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PDBsum entry 3qy1

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Top Page protein metals Protein-protein interface(s) links
Lyase PDB id
3qy1
Jmol
Contents
Protein chains
215 a.a.
Metals
_ZN ×2
Waters ×449
HEADER    LYASE                                   02-MAR-11   3QY1
TITLE     1.54A RESOLUTION CRYSTAL STRUCTURE OF A BETA-CARBONIC ANHYDRASE FROM
TITLE    2 SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM STR. LT2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 4.2.1.1;
COMPND   5 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE   3 TYPHIMURIUM;
SOURCE   4 ORGANISM_TAXID: 99287;
SOURCE   5 STRAIN: LT2;
SOURCE   6 GENE: STM0171, YADF;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS   2 DISEASES, CSGID, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.S.BRUNZELLE,Z.WAWRZAK,O.ONOPRIYENKO,W.F.ANDERSON,A.SAVCHENKO,CENTER
AUTHOR   2 FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT   1   16-MAR-11 3QY1    0
JRNL        AUTH   J.S.BRUNZELLE,Z.WAWRZAK,O.ONOPRIYENKO,W.F.ANDERSON,
JRNL        AUTH 2 A.SAVCHENKO,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
JRNL        AUTH 3 DISEASES (CSGID)
JRNL        TITL   1.54A RESOLUTION CRYSTAL STRUCTURE OF A BETA-CARBONIC
JRNL        TITL 2 ANHYDRASE FROM SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
JRNL        TITL 3 TYPHIMURIUM STR. LT2
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.54 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : BUSTER 2.8.0
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.55
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 59370
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)  : 0.157
REMARK   3   R VALUE            (WORKING SET)  : 0.156
REMARK   3   FREE R VALUE                      : 0.172
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050
REMARK   3   FREE R VALUE TEST SET COUNT       : 2999
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED               : 20
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.54
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.58
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3872
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2055
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3675
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2046
REMARK   3   BIN FREE R VALUE                        : 0.2221
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.09
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 197
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3411
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2
REMARK   3   SOLVENT ATOMS            : 447
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 21.46
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.80
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.87560
REMARK   3    B22 (A**2) : 2.47820
REMARK   3    B33 (A**2) : -4.35380
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : -0.59920
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.18
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL
REMARK   3
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.967
REMARK   3
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.
