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PDBsum entry 3e3i

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Lyase PDB id
3e3i
Jmol
Contents
Protein chains
(+ 6 more) 208 a.a.
Ligands
SO4 ×13
BCT ×11
Metals
_ZN ×12
Waters ×604
HEADER    LYASE                                   07-AUG-08   3E3I
TITLE     H. INFLUENZAE BETA-CARBONIC ANHYDRASE, VARIANT G41A WITH 100 MM
TITLE    2 BICARBONATE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE 2; BETA CARBONIC ANHYDRASE;
COMPND   5 EC: 4.2.1.1;
COMPND   6 ENGINEERED: YES;
COMPND   7 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE   3 ORGANISM_TAXID: 727;
SOURCE   4 GENE: CAN, HI1301;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTRC99
KEYWDS    BETA CARBONIC ANHYDRASE, ALLOSTERIC SITE MUTANT, LYASE, METAL-BINDING
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.S.ROWLETT,H.FAILING
REVDAT   3   13-JUL-11 3E3I    1       VERSN
REVDAT   2   26-MAY-10 3E3I    1       JRNL
REVDAT   1   18-AUG-09 3E3I    0
JRNL        AUTH   R.S.ROWLETT,K.M.HOFFMANN,H.FAILING,M.M.MYSLIWIEC,D.SAMARDZIC
JRNL        TITL   EVIDENCE FOR A BICARBONATE "ESCORT" SITE IN HAEMOPHILUS
JRNL        TITL 2 INFLUENZAE BETA-CARBONIC ANHYDRASE .
JRNL        REF    BIOCHEMISTRY                  V.  49  3640 2010
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   20359198
JRNL        DOI    10.1021/BI100328J
REMARK   2
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2
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) : 2.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.75
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.6
REMARK   3   NUMBER OF REFLECTIONS             : 205402
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) : 0.203
REMARK   3   R VALUE            (WORKING SET) : 0.201
REMARK   3   FREE R VALUE                     : 0.236
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 10347
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) : 2.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8250
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 51.18
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2510
REMARK   3   BIN FREE R VALUE SET COUNT          : 410
REMARK   3   BIN FREE R VALUE                    : 0.3140
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 20197
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 121
REMARK   3   SOLVENT ATOMS            : 604
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) : 36.16
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.06000
REMARK   3    B22 (A**2) : 0.04000
REMARK   3    B33 (A**2) : 0.03000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.04000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.185
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.164
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.110
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.573
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 20906 ; 0.011 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A): 13822 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 28283 ; 1.192 ; 1.930
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 33644 ; 0.856 ; 3.001
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2514 ; 5.542 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1022 ;35.853 ;24.276
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3652 ;15.298 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   120 ;17.163 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3125 ; 0.071 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 23067 ; 0.004 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  4209 ; 0.001 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4737 ; 0.213 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 14282 ; 0.189 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10152 ; 0.177 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A): 10470 ; 0.087 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   920 ; 0.149 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):     4 ; 0.083 ; 0.200
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):    29 ; 0.185 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    45 ; 0.248 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.205 ; 0.200
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): 16352 ; 0.782 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5137 ; 0.134 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 20157 ; 0.941 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9810 ; 1.598 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8123 ; 2.307 ; 4.500
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  : 12
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   220
REMARK   3    ORIGIN FOR THE GROUP (A): -12.5900 -11.9010  24.7950
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0795 T22:  -0.0208
REMARK   3      T33:  -0.0213 T12:  -0.0514
REMARK   3      T13:  -0.0039 T23:  -0.0279
REMARK   3    L TENSOR
REMARK   3      L11:   1.6336 L22:   1.2026
REMARK   3      L33:   0.3607 L12:   0.1955
REMARK   3      L13:   0.3902 L23:   0.1683
REMARK   3    S TENSOR
REMARK   3      S11:   0.0441 S12:  -0.0060 S13:  -0.2565
REMARK   3      S21:  -0.0480 S22:  -0.0304 S23:   0.1374
REMARK   3      S31:   0.0852 S32:  -0.0947 S33:  -0.0138
REMARK   3
REMARK   3   TLS GROUP : 2
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B     1        B   219
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3160  20.7370  28.9350
REMARK   3    T TENSOR
REMARK   3      T11:   0.0046 T22:  -0.0236
REMARK   3      T33:  -0.0718 T12:   0.0842
REMARK   3      T13:  -0.0426 T23:  -0.0117
REMARK   3    L TENSOR
REMARK   3      L11:   1.8654 L22:   1.4142
REMARK   3      L33:   1.3664 L12:  -0.1794
REMARK   3      L13:  -0.3271 L23:   0.2124
REMARK   3    S TENSOR
REMARK   3      S11:   0.0208 S12:   0.0057 S13:   0.2282
REMARK   3      S21:  -0.0095 S22:  -0.0816 S23:   0.0667
REMARK   3      S31:  -0.4261 S32:  -0.1943 S33:   0.0608
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 :   C     1        C   220
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2890 -12.0420  27.4890
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0746 T22:  -0.0426
REMARK   3      T33:   0.0059 T12:   0.0349
REMARK   3      T13:  -0.0105 T23:   0.0141
REMARK   3    L TENSOR
REMARK   3      L11:   1.7485 L22:   1.2949
REMARK   3      L33:   0.4635 L12:  -0.1789
REMARK   3      L13:   0.6007 L23:  -0.2770
REMARK   3    S TENSOR
REMARK   3      S11:   0.0957 S12:   0.1108 S13:  -0.2699
REMARK   3      S21:   0.0382 S22:  -0.0876 S23:  -0.1884
REMARK   3      S31:   0.1079 S32:   0.0748 S33:  -0.0081
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 :   D     1        D   220
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7230  20.4960  23.2540
REMARK   3    T TENSOR
REMARK   3      T11:   0.0004 T22:  -0.0460
REMARK   3      T33:  -0.0453 T12:  -0.0628
REMARK   3      T13:  -0.0328 T23:   0.0589
REMARK   3    L TENSOR
REMARK   3      L11:   2.0164 L22:   1.4569
REMARK   3      L33:   1.6481 L12:   0.0085
REMARK   3      L13:  -0.3642 L23:  -0.1903
REMARK   3    S TENSOR
REMARK   3      S11:   0.0197 S12:   0.1039 S13:   0.2503
REMARK   3      S21:  -0.0023 S22:  -0.0836 S23:  -0.1680
REMARK   3      S31:  -0.4461 S32:   0.1444 S33:   0.0639
