000
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: chain 'A' and (resseq 116:154)
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4355   4.2367  18.1141
REMARK   3    T TENSOR
REMARK   3      T11:   0.0995 T22:   0.0774
REMARK   3      T33:   0.0922 T12:  -0.0090
REMARK   3      T13:  -0.0030 T23:  -0.0035
REMARK   3    L TENSOR
REMARK   3      L11:   0.3777 L22:   0.0481
REMARK   3      L33:   0.3040 L12:   0.0149
REMARK   3      L13:   0.1405 L23:  -0.1093
REMARK   3    S TENSOR
REMARK   3      S11:   0.0171 S12:  -0.0274 S13:   0.0511
REMARK   3      S21:  -0.0015 S22:  -0.0605 S23:   0.0650
REMARK   3      S31:  -0.0125 S32:  -0.0083 S33:  -0.0096
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: chain 'A' and (resseq 155:167)
REMARK   3    ORIGIN FOR THE GROUP (A): -15.7411  -6.3005   0.0443
REMARK   3    T TENSOR
REMARK   3      T11:   0.1788 T22:   0.1559
REMARK   3      T33:   0.1495 T12:  -0.0220
REMARK   3      T13:  -0.0357 T23:  -0.0019
REMARK   3    L TENSOR
REMARK   3      L11:   0.0522 L22:   0.0847
REMARK   3      L33:   0.0726 L12:  -0.0104
REMARK   3      L13:   0.0238 L23:  -0.0488
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1653 S12:   0.1934 S13:   0.0067
REMARK   3      S21:  -0.4643 S22:   0.1315 S23:   0.2539
REMARK   3      S31:   0.1876 S32:  -0.1133 S33:  -0.0004
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION: chain 'A' and (resseq 168:190)
REMARK   3    ORIGIN FOR THE GROUP (A): -17.8728  -1.3155   7.7802
REMARK   3    T TENSOR
REMARK   3      T11:   0.1368 T22:   0.1524
REMARK   3      T33:   0.1311 T12:   0.0156
REMARK   3      T13:  -0.0058 T23:   0.0192
REMARK   3    L TENSOR
REMARK   3      L11:   0.3006 L22:   0.3111
REMARK   3      L33:   0.1774 L12:  -0.0081
REMARK   3      L13:   0.1971 L23:   0.0007
REMARK   3    S TENSOR
REMARK   3      S11:   0.0238 S12:   0.1095 S13:  -0.0408
REMARK   3      S21:  -0.1432 S22:  -0.0245 S23:   0.0565
REMARK   3      S31:   0.0098 S32:  -0.0859 S33:  -0.0000
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION: chain 'A' and (resseq 191:219)
REMARK   3    ORIGIN FOR THE GROUP (A): -10.4196  -2.0421  22.2659
REMARK   3    T TENSOR
REMARK   3      T11:   0.0921 T22:   0.1090
REMARK   3      T33:   0.1010 T12:  -0.0106
REMARK   3      T13:   0.0003 T23:  -0.0069
REMARK   3    L TENSOR
REMARK   3      L11:   0.1760 L22:   0.2092
REMARK   3      L33:   0.1469 L12:  -0.0622
REMARK   3      L13:   0.1154 L23:   0.0741
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0245 S12:  -0.0606 S13:  -0.0038
REMARK   3      S21:  -0.0119 S22:   0.0114 S23:   0.0118
REMARK   3      S31:  -0.0028 S32:  -0.0029 S33:  -0.0000
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION: chain 'A' and (resseq 220:238)
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1974 -11.1220   1.1877
REMARK   3    T TENSOR
REMARK   3      T11:   0.1770 T22:   0.1805
REMARK   3      T33:   0.1358 T12:  -0.0035
REMARK   3      T13:   0.0263 T23:  -0.0147
REMARK   3    L TENSOR
REMARK   3      L11:   0.2577 L22:   0.2141
REMARK   3      L33:   0.1042 L12:  -0.2744
REMARK   3      L13:   0.0950 L23:  -0.0991
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0168 S12:   0.2871 S13:  -0.2756
REMARK   3      S21:  -0.2255 S22:  -0.0111 S23:  -0.0668
REMARK   3      S31:   0.1512 S32:   0.0439 S33:   0.0020
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION: chain 'A' and (resseq 239:261)
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3947  -6.5338  24.0418
REMARK   3    T TENSOR
REMARK   3      T11:   0.1157 T22:   0.1296