REMARK   3    BOND LENGTHS              : 3524   ; 2.000  ; HARMONIC
REMARK   3    BOND ANGLES               : 4795   ; 2.000  ; HARMONIC
REMARK   3    TORSION ANGLES            : 1635   ; 2.000  ; SINUSOIDAL
REMARK   3    TRIGONAL CARBON PLANES    : 99     ; 2.000  ; HARMONIC
REMARK   3    GENERAL PLANES            : 507    ; 5.000  ; HARMONIC
REMARK   3    ISOTROPIC THERMAL FACTORS : 3524   ; 20.000 ; HARMONIC
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL
REMARK   3    CHIRAL IMPROPER TORSION   : 452    ; 5.000  ; SEMIHARMONIC
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL
REMARK   3    IDEAL-DIST CONTACT TERM   : 4707   ; 4.000  ; SEMIHARMONIC
REMARK   3
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND LENGTHS                       (A) : 0.010
REMARK   3    BOND ANGLES                  (DEGREES) : 0.95
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.54
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.69
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 18
REMARK   3
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION:   A    3    A   31
REMARK   3    ORIGIN FOR THE GROUP (A):   19.5191  -12.3724  -30.8923
REMARK   3    T TENSOR
REMARK   3     T11:    0.0425 T22:   -0.0615
REMARK   3     T33:   -0.1294 T12:   -0.0350
REMARK   3     T13:    0.1130 T23:   -0.0633
REMARK   3    L TENSOR
REMARK   3     L11:    2.9858 L22:    4.0811
REMARK   3     L33:    8.9547 L12:    1.8886
REMARK   3     L13:   -2.9913 L23:   -2.4374
REMARK   3    S TENSOR
REMARK   3     S11:    0.0082 S12:    0.0937 S13:   -0.1240
REMARK   3     S21:   -0.3724 S22:    0.0563 S23:   -0.1491
REMARK   3     S31:   -0.0859 S32:    0.4642 S33:   -0.0645
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION:   A   32    A   54
REMARK   3    ORIGIN FOR THE GROUP (A):    0.9304   -8.5927  -23.8364
REMARK   3    T TENSOR
REMARK   3     T11:    0.0009 T22:   -0.0254
REMARK   3     T33:   -0.1232 T12:    0.0478
REMARK   3     T13:    0.0151 T23:    0.0174
REMARK   3    L TENSOR
REMARK   3     L11:    2.0240 L22:    3.5350
REMARK   3     L33:    3.8453 L12:    0.1185
REMARK   3     L13:   -0.5549 L23:    0.0719
REMARK   3    S TENSOR
REMARK   3     S11:    0.1582 S12:    0.4245 S13:    0.0562
REMARK   3     S21:   -0.4826 S22:   -0.0883 S23:   -0.1638
REMARK   3     S31:   -0.2317 S32:    0.0118 S33:   -0.0699
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION:   A   55    A  104
REMARK   3    ORIGIN FOR THE GROUP (A):   -1.4666   -7.2573  -15.1380
REMARK   3    T TENSOR
REMARK   3     T11:    0.0309 T22:   -0.0345
REMARK   3     T33:   -0.0519 T12:    0.0264
REMARK   3     T13:    0.0009 T23:    0.0163
REMARK   3    L TENSOR
REMARK   3     L11:    1.2421 L22:    1.2684
REMARK   3     L33:    0.6409 L12:   -0.1993
REMARK   3     L13:   -0.1689 L23:    0.1135
REMARK   3    S TENSOR
REMARK   3     S11:    0.0528 S12:    0.2068 S13:    0.0865
REMARK   3     S21:   -0.2788 S22:   -0.0412 S23:   -0.0166
REMARK   3     S31:   -0.1573 S32:   -0.0792 S33:   -0.0116
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION:   A  105    A  127
REMARK   3    ORIGIN FOR THE GROUP (A):  -10.9070  -24.2169   -8.1969
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0262 T22:   -0.0469
REMARK   3     T33:    0.0084 T12:   -0.0088