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 :   E     1        E   219
REMARK   3    ORIGIN FOR THE GROUP (A):  63.2250 -14.0450  47.7850
REMARK   3    T TENSOR
REMARK   3      T11:   0.0088 T22:  -0.0360
REMARK   3      T33:  -0.1128 T12:  -0.0263
REMARK   3      T13:   0.0005 T23:  -0.0405
REMARK   3    L TENSOR
REMARK   3      L11:   1.1617 L22:   1.9162
REMARK   3      L33:   1.2248 L12:   0.0060
REMARK   3      L13:   0.0010 L23:   0.4489
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0032 S12:  -0.0062 S13:   0.1401
REMARK   3      S21:   0.1074 S22:   0.0525 S23:  -0.0827
REMARK   3      S31:  -0.2086 S32:   0.3420 S33:  -0.0493
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 :   F     1        F   215
REMARK   3    ORIGIN FOR THE GROUP (A):  34.1500 -29.4390  44.8010
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0690 T22:  -0.0964
REMARK   3      T33:   0.0592 T12:   0.0359
REMARK   3      T13:  -0.0121 T23:   0.0071
REMARK   3    L TENSOR
REMARK   3      L11:   1.5002 L22:   1.9833
REMARK   3      L33:   1.2891 L12:  -0.2153
REMARK   3      L13:   0.2674 L23:  -0.1429
REMARK   3    S TENSOR
REMARK   3      S11:   0.0298 S12:  -0.0185 S13:  -0.0416
REMARK   3      S21:  -0.0330 S22:   0.0735 S23:   0.5122
REMARK   3      S31:   0.1002 S32:  -0.1331 S33:  -0.1033
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 :   G     1        G   221
REMARK   3    ORIGIN FOR THE GROUP (A):  71.7180 -30.9840  41.5500
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0639 T22:   0.0572
REMARK   3      T33:  -0.1011 T12:   0.0842
REMARK   3      T13:  -0.0163 T23:  -0.0552
REMARK   3    L TENSOR
REMARK   3      L11:   1.3094 L22:   1.6275
REMARK   3      L33:   1.4337 L12:  -0.4242
REMARK   3      L13:  -0.1659 L23:   0.2798
REMARK   3    S TENSOR
REMARK   3      S11:   0.0197 S12:   0.0486 S13:  -0.0245
REMARK   3      S21:  -0.0031 S22:   0.0497 S23:  -0.2590
REMARK   3      S31:   0.0355 S32:   0.4721 S33:  -0.0693
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 :   H     1        H   219
REMARK   3    ORIGIN FOR THE GROUP (A):  43.2020 -46.4980  47.6130
REMARK   3    T TENSOR
REMARK   3      T11:   0.0783 T22:  -0.1590
REMARK   3      T33:  -0.0196 T12:   0.0290
REMARK   3      T13:  -0.0493 T23:  -0.0020
REMARK   3    L TENSOR
REMARK   3      L11:   1.1774 L22:   1.8733
REMARK   3      L33:   0.9115 L12:  -0.3061
REMARK   3      L13:   0.2949 L23:  -0.5044
REMARK   3    S TENSOR
REMARK   3      S11:   0.0679 S12:  -0.0544 S13:  -0.2401
REMARK   3      S21:  -0.0092 S22:   0.0725 S23:   0.2537
REMARK   3      S31:   0.3380 S32:  -0.0513 S33:  -0.1404
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   I     1        I   220
REMARK   3    ORIGIN FOR THE GROUP (A):  67.2840 -15.0740  -4.1330
REMARK   3    T TENSOR
REMARK   3      T11:   0.0215 T22:   0.0030
REMARK   3      T33:  -0.1059 T12:  -0.0811
REMARK   3      T13:   0.0696 T23:  -0.0910
REMARK   3    L TENSOR
REMARK   3      L11:   1.4183 L22:   2.4199
REMARK   3      L33:   1.6786 L12:   0.0131
REMARK   3      L13:  -0.1654 L23:   1.0282
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0039 S12:  -0.0582 S13:   0.2196
REMARK   3      S21:  -0.2405 S22:   0.2299 S23:  -0.2031
REMARK   3      S31:  -0.4413 S32:   0.5007 S33:  -0.2260
REMARK   3
REMARK   3   TLS GROUP : 10
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   J     1        J   215
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1870 -29.5490  -7.2710
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0855 T22:  -0.0680
REMARK   3      T33:   0.0340 T12:   0.0652
REMARK   3      T13:  -0.0235 T23:  -0.0166
REMARK   3    L TENSOR
REMARK   3      L11:   1.6747 L22:   2.0123
REMARK   3      L33:   1.3237 L12:  -0.4051
REMARK   3      L13:   0.1272 L23:  -0.1761
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0083 S12:  -0.0065 S13:  -0.0015
REMARK   3      S21:  -0.0892 S22:   0.0425 S23:   0.5205
REMARK   3      S31:   0.0366 S32:  -0.1601 S33:  -0.0342
REMARK   3
REMARK   3   TLS GROUP : 11
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   K     1        K   219
REMARK   3    ORIGIN FOR THE GROUP (A):  75.5780 -32.5080 -10.1340
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1118 T22:   0.1592
REMARK   3      T33:  -0.0919 T12:   0.0308
REMARK   3      T13:   0.0580 T23:  -0.1598
REMARK   3    L TENSOR
REMARK   3      L11:   1.5545 L22:   2.5217
REMARK   3      L33:   1.9850 L12:  -0.5696
REMARK   3      L13:  -0.3866 L23:   1.1219
REMARK   3    S TENSOR
REMARK   3      S11:   0.0182 S12:  -0.0245 S13:  -0.0138
REMARK   3      S21:  -0.1751 S22:   0.3326 S23:  -0.4400
REMARK   3      S31:  -0.0784 S32:   0.7317 S33:  -0.3508
REMARK   3
REMARK   3   TLS GROUP : 12
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   L     1        L   216
REMARK   3    ORIGIN FOR THE GROUP (A):  46.6990 -46.7420  -4.4690
REMARK   3    T TENSOR
REMARK   3      T11:   0.0333 T22:  -0.1331
REMARK   3      T33:  -0.0222 T12:   0.0520
REMARK   3      T13:  -0.0118 T23:   0.0157
REMARK   3    L TENSOR
REMARK   3      L11:   1.4524 L22:   1.8434
REMARK   3      L33:   1.1096 L12:  -0.4039
REMARK   3      L13:   0.1257 L23:  -0.2659
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0397 S12:  -0.0976 S13:  -0.2945
REMARK   3      S21:   0.0141 S22:   0.1131 S23:   0.2845
REMARK   3      S31:   0.2927 S32:  -0.0301 S33:  -0.0734
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
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 3E3I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048828.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : F2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 205440
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 122.169
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.6
REMARK 200  DATA REDUNDANCY                : 4.800
REMARK 200  R MERGE                    (I) : 0.05500
REMARK 200  R SYM                      (I) : 0.05500
REMARK 200   FOR THE DATA SET  : 19.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.47500
REMARK 200  R SYM FOR SHELL            (I) : 0.47500
REMARK 200   FOR SHELL         : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2A8D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 55.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 1.8 M AMMONIUM SULFATE,
REMARK 280  4% PEG 400, 100 MM SODIUM BICARBONATE, 12 MG/ML PROTEIN, PH 7.5,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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      114.79650
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.21850
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      114.79650
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       72.21850
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, 3
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: 18030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -185.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -164.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, G, F, H
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: 3
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: 17650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -156.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, K, J, L
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     ASN A    22