REMARK   3      T33:   0.1043 T12:   0.0005
REMARK   3      T13:   0.0059 T23:  -0.0077
REMARK   3    L TENSOR
REMARK   3      L11:   0.5506 L22:   0.4993
REMARK   3      L33:   0.1987 L12:  -0.2061
REMARK   3      L13:   0.3323 L23:  -0.0786
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0226 S12:  -0.1576 S13:   0.0163
REMARK   3      S21:   0.0902 S22:   0.0490 S23:  -0.0692
REMARK   3      S31:   0.1638 S32:   0.0895 S33:  -0.0000
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3RG4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064888.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-JAN-10
REMARK 200  TEMPERATURE           (KELVIN) : 298
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 RUH3R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : RIGAKU VARIMAX HR OPTIC
REMARK 200  OPTICS                         : 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   : 34955
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.9
REMARK 200  DATA REDUNDANCY                : 2.100
REMARK 200  R MERGE                    (I) : 0.08600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.25300
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 2ILI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2-1.4 M SODIUM CITRATE, 100 MM TRIS,
REMARK 280  PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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       20.73750
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 465     HIS A     3
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    ARG A  27       53.47   -141.05
REMARK 500    ASN A 244       48.07    -94.45
REMARK 500    LYS A 252     -132.48     52.46
REMARK 500    ASN A 253       46.59    -89.82
REMARK 500
REMARK 500 REMARK: NULL
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 HOH A 263   O
REMARK 620 2 HIS A  94   NE2 109.7
REMARK 620 3 HIS A  96   NE2 115.7 104.9
REMARK 620 4 HIS A 119   ND1 116.2 111.1  98.3
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RG3   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II WITH THE W5E MUTATION
REMARK 900 RELATED ID: 3RG5   RELATED DB: PDB
REMARK 900 HUMAN CARBONIC ANHYDRASE II WITH THE W5H MUTATION
DBREF  3RG4 A    1   261  UNP    P00918   CAH2_HUMAN       1    260
SEQADV 3RG4 PHE A    5  UNP  P00918    TRP     5 ENGINEERED MUTATION
SEQRES   1 A  260  MET SER HIS HIS PHE 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
HETNAM      ZN ZINC ION
FORMUL   2   ZN    ZN 2+
FORMUL   3  HOH   *201(H2 O)
HELIX    1   1 GLY A   12  ASP A   19  5                                   8
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  LEU A 212
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 LEU A  47  SER A  50  0
SHEET    2   C 6 VAL A  78  GLY A  81 -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                 O   HOH A 263     1555   1555  1.96
LINK         NE2 HIS A  94                ZN    ZN A 262     1555   1555  2.02
LINK         NE2 HIS A  96                ZN    ZN A 262     1555   1555  2.04
LINK         ND1 HIS A 119                ZN    ZN A 262     1555   1555  2.06
CISPEP   1 SER A   29    PRO A   30          0        -1.58
CISPEP   2 PRO A  201    PRO A  202          0        14.62
SITE     1 AC1  4 HIS A  94  HIS A  96  HIS A 119  HOH A 263
CRYST1   42.683   41.475   72.651  90.00 104.40  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      0.023429  0.000000  0.006014        0.00000
SCALE2      0.000000  0.024111  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014211        0.00000
      
PROCHECK
Go to PROCHECK summary
 References