REMARK   3     T13:   -0.0269 T23:   -0.0082
REMARK   3    L TENSOR
REMARK   3     L11:    1.1816 L22:    2.2144
REMARK   3     L33:    0.1554 L12:   -1.3730
REMARK   3     L13:    0.4354 L23:   -0.7512
REMARK   3    S TENSOR
REMARK   3     S11:    0.0706 S12:    0.0205 S13:   -0.1991
REMARK   3     S21:   -0.2193 S22:   -0.0094 S23:    0.2009
REMARK   3     S31:    0.0775 S32:   -0.1166 S33:   -0.0612
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION:   A  128    A  145
REMARK   3    ORIGIN FOR THE GROUP (A):  -24.0849  -20.4921  -16.9924
REMARK   3    T TENSOR
REMARK   3     T11:    0.0011 T22:    0.0793
REMARK   3     T33:    0.0847 T12:    0.0168
REMARK   3     T13:   -0.1179 T23:   -0.0231
REMARK   3    L TENSOR
REMARK   3     L11:    6.6869 L22:    2.0508
REMARK   3     L33:    3.4852 L12:    1.3672
REMARK   3     L13:    0.7319 L23:    0.0123
REMARK   3    S TENSOR
REMARK   3     S11:    0.0576 S12:    0.5216 S13:   -0.3547
REMARK   3     S21:   -0.2510 S22:    0.0705 S23:    0.4505
REMARK   3     S31:    0.1227 S32:   -0.2685 S33:   -0.1281
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION:   A  146    A  167
REMARK   3    ORIGIN FOR THE GROUP (A):  -11.9112   -5.9106  -11.7487
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0638 T22:   -0.0639
REMARK   3     T33:   -0.0725 T12:    0.0628
REMARK   3     T13:   -0.0115 T23:    0.0153
REMARK   3    L TENSOR
REMARK   3     L11:    1.2424 L22:    4.3178
REMARK   3     L33:    2.2825 L12:    1.5328
REMARK   3     L13:    0.4011 L23:    1.3884
REMARK   3    S TENSOR
REMARK   3     S11:    0.1160 S12:    0.1539 S13:    0.0621
REMARK   3     S21:   -0.0954 S22:   -0.0497 S23:    0.2001
REMARK   3     S31:   -0.1556 S32:   -0.1868 S33:   -0.0663
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    SELECTION:   A  168    A  196
REMARK   3    ORIGIN FOR THE GROUP (A):  -10.3365   -4.1330  -21.5009
REMARK   3    T TENSOR
REMARK   3     T11:    0.0889 T22:    0.0195
REMARK   3     T33:   -0.0845 T12:    0.0743
REMARK   3     T13:   -0.0496 T23:    0.0262
REMARK   3    L TENSOR
REMARK   3     L11:    1.6733 L22:    2.3946
REMARK   3     L33:   -0.0980 L12:    0.5928
REMARK   3     L13:   -0.2530 L23:    0.2377
REMARK   3    S TENSOR
REMARK   3     S11:    0.0902 S12:    0.4378 S13:    0.1098
REMARK   3     S21:   -0.4080 S22:   -0.0669 S23:    0.2128
REMARK   3     S31:   -0.1944 S32:   -0.3221 S33:   -0.0233
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    SELECTION:   A  197    A  201
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.8452    4.7091  -12.6393
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0126 T22:   -0.0512
REMARK   3     T33:    0.0348 T12:    0.0965
REMARK   3     T13:    0.0012 T23:    0.0633
REMARK   3    L TENSOR
REMARK   3     L11:    1.0308 L22:    1.4957
REMARK   3     L33:   -1.0308 L12:   -0.3983
REMARK   3     L13:   -0.9646 L23:   -2.2340
REMARK   3    S TENSOR
REMARK   3     S11:    0.0843 S12:    0.0006 S13:    0.1325
REMARK   3     S21:   -0.0417 S22:    0.0089 S23:    0.0136
REMARK   3     S31:   -0.1160 S32:   -0.0347 S33:   -0.0932
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    SELECTION:   A  202    A  217
REMARK   3    ORIGIN FOR THE GROUP (A):  -23.8844   -8.1902  -19.1318