REMARK 465     SER A    23
REMARK 465     THR A    24
REMARK 465     TYR A    25
REMARK 465     PHE A    26
REMARK 465     LYS A    27
REMARK 465     GLU A    28
REMARK 465     LEU A    29
REMARK 465     ALA A    30
REMARK 465     ASP A    31
REMARK 465     HIS A    32
REMARK 465     GLN A    33
REMARK 465     LEU A   221
REMARK 465     LYS A   222
REMARK 465     LYS A   223
REMARK 465     ASP A   224
REMARK 465     HIS A   225
REMARK 465     LEU A   226
REMARK 465     GLU A   227
REMARK 465     ASN A   228
REMARK 465     THR A   229
REMARK 465     ASN B    22
REMARK 465     SER B    23
REMARK 465     THR B    24
REMARK 465     TYR B    25
REMARK 465     PHE B    26
REMARK 465     LYS B    27
REMARK 465     GLU B    28
REMARK 465     ILE B   220
REMARK 465     LEU B   221
REMARK 465     LYS B   222
REMARK 465     LYS B   223
REMARK 465     ASP B   224
REMARK 465     HIS B   225
REMARK 465     LEU B   226
REMARK 465     GLU B   227
REMARK 465     ASN B   228
REMARK 465     THR B   229
REMARK 465     ASN C    22
REMARK 465     SER C    23
REMARK 465     THR C    24
REMARK 465     TYR C    25
REMARK 465     PHE C    26
REMARK 465     LYS C    27
REMARK 465     GLU C    28
REMARK 465     LEU C    29
REMARK 465     ALA C    30
REMARK 465     ASP C    31
REMARK 465     HIS C    32
REMARK 465     GLN C    33
REMARK 465     LEU C   221
REMARK 465     LYS C   222
REMARK 465     LYS C   223
REMARK 465     ASP C   224
REMARK 465     HIS C   225
REMARK 465     LEU C   226
REMARK 465     GLU C   227
REMARK 465     ASN C   228
REMARK 465     THR C   229
REMARK 465     ASN D    22
REMARK 465     SER D    23
REMARK 465     THR D    24
REMARK 465     TYR D    25
REMARK 465     PHE D    26
REMARK 465     LYS D    27
REMARK 465     GLU D    28
REMARK 465     LEU D   221
REMARK 465     LYS D   222
REMARK 465     LYS D   223
REMARK 465     ASP D   224
REMARK 465     HIS D   225
REMARK 465     LEU D   226
REMARK 465     GLU D   227
REMARK 465     ASN D   228
REMARK 465     THR D   229
REMARK 465     ASN E    22
REMARK 465     SER E    23
REMARK 465     THR E    24
REMARK 465     TYR E    25
REMARK 465     PHE E    26
REMARK 465     LYS E    27
REMARK 465     GLU E    28
REMARK 465     ILE E   220
REMARK 465     LEU E   221
REMARK 465     LYS E   222
REMARK 465     LYS E   223
REMARK 465     ASP E   224
REMARK 465     HIS E   225
REMARK 465     LEU E   226
REMARK 465     GLU E   227
REMARK 465     ASN E   228
REMARK 465     THR E   229
REMARK 465     ASN F    22
REMARK 465     SER F    23
REMARK 465     THR F    24
REMARK 465     TYR F    25
REMARK 465     PHE F    26
REMARK 465     LYS F    27
REMARK 465     GLU F    28
REMARK 465     ASP F   216
REMARK 465     GLU F   217
REMARK 465     GLU F   218
REMARK 465     ASN F   219
REMARK 465     ILE F   220
REMARK 465     LEU F   221
REMARK 465     LYS F   222
REMARK 465     LYS F   223
REMARK 465     ASP F   224
REMARK 465     HIS F   225
REMARK 465     LEU F   226
REMARK 465     GLU F   227
REMARK 465     ASN F   228
REMARK 465     THR F   229
REMARK 465     ASN G    22
REMARK 465     SER G    23
REMARK 465     THR G    24
REMARK 465     TYR G    25
REMARK 465     PHE G    26
REMARK 465     LYS G    27
REMARK 465     GLU G    28
REMARK 465     LYS G   222
REMARK 465     LYS G   223
REMARK 465     ASP G   224
REMARK 465     HIS G   225
REMARK 465     LEU G   226
REMARK 465     GLU G   227
REMARK 465     ASN G   228
REMARK 465     THR G   229
REMARK 465     ASN H    22
REMARK 465     SER H    23
REMARK 465     THR H    24
REMARK 465     TYR H    25
REMARK 465     PHE H    26
REMARK 465     LYS H    27
REMARK 465     GLU H    28
REMARK 465     LEU H    29
REMARK 465     ALA H    30
REMARK 465     ASP H    31
REMARK 465     ILE H   220
REMARK 465     LEU H   221
REMARK 465     LYS H   222
REMARK 465     LYS H   223
REMARK 465     ASP H   224
REMARK 465     HIS H   225
REMARK 465     LEU H   226
REMARK 465     GLU H   227
REMARK 465     ASN H   228
REMARK 465     THR H   229
REMARK 465     ASN I    22
REMARK 465     SER I    23
REMARK 465     THR I    24
REMARK 465     TYR I    25
REMARK 465     PHE I    26
REMARK 465     LYS I    27
REMARK 465     GLU I    28
REMARK 465     LEU I    29
REMARK 465     ALA I    30
REMARK 465     ASP I    31
REMARK 465     LEU I   221
REMARK 465     LYS I   222
REMARK 465     LYS I   223
REMARK 465     ASP I   224
REMARK 465     HIS I   225
REMARK 465     LEU I   226
REMARK 465     GLU I   227
REMARK 465     ASN I   228
REMARK 465     THR I   229
REMARK 465     ASN J    22
REMARK 465     SER J    23
REMARK 465     THR J    24
REMARK 465     TYR J    25
REMARK 465     PHE J    26
REMARK 465     LYS J    27
REMARK 465     GLU J    28
REMARK 465     LEU J    29
REMARK 465     ALA J    30
REMARK 465     ASP J    31
REMARK 465     ASP J   216
REMARK 465     GLU J   217
REMARK 465     GLU J   218
REMARK 465     ASN J   219
REMARK 465     ILE J   220
REMARK 465     LEU J   221
REMARK 465     LYS J   222
REMARK 465     LYS J   223
REMARK 465     ASP J   224
REMARK 465     HIS J   225
REMARK 465     LEU J   226
REMARK 465     GLU J   227
REMARK 465     ASN J   228
REMARK 465     THR J   229
REMARK 465     ASN K    22
REMARK 465     SER K    23
REMARK 465     THR K    24
REMARK 465     TYR K    25
REMARK 465     PHE K    26
REMARK 465     LYS K    27
REMARK 465     GLU K    28
REMARK 465     LEU K    29
REMARK 465     ALA K    30
REMARK 465     ASP K    31
REMARK 465     ILE K   220
REMARK 465     LEU K   221
REMARK 465     LYS K   222
REMARK 465     LYS K   223
REMARK 465     ASP K   224
REMARK 465     HIS K   225
REMARK 465     LEU K   226
REMARK 465     GLU K   227
REMARK 465     ASN K   228
REMARK 465     THR K   229
REMARK 465     ASN L    22
REMARK 465     SER L    23
REMARK 465     THR L    24
REMARK 465     TYR L    25
REMARK 465     PHE L    26
REMARK 465     LYS L    27
REMARK 465     GLU L    28
REMARK 465     LEU L    29
REMARK 465     ALA L    30
REMARK 465     ASP L    31
REMARK 465     GLU L   217
REMARK 465     GLU L   218
REMARK 465     ASN L   219
REMARK 465     ILE L   220
REMARK 465     LEU L   221
REMARK 465     LYS L   222
REMARK 465     LYS L   223
REMARK 465     ASP L   224
REMARK 465     HIS L   225
REMARK 465     LEU L   226
REMARK 465     GLU L   227
REMARK 465     ASN L   228
REMARK 465     THR L   229
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     ASN G 219    CG   OD1
REMARK 470     ASN I 219    OD1
REMARK 470     ILE I 220    CG1  CG2  CD1
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    MET C     1     O    HOH C   273              2.03
REMARK 500   N    MET A     1     O    HOH A   271              2.17
REMARK 500   O    HOH K   271     O    HOH K   273              2.18
REMARK 500   NH2  ARG C   198     OE2  GLU C   202              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LEU A  52   CA  -  CB  -  CG  ANGL. DEV. =  19.2 DEGREES
REMARK 500    ARG C  64   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG C  64   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG F 160   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG G 170   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
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    ASP A 110       35.48    -98.57
REMARK 500    GLU A 217       66.16    -49.65
REMARK 500    GLU A 218       47.95   -144.58