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0315 T22:    0.0552
REMARK   3     T33:    0.0558 T12:    0.0679
REMARK   3     T13:   -0.1303 T23:    0.0720
REMARK   3    L TENSOR
REMARK   3     L11:    2.2447 L22:    0.5486
REMARK   3     L33:    4.7981 L12:    2.0373
REMARK   3     L13:    0.2351 L23:    2.4270
REMARK   3    S TENSOR
REMARK   3     S11:    0.0362 S12:    0.4229 S13:    0.1891
REMARK   3     S21:   -0.2709 S22:    0.1454 S23:    0.5583
REMARK   3     S31:   -0.1003 S32:   -0.4189 S33:   -0.1816
REMARK   3
REMARK   3   TLS GROUP : 10
REMARK   3    SELECTION:   B    2    B   14
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.4163   -4.2061  -33.3988
REMARK   3    T TENSOR
REMARK   3     T11:    0.1277 T22:    0.1914
REMARK   3     T33:   -0.3435 T12:    0.0903
REMARK   3     T13:    0.0005 T23:    0.0085
REMARK   3    L TENSOR
REMARK   3     L11:   -0.2469 L22:    2.0467
REMARK   3     L33:    1.5800 L12:    1.2353
REMARK   3     L13:    1.6129 L23:   -0.9891
REMARK   3    S TENSOR
REMARK   3     S11:    0.0232 S12:    0.3252 S13:    0.1788
REMARK   3     S21:   -0.1008 S22:    0.1089 S23:    0.0533
REMARK   3     S31:   -0.1315 S32:   -0.0935 S33:   -0.1321
REMARK   3
REMARK   3   TLS GROUP : 11
REMARK   3    SELECTION:   B   15    B   31
REMARK   3    ORIGIN FOR THE GROUP (A):   -4.9376  -21.2879  -38.1508
REMARK   3    T TENSOR
REMARK   3     T11:    0.2581 T22:    0.3222
REMARK   3     T33:   -0.4287 T12:   -0.1423
REMARK   3     T13:   -0.0529 T23:   -0.1522
REMARK   3    L TENSOR
REMARK   3     L11:    1.8620 L22:    2.6996
REMARK   3     L33:    2.3654 L12:    0.0579
REMARK   3     L13:    1.7622 L23:    3.9078
REMARK   3    S TENSOR
REMARK   3     S11:    0.0641 S12:    0.0782 S13:   -0.1811
REMARK   3     S21:   -0.1047 S22:   -0.0468 S23:   -0.0416
REMARK   3     S31:   -0.0091 S32:   -0.0090 S33:   -0.0173
REMARK   3
REMARK   3   TLS GROUP : 12
REMARK   3    SELECTION:   B   32    B   54
REMARK   3    ORIGIN FOR THE GROUP (A):    8.7931  -17.8860  -22.2656
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0364 T22:   -0.1105
REMARK   3     T33:   -0.1104 T12:    0.0028
REMARK   3     T13:    0.0154 T23:   -0.0240
REMARK   3    L TENSOR
REMARK   3     L11:    1.6407 L22:    3.3371
REMARK   3     L33:    1.8710 L12:    1.1068
REMARK   3     L13:   -1.3448 L23:   -0.3290
REMARK   3    S TENSOR
REMARK   3     S11:   -0.0889 S12:    0.3117 S13:   -0.0698
REMARK   3     S21:   -0.4559 S22:    0.0915 S23:   -0.0333
REMARK   3     S31:    0.0986 S32:   -0.0429 S33:   -0.0026
REMARK   3
REMARK   3   TLS GROUP : 13
REMARK   3    SELECTION:   B   55    B  102
REMARK   3    ORIGIN FOR THE GROUP (A):    6.9799  -19.9387  -13.4975
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0236 T22:   -0.0756
REMARK   3     T33:   -0.0215 T12:    0.0052
REMARK   3     T13:    0.0210 T23:   -0.0137
REMARK   3    L TENSOR
REMARK   3     L11:    1.3247 L22:    1.2420
REMARK   3     L33:    0.7946 L12:    0.0386
REMARK   3     L13:   -0.0481 L23:   -0.0504
REMARK   3    S TENSOR
REMARK   3     S11:   -0.0164 S12:    0.1038 S13:   -0.1393
REMARK   3     S21:   -0.2472 S22:    0.0026 S23:   -0.0895
REMARK   3     S31:    0.0128 S32:    0.0134 S33:    0.0139