REMARK 500    HIS B  32       73.75   -119.86
REMARK 500    ASP B 185      -13.79   -143.29
REMARK 500    GLU B 217      -53.63     -5.06
REMARK 500    GLU C 217       67.86    -67.35
REMARK 500    HIS D  32       72.20   -104.53
REMARK 500    ASP D 185      -13.17   -141.21
REMARK 500    HIS E  32       69.09   -113.66
REMARK 500    HIS F  32       70.36   -102.69
REMARK 500    ASP F 185      -20.27   -141.71
REMARK 500    HIS G  32       66.61   -115.69
REMARK 500    SER I  45       60.02     39.99
REMARK 500    ASN I 219      -96.38    -75.51
REMARK 500    GLU J 140      -70.96    -53.11
REMARK 500    ASP J 185      -19.50   -148.40
REMARK 500    ASP K 185      -18.31   -142.79
REMARK 500    ASP L 185      -13.28   -143.15
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 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  42   SG
REMARK 620 2 ASP A  44   OD2 103.4
REMARK 620 3 HIS A  98   NE2 117.2  86.9
REMARK 620 4 CYS A 101   SG  112.1 123.1 112.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B  42   SG
REMARK 620 2 ASP B  44   OD2 101.3
REMARK 620 3 HIS B  98   NE2 121.7 105.7
REMARK 620 4 CYS B 101   SG  112.4 108.8 106.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN C 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C  42   SG
REMARK 620 2 ASP C  44   OD2 105.1
REMARK 620 3 HIS C  98   NE2 121.0  91.8
REMARK 620 4 CYS C 101   SG  110.4 119.9 108.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN D 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D  42   SG
REMARK 620 2 ASP D  44   OD2 101.5
REMARK 620 3 HIS D  98   NE2 122.8 100.3
REMARK 620 4 CYS D 101   SG  112.2 108.8 109.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN E 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E  42   SG
REMARK 620 2 ASP E  44   OD2  99.9
REMARK 620 3 HIS E  98   NE2 114.3 104.1
REMARK 620 4 CYS E 101   SG  117.8 109.6 109.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN F 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F  42   SG
REMARK 620 2 ASP F  44   OD2 103.4
REMARK 620 3 HIS F  98   NE2 116.9  99.5
REMARK 620 4 CYS F 101   SG  114.1 109.4 111.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN G 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G  42   SG
REMARK 620 2 ASP G  44   OD2 110.2
REMARK 620 3 HIS G  98   NE2 111.3 104.2
REMARK 620 4 CYS G 101   SG  116.1 104.4 109.7
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN H 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H  42   SG
REMARK 620 2 ASP H  44   OD2 109.2
REMARK 620 3 HIS H  98   NE2 120.3  93.9
REMARK 620 4 CYS H 101   SG  114.9 109.5 106.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN I 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I  42   SG
REMARK 620 2 ASP I  44   OD2 104.5
REMARK 620 3 HIS I  98   NE2 113.0 101.9
REMARK 620 4 CYS I 101   SG  118.4 109.1 108.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN J 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J  42   SG
REMARK 620 2 ASP J  44   OD2 106.7
REMARK 620 3 HIS J  98   NE2 113.5 106.0
REMARK 620 4 CYS J 101   SG  111.3 108.5 110.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN K 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K  42   SG
REMARK 620 2 ASP K  44   OD2 103.3
REMARK 620 3 HIS K  98   NE2 114.7  99.5
REMARK 620 4 CYS K 101   SG  118.1 107.8 111.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN L 230  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L  42   SG
REMARK 620 2 ASP L  44   OD2 108.9
REMARK 620 3 HIS L  98   NE2 119.9  97.9
REMARK 620 4 CYS L 101   SG  111.5 107.5 109.8
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 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT B 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT C 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT D 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT E 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT F 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT G 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT H 233
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT I 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT J 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 K 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT K 232
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 231
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT L 232
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A8C   RELATED DB: PDB
REMARK 900 RELATED ID: 2A8D   RELATED DB: PDB
REMARK 900 RELATED ID: 3E24   RELATED DB: PDB
REMARK 900 RELATED ID: 3E28   RELATED DB: PDB
REMARK 900 RELATED ID: 3E2A   RELATED DB: PDB
REMARK 900 RELATED ID: 3E2W   RELATED DB: PDB
REMARK 900 RELATED ID: 3E2X   RELATED DB: PDB
REMARK 900 RELATED ID: 3E31   RELATED DB: PDB
REMARK 900 RELATED ID: 3E3F   RELATED DB: PDB
REMARK 900 RELATED ID: 3E3G   RELATED DB: PDB
DBREF  3E3I A    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I B    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I C    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I D    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I E    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I F    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I G    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I H    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I I    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I J    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I K    1   229  UNP    P45148   CAN_HAEIN        1    229
DBREF  3E3I L    1   229  UNP    P45148   CAN_HAEIN        1    229
SEQADV 3E3I ALA A   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA B   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA C   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA D   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA E   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA F   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA G   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA H   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA I   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA J   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA K   41  UNP  P45148    GLY    41 ENGINEERED
SEQADV 3E3I ALA L   41  UNP  P45148    GLY    41 ENGINEERED
SEQRES   1 A  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 A  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 A  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 A  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 A  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 A  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 A  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 A  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 A  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 A  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 A  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 A  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 A  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 A  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 A  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 A  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 A  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 A  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 B  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 B  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 B  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 B  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 B  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 B  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 B  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 B  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 B  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 B  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 B  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 B  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 B  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 B  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 B  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 B  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 B  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 B  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 C  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 C  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 C  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 C  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 C  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 C  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 C  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 C  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 C  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 C  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 C  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 C  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 C  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 C  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 C  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 C  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 C  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 C  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 D  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 D  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 D  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 D  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 D  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 D  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 D  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 D  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 D  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 D  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 D  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 D  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 D  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 D  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 D  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 D  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 D  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 D  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 E  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 E  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 E  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 E  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 E  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 E  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 E  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 E  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 E  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 E  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 E  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 E  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 E  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 E  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 E  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 E  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 E  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 E  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 F  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 F  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 F  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 F  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 F  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 F  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 F  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 F  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 F  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 F  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 F  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 F  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 F  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 F  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 F  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 F  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 F  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 F  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 G  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 G  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 G  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 G  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 G  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 G  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 G  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 G  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 G  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 G  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 G  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 G  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 G  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 G  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 G  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 G  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 G  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 G  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 H  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 H  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 H  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 H  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 H  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 H  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 H  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 H  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 H  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 H  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 H  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 H  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 H  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 H  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 H  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 H  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 H  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 H  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 I  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 I  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 I  