REMARK   3
REMARK   3   TLS GROUP : 14
REMARK   3    SELECTION:   B  103    B  116
REMARK   3    ORIGIN FOR THE GROUP (A):   12.9099    0.9048   -5.7311
REMARK   3    T TENSOR
REMARK   3     T11:    0.0316 T22:   -0.0412
REMARK   3     T33:    0.0556 T12:   -0.0315
REMARK   3     T13:    0.0428 T23:   -0.0188
REMARK   3    L TENSOR
REMARK   3     L11:    0.1888 L22:    3.8824
REMARK   3     L33:   -0.0735 L12:    0.3297
REMARK   3     L13:   -0.0437 L23:    1.1033
REMARK   3    S TENSOR
REMARK   3     S11:    0.1245 S12:   -0.0641 S13:    0.2584
REMARK   3     S21:   -0.0908 S22:    0.0979 S23:   -0.4041
REMARK   3     S31:   -0.2042 S32:    0.1152 S33:   -0.2224
REMARK   3
REMARK   3   TLS GROUP : 15
REMARK   3    SELECTION:   B  117    B  133
REMARK   3    ORIGIN FOR THE GROUP (A):   17.4625   -7.2202   -1.3099
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0212 T22:   -0.0013
REMARK   3     T33:    0.0436 T12:   -0.0392
REMARK   3     T13:    0.0177 T23:    0.0027
REMARK   3    L TENSOR
REMARK   3     L11:    4.2929 L22:    1.0897
REMARK   3     L33:    1.5151 L12:   -0.8758
REMARK   3     L13:   -0.9356 L23:   -0.1448
REMARK   3    S TENSOR
REMARK   3     S11:    0.0444 S12:   -0.1034 S13:    0.1016
REMARK   3     S21:   -0.0420 S22:   -0.0455 S23:   -0.2131
REMARK   3     S31:   -0.1941 S32:    0.2989 S33:    0.0011
REMARK   3
REMARK   3   TLS GROUP : 16
REMARK   3    SELECTION:   B  134    B  167
REMARK   3    ORIGIN FOR THE GROUP (A):   20.3253  -15.2090   -6.8726
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0849 T22:   -0.0183
REMARK   3     T33:    0.0321 T12:    0.0053
REMARK   3     T13:    0.0086 T23:    0.0103
REMARK   3    L TENSOR
REMARK   3     L11:    1.2854 L22:    3.1794
REMARK   3     L33:    0.9490 L12:    1.9060
REMARK   3     L13:   -0.7818 L23:   -0.8756
REMARK   3    S TENSOR
REMARK   3     S11:    0.0354 S12:   -0.1199 S13:   -0.0815
REMARK   3     S21:    0.0193 S22:   -0.0891 S23:   -0.2366
REMARK   3     S31:   -0.0041 S32:    0.2556 S33:    0.0538
REMARK   3
REMARK   3   TLS GROUP : 17
REMARK   3    SELECTION:   B  168    B  197
REMARK   3    ORIGIN FOR THE GROUP (A):   18.1506  -22.4811  -15.5942
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0093 T22:   -0.0474
REMARK   3     T33:    0.0578 T12:    0.0277
REMARK   3     T13:    0.0618 T23:    0.0034
REMARK   3    L TENSOR
REMARK   3     L11:    0.8396 L22:    1.1236
REMARK   3     L33:    1.6421 L12:    0.5770
REMARK   3     L13:   -0.4740 L23:   -0.1727
REMARK   3    S TENSOR
REMARK   3     S11:   -0.0464 S12:    0.0901 S13:   -0.1975
REMARK   3     S21:   -0.2085 S22:   -0.0462 S23:   -0.4026
REMARK   3     S31:    0.0652 S32:    0.3738 S33:    0.0927
REMARK   3
REMARK   3   TLS GROUP : 18
REMARK   3    SELECTION:   B  198    B  217
REMARK   3    ORIGIN FOR THE GROUP (A):   27.4016  -21.4228   -7.2379
REMARK   3    T TENSOR
REMARK   3     T11:   -0.0953 T22:    0.0291
REMARK   3     T33:    0.1060 T12:    0.0488
REMARK   3     T13:    0.0344 T23:    0.0341
REMARK   3    L TENSOR
REMARK   3     L11:    2.8647 L22:    2.0295
REMARK   3     L33:    0.2746 L12:   -0.1444
REMARK   3     L13:    0.2845 L23:    0.3066
REMARK   3    S TENSOR
REMARK   3     S11:    0.0559 S12:   -0.0513 S13:   -0.2532