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 I  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 I  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 I  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 I  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 I  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 I  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 I  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 I  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 I  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 I  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 I  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 I  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 I  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 I  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 I  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 J  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 J  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 J  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 J  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 J  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 J  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 J  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 J  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 J  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 J  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 J  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 J  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 J  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 J  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 J  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 J  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 J  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 J  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 K  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 K  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 K  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 K  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 K  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 K  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 K  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 K  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 K  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 K  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 K  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 K  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 K  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 K  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 K  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 K  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 K  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 K  229  LYS LYS ASP HIS LEU GLU ASN THR
SEQRES   1 L  229  MET ASP LYS ILE LYS GLN LEU PHE ALA ASN ASN TYR SER
SEQRES   2 L  229  TRP ALA GLN ARG MET LYS GLU GLU ASN SER THR TYR PHE
SEQRES   3 L  229  LYS GLU LEU ALA ASP HIS GLN THR PRO HIS TYR LEU TRP
SEQRES   4 L  229  ILE ALA CYS SER ASP SER ARG VAL PRO ALA GLU LYS LEU
SEQRES   5 L  229  THR ASN LEU GLU PRO GLY GLU LEU PHE VAL HIS ARG ASN
SEQRES   6 L  229  VAL ALA ASN GLN VAL ILE HIS THR ASP PHE ASN CYS LEU
SEQRES   7 L  229  SER VAL VAL GLN TYR ALA VAL ASP VAL LEU LYS ILE GLU
SEQRES   8 L  229  HIS ILE ILE ILE CYS GLY HIS THR ASN CYS GLY GLY ILE
SEQRES   9 L  229  HIS ALA ALA MET ALA ASP LYS ASP LEU GLY LEU ILE ASN
SEQRES  10 L  229  ASN TRP LEU LEU HIS ILE ARG ASP ILE TRP PHE LYS HIS
SEQRES  11 L  229  GLY HIS LEU LEU GLY LYS LEU SER PRO GLU LYS ARG ALA
SEQRES  12 L  229  ASP MET LEU THR LYS ILE ASN VAL ALA GLU GLN VAL TYR
SEQRES  13 L  229  ASN LEU GLY ARG THR SER ILE VAL LYS SER ALA TRP GLU
SEQRES  14 L  229  ARG GLY GLN LYS LEU SER LEU HIS GLY TRP VAL TYR ASP
SEQRES  15 L  229  VAL ASN ASP GLY PHE LEU VAL ASP GLN GLY VAL MET ALA
SEQRES  16 L  229  THR SER ARG GLU THR LEU GLU ILE SER TYR ARG ASN ALA
SEQRES  17 L  229  ILE ALA ARG LEU SER ILE LEU ASP GLU GLU ASN ILE LEU
SEQRES  18 L  229  LYS LYS ASP HIS LEU GLU ASN THR
HET     ZN  A 230       1
HET    SO4  A 231       5
HET     ZN  B 230       1
HET    SO4  B 231       5
HET    SO4  B 232       5
HET    BCT  B 233       4
HET     ZN  C 230       1
HET    SO4  C 231       5
HET    BCT  C 232       4
HET     ZN  D 230       1
HET    SO4  D 231       5
HET    BCT  D 232       4
HET     ZN  E 230       1
HET    SO4  E 231       5
HET    SO4  E 232       5
HET    BCT  E 233       4
HET     ZN  F 230       1
HET    BCT  F 231       4
HET     ZN  G 230       1
HET    BCT  G 231       4
HET     ZN  H 230       1
HET    SO4  H 231       5
HET    SO4  H 232       5
HET    BCT  H 233       4
HET     ZN  I 230       1
HET    SO4  I 231       5
HET    BCT  I 232       4
HET     ZN  J 230       1
HET    SO4  J 231       5
HET    BCT  J 232       4
HET     ZN  K 230       1
HET    SO4  K 231       5
HET    BCT  K 232       4
HET     ZN  L 230       1
HET    SO4  L 231       5
HET    BCT  L 232       4
HETNAM      ZN ZINC ION
HETNAM     SO4 SULFATE ION
HETNAM     BCT BICARBONATE ION
FORMUL  13   ZN    12(ZN 2+)
FORMUL  14  SO4    13(O4 S 2-)
FORMUL  18  BCT    11(C H O3 1-)
FORMUL  49  HOH   *604(H2 O)
HELIX    1   1 MET A    1  GLU A   21  1                                  21
HELIX    2   2 PRO A   48  ASN A   54  1                                   7
HELIX    3   3 ASP A   74  VAL A   87  1                                  14
HELIX    4   4 CYS A  101  ALA A  109  1                                   9
HELIX    5   5 LEU A  115  HIS A  130  1                                  16
HELIX    6   6 HIS A  130  LYS A  136  1                                   7
HELIX    7   7 LEU A  137  GLU A  140  5                                   4
HELIX    8   8 LYS A  141  ARG A  160  1                                  20
HELIX    9   9 THR A  161  ARG A  170  1                                  10
HELIX   10  10 SER A  197  SER A  213  1                                  17
HELIX   11  11 MET B    1  GLU B   21  1                                  21
HELIX   12  12 PRO B   48  ASN B   54  1                                   7
HELIX   13  13 ASP B   74  VAL B   87  1                                  14
HELIX   14  14 CYS B  101  ALA B  109  1                                   9
HELIX   15  15 LEU B  115  HIS B  130  1                                  16
HELIX   16  16 HIS B  130  LYS B  136  1                                   7
HELIX   17  17 SER B  138  THR B  161  1                                  24
HELIX   18  18 THR B  161  ARG B  170  1                                  10
HELIX   19  19 SER B  197  SER B  213  1                                  17
HELIX   20  20 ASP C    2  GLU C   21  1                                  20
HELIX   21  21 PRO C   48  ASN C   54  1                                   7
HELIX   22  22 ASP C   74  VAL C   87  1                                  14
HELIX   23  23 CYS C  101  ALA C  109  1                                   9
HELIX   24  24 LEU C  115  HIS C  130  1                                  16
HELIX   25  25 HIS C  130  LYS C  136  1                                   7
HELIX   26  26 LEU C  137  GLU C  140  5                                   4