REMARK   3     S21:   -0.0609 S22:   -0.2033 S23:   -0.1784
REMARK   3     S31:    0.0583 S32:    0.2545 S33:    0.1474
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3QY1 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064246.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-10
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 21-ID-F
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787
REMARK 200  MONOCHROMATOR                  : DIAMOND
REMARK 200  OPTICS                         : BE LENS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59389
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.540
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.880
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 5.000
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.62500
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MRBUMP
REMARK 200 STARTING MODEL: 1T75
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 39.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30%PEG 4K,0.2M NH4 ACETATE, 0.1NA
REMARK 280  CITRATE, PH 6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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       57.62600
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.11150
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       57.62600
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.11150
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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 A    -2
REMARK 465     ASN A    -1
REMARK 465     ALA A     0
REMARK 465     MET A     1
REMARK 465     LYS A     2
REMARK 465     PRO A   218
REMARK 465     HIS A   219
REMARK 465     GLN A   220
REMARK 465     SER B    -2
REMARK 465     ASN B    -1
REMARK 465     ALA B     0
REMARK 465     MET B     1
REMARK 465     PRO B   218
REMARK 465     HIS B   219
REMARK 465     GLN B   220
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     GLU B 112    CG   CD   OE1  OE2
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    ASP A  22       82.59   -151.18
REMARK 500    SER A  45       54.84     37.81
REMARK 500    SER B  45       59.01     36.24
REMARK 500    ASP B 185      -12.01   -141.00
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 390        DISTANCE =  7.27 ANGSTROMS
REMARK 525    HOH B 399        DISTANCE =  5.62 ANGSTROMS
REMARK 525    HOH A 434        DISTANCE =  9.22 ANGSTROMS
REMARK 525    HOH A 436        DISTANCE =  6.69 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 B 221  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  98   NE2
REMARK 620 2 ASP B  44   OD2 100.0
REMARK 620 3 CYS B  42   SG  117.0 105.0
REMARK 620 4 CYS B 101   SG  110.1 107.7 115.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 221  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  98   NE2
REMARK 620 2 ASP A  44   OD2  98.9
REMARK 620 3 CYS A  42   SG  116.6 104.6
REMARK 620 4 CYS A 101   SG  110.5 109.2 115.3
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 221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 221
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP00909   RELATED DB: TARGETDB
DBREF  3QY1 A    1   220  UNP    Q8ZRS0   Q8ZRS0_SALTY     1    220
DBREF  3QY1 B    1   220  UNP    Q8ZRS0   Q8ZRS0_SALTY     1    220
SEQADV 3QY1 SER A   -2  UNP  Q8ZRS0              EXPRESSION TAG
SEQADV 3QY1 ASN A   -1  UNP  Q8ZRS0              EXPRESSION TAG
SEQADV 3QY1 ALA A    0  UNP  Q8ZRS0              EXPRESSION TAG
SEQADV 3QY1 SER B   -2  UNP  Q8ZRS0              EXPRESSION TAG
SEQADV 3QY1 ASN B   -1  UNP  Q8ZRS0              EXPRESSION TAG
SEQADV 3QY1 ALA B    0  UNP  Q8ZRS0              EXPRESSION TAG
SEQRES   1 A  223  SER ASN ALA MET LYS ASP ILE ASP THR LEU ILE SER ASN
SEQRES   2 A  223  ASN ALA LEU TRP SER LYS MET LEU VAL GLU GLU ASP PRO
SEQRES   3 A  223  GLY PHE PHE GLU LYS LEU ALA GLN ALA GLN LYS PRO ARG
SEQRES   4 A  223  PHE LEU TRP ILE GLY CYS SER ASP SER ARG VAL PRO ALA
SEQRES   5 A  223  GLU ARG LEU THR GLY LEU GLU PRO GLY GLU LEU PHE VAL
SEQRES   6 A  223  HIS ARG ASN VAL ALA ASN LEU VAL ILE HIS THR ASP LEU
SEQRES   7 A  223  ASN CYS LEU SER VAL VAL GLN TYR ALA VAL ASP VAL LEU
SEQRES   8 A  223  GLU VAL GLU HIS ILE ILE ILE CYS GLY HIS SER GLY CYS
SEQRES   9 A  223  GLY GLY ILE LYS ALA ALA VAL GLU ASN PRO GLU LEU GLY
SEQRES  10 A  223  LEU ILE ASN ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP
SEQRES  11 A  223  LEU LYS HIS SER SER LEU LEU GLY LYS MET PRO GLU GLU
SEQRES  12 A  223  GLN ARG LEU ASP ALA LEU TYR GLU LEU ASN VAL MET GLU
SEQRES  13 A  223  GLN VAL TYR ASN LEU GLY HIS SER THR ILE MET GLN SER
SEQRES  14 A  223  ALA TRP LYS ARG GLY GLN ASN VAL THR ILE HIS GLY TRP
SEQRES  15 A  223  ALA TYR SER ILE ASN ASP GLY LEU LEU ARG ASP LEU ASP
SEQRES  16 A  223  VAL THR ALA THR ASN ARG GLU THR LEU GLU ASN GLY TYR
SEQRES  17 A  223  HIS LYS GLY ILE SER ALA LEU SER LEU LYS TYR ILE PRO
SEQRES  18 A  223  HIS GLN
SEQRES   1 B  223  SER ASN ALA MET LYS ASP ILE ASP THR LEU ILE SER ASN
SEQRES   2 B  223  ASN ALA LEU TRP SER LYS MET LEU VAL GLU GLU ASP PRO
SEQRES   3 B  223  GLY PHE PHE GLU LYS LEU ALA GLN ALA GLN LYS PRO ARG
SEQRES   4 B  223  PHE LEU TRP ILE GLY CYS SER ASP SER ARG VAL PRO ALA
SEQRES   5 B  223  GLU ARG LEU THR GLY LEU GLU PRO GLY GLU LEU PHE VAL
SEQRES   6 B  223  HIS ARG ASN VAL ALA ASN LEU VAL ILE HIS THR ASP LEU
SEQRES   7 B  223  ASN CYS LEU SER VAL VAL GLN TYR ALA VAL ASP VAL LEU
SEQRES   8 B  223  GLU VAL GLU HIS ILE ILE ILE CYS GLY HIS SER GLY CYS
SEQRES   9 B  223  GLY GLY ILE LYS ALA ALA VAL GLU ASN PRO GLU LEU GLY
SEQRES  10 B  223  LEU ILE ASN ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP
SEQRES  11 B  223  LEU LYS HIS SER SER LEU LEU GLY LYS MET PRO GLU GLU
SEQRES  12 B  223  GLN ARG LEU ASP ALA LEU TYR GLU LEU ASN VAL MET GLU
SEQRES  13 B  223  GLN VAL TYR ASN LEU GLY HIS SER THR ILE MET GLN SER
SEQRES  14 B  223  ALA TRP LYS ARG GLY GLN ASN VAL THR ILE HIS GLY TRP
SEQRES  15 B  223  ALA TYR SER ILE ASN ASP GLY LEU LEU ARG ASP LEU ASP
SEQRES  16 B  223  VAL THR ALA THR ASN ARG GLU THR LEU GLU ASN GLY TYR
SEQRES  17 B  223  HIS LYS GLY ILE SER ALA LEU SER LEU LYS TYR ILE PRO
SEQRES  18 B  223  HIS GLN
HET     ZN  A 221       1
HET     ZN  B 221       1
HETNAM      ZN ZINC ION
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  HOH   *447(H2 O)
HELIX    1   1 ASP A    3  ASP A   22  1                                  20
HELIX    2   2 PRO A   23  GLN A   31  1                                   9
HELIX    3   3 PRO A   48  GLY A   54  1                                   7