HELIX   27  27 LYS C  141  THR C  161  1                                  21
HELIX   28  28 THR C  161  ARG C  170  1                                  10
HELIX   29  29 SER C  197  SER C  213  1                                  17
HELIX   30  30 MET D    1  GLU D   21  1                                  21
HELIX   31  31 PRO D   48  ASN D   54  1                                   7
HELIX   32  32 ASP D   74  VAL D   87  1                                  14
HELIX   33  33 CYS D  101  ALA D  109  1                                   9
HELIX   34  34 GLY D  114  HIS D  130  1                                  17
HELIX   35  35 HIS D  130  LYS D  136  1                                   7
HELIX   36  36 LEU D  137  GLU D  140  5                                   4
HELIX   37  37 LYS D  141  ARG D  160  1                                  20
HELIX   38  38 THR D  161  ARG D  170  1                                  10
HELIX   39  39 SER D  197  SER D  213  1                                  17
HELIX   40  40 MET E    1  GLU E   21  1                                  21
HELIX   41  41 PRO E   48  ASN E   54  1                                   7
HELIX   42  42 ASP E   74  VAL E   87  1                                  14
HELIX   43  43 CYS E  101  ALA E  109  1                                   9
HELIX   44  44 GLY E  114  HIS E  130  1                                  17
HELIX   45  45 HIS E  130  LEU E  137  1                                   8
HELIX   46  46 SER E  138  ARG E  160  1                                  23
HELIX   47  47 THR E  161  ARG E  170  1                                  10
HELIX   48  48 SER E  197  ILE E  214  1                                  18
HELIX   49  49 MET F    1  GLU F   21  1                                  21
HELIX   50  50 PRO F   48  ASN F   54  1                                   7
HELIX   51  51 ASP F   74  VAL F   87  1                                  14
HELIX   52  52 CYS F  101  ALA F  109  1                                   9
HELIX   53  53 GLY F  114  HIS F  130  1                                  17
HELIX   54  54 HIS F  130  GLY F  135  1                                   6
HELIX   55  55 SER F  138  THR F  161  1                                  24
HELIX   56  56 THR F  161  ARG F  170  1                                  10
HELIX   57  57 SER F  197  ILE F  214  1                                  18
HELIX   58  58 MET G    1  GLU G   20  1                                  20
HELIX   59  59 PRO G   48  ASN G   54  1                                   7
HELIX   60  60 ASP G   74  VAL G   87  1                                  14
HELIX   61  61 CYS G  101  ALA G  109  1                                   9
HELIX   62  62 GLY G  114  HIS G  130  1                                  17
HELIX   63  63 HIS G  130  LYS G  136  1                                   7
HELIX   64  64 LEU G  137  GLU G  140  5                                   4
HELIX   65  65 LYS G  141  THR G  161  1                                  21
HELIX   66  66 THR G  161  ARG G  170  1                                  10
HELIX   67  67 SER G  197  ILE G  214  1                                  18
HELIX   68  68 ASP G  216  ILE G  220  5                                   5
HELIX   69  69 MET H    1  GLU H   21  1                                  21
HELIX   70  70 PRO H   48  ASN H   54  1                                   7
HELIX   71  71 ASP H   74  VAL H   87  1                                  14
HELIX   72  72 CYS H  101  ALA H  109  1                                   9
HELIX   73  73 GLY H  114  HIS H  130  1                                  17
HELIX   74  74 HIS H  130  LYS H  136  1                                   7
HELIX   75  75 LEU H  137  GLU H  140  5                                   4
HELIX   76  76 LYS H  141  ARG H  160  1                                  20
HELIX   77  77 THR H  161  ARG H  170  1                                  10
HELIX   78  78 SER H  197  SER H  213  1                                  17
HELIX   79  79 MET I    1  GLU I   21  1                                  21
HELIX   80  80 PRO I   48  ASN I   54  1                                   7
HELIX   81  81 ASP I   74  VAL I   87  1                                  14
HELIX   82  82 CYS I  101  ALA I  109  1                                   9
HELIX   83  83 GLY I  114  HIS I  130  1                                  17
HELIX   84  84 HIS I  130  LEU I  137  1                                   8
HELIX   85  85 SER I  138  GLU I  140  5                                   3
HELIX   86  86 LYS I  141  ARG I  160  1                                  20
HELIX   87  87 THR I  161  GLY I  171  1                                  11
HELIX   88  88 SER I  197  SER I  213  1                                  17
HELIX   89  89 MET J    1  GLU J   21  1                                  21
HELIX   90  90 PRO J   48  ASN J   54  1                                   7
HELIX   91  91 ASP J   74  VAL J   87  1                                  14
HELIX   92  92 CYS J  101  ALA J  109  1                                   9
HELIX   93  93 GLY J  114  HIS J  130  1                                  17
HELIX   94  94 HIS J  130  GLY J  135  1                                   6
HELIX   95  95 SER J  138  ARG J  160  1                                  23
HELIX   96  96 THR J  161  GLY J  171  1                                  11
HELIX   97  97 SER J  197  SER J  213  1                                  17
HELIX   98  98 MET K    1  GLU K   20  1                                  20
HELIX   99  99 PRO K   48  ASN K   54  1                                   7
HELIX  100 100 ASP K   74  VAL K   87  1                                  14
HELIX  101 101 CYS K  101  ALA K  109  1                                   9
HELIX  102 102 GLY K  114  HIS K  130  1                                  17
HELIX  103 103 HIS K  130  LEU K  137  1                                   8
HELIX  104 104 SER K  138  ARG K  160  1                                  23
HELIX  105 105 THR K  161  ARG K  170  1                                  10
HELIX  106 106 SER K  197  SER K  213  1                                  17
HELIX  107 107 MET L    1  GLU L   21  1                                  21
HELIX  108 108 PRO L   48  ASN L   54  1                                   7
HELIX  109 109 ASP L   74  VAL L   87  1                                  14
HELIX  110 110 CYS L  101  ALA L  109  1                                   9
HELIX  111 111 GLY L  114  HIS L  130  1                                  17
HELIX  112 112 HIS L  130  LEU L  137  1                                   8
HELIX  113 113 SER L  138  GLU L  140  5                                   3
HELIX  114 114 LYS L  141  ARG L  160  1                                  20
HELIX  115 115 THR L  161  ARG L  170  1                                  10
HELIX  116 116 SER L  197  SER L  213  1                                  17
SHEET    1   A 5 LEU A  60  ASN A  65  0
SHEET    2   A 5 TYR 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  LEU A  38
SHEET    4   A 5 SER A 175  TYR A 181  1  O  TYR A 181   N  GLY A  97
SHEET    5   A 5 LEU A 188  ALA A 195 -1  O  VAL A 189   N  VAL A 180
SHEET    1   B 5 LEU B  60  ASN B  65  0
SHEET    2   B 5 TYR 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  ILE B  40