HELIX    4   4 GLU A   56  GLY A   58  5                                   3
HELIX    5   5 ASP A   74  VAL A   87  1                                  14
HELIX    6   6 CYS A  101  ASN A  110  1                                  10
HELIX    7   7 LEU A  115  HIS A  130  1                                  16
HELIX    8   8 HIS A  130  LYS A  136  1                                   7
HELIX    9   9 MET A  137  GLU A  140  5                                   4
HELIX   10  10 GLN A  141  SER A  161  1                                  21
HELIX   11  11 SER A  161  ARG A  170  1                                  10
HELIX   12  12 ASN A  197  ILE A  217  1                                  21
HELIX   13  13 ASP B    3  ASP B   22  1                                  20
HELIX   14  14 PRO B   23  ALA B   32  1                                  10
HELIX   15  15 PRO B   48  GLY B   54  1                                   7
HELIX   16  16 ASP B   74  VAL B   87  1                                  14
HELIX   17  17 CYS B  101  ASN B  110  1                                  10
HELIX   18  18 LEU B  115  HIS B  130  1                                  16
HELIX   19  19 HIS B  130  LYS B  136  1                                   7
HELIX   20  20 MET B  137  GLU B  140  5                                   4
HELIX   21  21 GLN B  141  SER B  161  1                                  21
HELIX   22  22 SER B  161  ARG B  170  1                                  10
HELIX   23  23 ASN B  197  ILE B  217  1                                  21
SHEET    1   A 5 LEU A  60  ASN A  65  0
SHEET    2   A 5 PHE A  37  CYS A  42  1  N  TRP A  39   O  PHE A  61
SHEET    3   A 5 HIS A  92  HIS A  98  1  O  ILE A  94   N  ILE A  40
SHEET    4   A 5 THR A 175  TYR A 181  1  O  TRP A 179   N  ILE A  95
SHEET    5   A 5 LEU A 188  ASP A 190 -1  O  ARG A 189   N  ALA A 180
SHEET    1   B 5 LEU B  60  ASN B  65  0
SHEET    2   B 5 PHE B  37  CYS B  42  1  N  TRP B  39   O  PHE B  61
SHEET    3   B 5 HIS B  92  HIS B  98  1  O  ILE B  94   N  LEU B  38
SHEET    4   B 5 THR B 175  TYR B 181  1  O  TRP B 179   N  ILE B  95
SHEET    5   B 5 LEU B 188  ASP B 190 -1  O  ARG B 189   N  ALA B 180
LINK         NE2 HIS B  98                ZN    ZN B 221     1555   1555  2.12
LINK         NE2 HIS A  98                ZN    ZN A 221     1555   1555  2.12
LINK         OD2 ASP B  44                ZN    ZN B 221     1555   1555  2.17
LINK         OD2 ASP A  44                ZN    ZN A 221     1555   1555  2.20
LINK         SG  CYS B  42                ZN    ZN B 221     1555   1555  2.25
LINK         SG  CYS B 101                ZN    ZN B 221     1555   1555  2.26
LINK         SG  CYS A  42                ZN    ZN A 221     1555   1555  2.26
LINK         SG  CYS A 101                ZN    ZN A 221     1555   1555  2.27
SITE     1 AC1  4 CYS A  42  ASP A  44  HIS A  98  CYS A 101
SITE     1 AC2  4 CYS B  42  ASP B  44  HIS B  98  CYS B 101
CRYST1  115.252   48.223   80.072  90.00 113.45  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      0.008677  0.000000  0.003764        0.00000
SCALE2      0.000000  0.020737  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013613        0.00000
      
PROCHECK
Go to PROCHECK summary
 References