SHEET    4   B 5 SER B 175  TYR B 181  1  O  TRP B 179   N  ILE B  95
SHEET    5   B 5 LEU B 188  ALA B 195 -1  O  VAL B 189   N  VAL B 180
SHEET    1   C 5 LEU C  60  ASN C  65  0
SHEET    2   C 5 TYR C  37  CYS C  42  1  N  TRP C  39   O  PHE C  61
SHEET    3   C 5 HIS C  92  HIS C  98  1  O  ILE C  94   N  ILE C  40
SHEET    4   C 5 SER C 175  TYR C 181  1  O  HIS C 177   N  ILE C  95
SHEET    5   C 5 LEU C 188  ALA C 195 -1  O  VAL C 189   N  VAL C 180
SHEET    1   D 5 LEU D  60  ASN D  65  0
SHEET    2   D 5 TYR D  37  CYS D  42  1  N  TRP D  39   O  PHE D  61
SHEET    3   D 5 HIS D  92  HIS D  98  1  O  ILE D  94   N  LEU D  38
SHEET    4   D 5 SER D 175  TYR D 181  1  O  TRP D 179   N  ILE D  95
SHEET    5   D 5 LEU D 188  ASP D 190 -1  O  VAL D 189   N  VAL D 180
SHEET    1   E 5 LEU E  60  ASN E  65  0
SHEET    2   E 5 TYR E  37  CYS E  42  1  N  TRP E  39   O  PHE E  61
SHEET    3   E 5 HIS E  92  HIS E  98  1  O  ILE E  94   N  ILE E  40
SHEET    4   E 5 SER E 175  TYR E 181  1  O  SER E 175   N  ILE E  93
SHEET    5   E 5 LEU E 188  ALA E 195 -1  O  VAL E 189   N  VAL E 180
SHEET    1   F 5 LEU F  60  ASN F  65  0
SHEET    2   F 5 TYR F  37  CYS F  42  1  N  TRP F  39   O  PHE F  61
SHEET    3   F 5 HIS F  92  HIS F  98  1  O  ILE F  94   N  ILE F  40
SHEET    4   F 5 SER F 175  TYR F 181  1  O  TRP F 179   N  GLY F  97
SHEET    5   F 5 LEU F 188  ALA F 195 -1  O  VAL F 189   N  VAL F 180
SHEET    1   G 5 LEU G  60  ASN G  65  0
SHEET    2   G 5 TYR G  37  CYS G  42  1  N  TRP G  39   O  PHE G  61
SHEET    3   G 5 HIS G  92  HIS G  98  1  O  ILE G  94   N  LEU G  38
SHEET    4   G 5 SER G 175  TYR G 181  1  O  HIS G 177   N  ILE G  95
SHEET    5   G 5 LEU G 188  ALA G 195 -1  O  VAL G 189   N  VAL G 180
SHEET    1   H 5 LEU H  60  ASN H  65  0
SHEET    2   H 5 TYR H  37  CYS H  42  1  N  TRP H  39   O  PHE H  61
SHEET    3   H 5 HIS H  92  HIS H  98  1  O  ILE H  94   N  ILE H  40
SHEET    4   H 5 SER H 175  TYR H 181  1  O  TRP H 179   N  ILE H  95
SHEET    5   H 5 LEU H 188  ALA H 195 -1  O  ALA H 195   N  LEU H 176
SHEET    1   I 5 LEU I  60  ASN I  65  0
SHEET    2   I 5 TYR I  37  CYS I  42  1  N  TRP I  39   O  PHE I  61
SHEET    3   I 5 HIS I  92  HIS I  98  1  O  ILE I  94   N  ILE I  40
SHEET    4   I 5 SER I 175  TYR I 181  1  O  TRP I 179   N  ILE I  95
SHEET    5   I 5 LEU I 188  ALA I 195 -1  O  GLN I 191   N  GLY I 178
SHEET    1   J 5 LEU J  60  ASN J  65  0
SHEET    2   J 5 TYR J  37  CYS J  42  1  N  TRP J  39   O  PHE J  61
SHEET    3   J 5 HIS J  92  HIS J  98  1  O  ILE J  94   N  ILE J  40
SHEET    4   J 5 SER J 175  TYR J 181  1  O  TRP J 179   N  ILE J  95
SHEET    5   J 5 LEU J 188  ALA J 195 -1  O  VAL J 189   N  VAL J 180
SHEET    1   K 5 LEU K  60  ASN K  65  0
SHEET    2   K 5 TYR K  37  CYS K  42  1  N  TRP K  39   O  PHE K  61
SHEET    3   K 5 HIS K  92  HIS K  98  1  O  ILE K  94   N  LEU K  38
SHEET    4   K 5 SER K 175  TYR K 181  1  O  HIS K 177   N  ILE K  95
SHEET    5   K 5 LEU K 188  ASP K 190 -1  O  VAL K 189   N  VAL K 180
SHEET    1   L 5 LEU L  60  ASN L  65  0
SHEET    2   L 5 TYR L  37  CYS L  42  1  N  TRP L  39   O  PHE L  61
SHEET    3   L 5 HIS L  92  HIS L  98  1  O  ILE L  94   N  LEU L  38
SHEET    4   L 5 SER L 175  TYR L 181  1  O  SER L 175   N  ILE L  93
SHEET    5   L 5 LEU L 188  ALA L 195 -1  O  GLN L 191   N  GLY L 178
LINK         SG  CYS A  42                ZN    ZN A 230     1555   1555  2.32
LINK         OD2 ASP A  44                ZN    ZN A 230     1555   1555  1.98
LINK         NE2 HIS A  98                ZN    ZN A 230     1555   1555  2.08
LINK         SG  CYS A 101                ZN    ZN A 230     1555   1555  2.27
LINK         SG  CYS B  42                ZN    ZN B 230     1555   1555  2.35
LINK         OD2 ASP B  44                ZN    ZN B 230     1555   1555  2.01
LINK         NE2 HIS B  98                ZN    ZN B 230     1555   1555  2.07
LINK         SG  CYS B 101                ZN    ZN B 230     1555   1555  2.28
LINK         SG  CYS C  42                ZN    ZN C 230     1555   1555  2.31
LINK         OD2 ASP C  44                ZN    ZN C 230     1555   1555  1.99
LINK         NE2 HIS C  98                ZN    ZN C 230     1555   1555  2.07
LINK         SG  CYS C 101                ZN    ZN C 230     1555   1555  2.26
LINK         SG  CYS D  42                ZN    ZN D 230     1555   1555  2.37
LINK         OD2 ASP D  44                ZN    ZN D 230     1555   1555  1.99
LINK         NE2 HIS D  98                ZN    ZN D 230     1555   1555  2.09
LINK         SG  CYS D 101                ZN    ZN D 230     1555   1555  2.26
LINK         SG  CYS E  42                ZN    ZN E 230     1555   1555  2.30
LINK         OD2 ASP E  44                ZN    ZN E 230     1555   1555  2.04
LINK         NE2 HIS E  98                ZN    ZN E 230     1555   1555  2.07
LINK         SG  CYS E 101                ZN    ZN E 230     1555   1555  2.29
LINK         SG  CYS F  42                ZN    ZN F 230     1555   1555  2.32
LINK         OD2 ASP F  44                ZN    ZN F 230     1555   1555  1.96
LINK         NE2 HIS F  98                ZN    ZN F 230     1555   1555  2.06
LINK         SG  CYS F 101                ZN    ZN F 230     1555   1555  2.31
LINK         SG  CYS G  42                ZN    ZN G 230     1555   1555  2.35
LINK         OD2 ASP G  44                ZN    ZN G 230     1555   1555  2.01
LINK         NE2 HIS G  98                ZN    ZN G 230     1555   1555  2.08
LINK         SG  CYS G 101                ZN    ZN G 230     1555   1555  2.29
LINK         SG  CYS H  42                ZN    ZN H 230     1555   1555  2.35
LINK         OD2 ASP H  44                ZN    ZN H 230     1555   1555  2.00
LINK         NE2 HIS H  98                ZN    ZN H 230     1555   1555  2.06
LINK         SG  CYS H 101                ZN    ZN H 230     1555   1555  2.28
LINK         SG  CYS I  42                ZN    ZN I 230     1555   1555  2.32
LINK         OD2 ASP I  44                ZN    ZN I 230     1555   1555  2.02
LINK         NE2 HIS I  98                ZN    ZN I 230     1555   1555  2.06
LINK         SG  CYS I 101                ZN    ZN I 230     1555   1555  2.27
LINK         SG  CYS J  42                ZN    ZN J 230     1555   1555  2.32
LINK         OD2 ASP J  44                ZN    ZN J 230     1555   1555  1.97
LINK         NE2 HIS J  98                ZN    ZN J 230     1555   1555  2.08
LINK         SG  CYS J 101                ZN    ZN J 230     1555   1555  2.31
LINK         SG  CYS K  42                ZN    ZN K 230     1555   1555  2.31
LINK         OD2 ASP K  44                ZN    ZN K 230     1555   1555  2.03
LINK         NE2 HIS K  98                ZN    ZN K 230     1555   1555  2.07
LINK         SG  CYS K 101                ZN    ZN K 230     1555   1555  2.29
LINK         SG  CYS L  42                ZN    ZN L 230     1555   1555  2.34
LINK         OD2 ASP L  44                ZN    ZN L 230     1555   1555  2.00
LINK         NE2 HIS L  98                ZN    ZN L 230     1555   1555  2.07
LINK         SG  CYS L 101                ZN    ZN L 230     1555   1555  2.31
SITE     1 AC1  4 CYS A  42  ASP A  44  HIS A  98  CYS A 101
SITE     1 AC2  7 SER A  45  ARG A  46  VAL A  47  HIS A  98
SITE     2 AC2  7 TYR A 181  VAL A 183  HOH A 278
SITE     1 AC3  4 CYS B  42  ASP B  44  HIS B  98  CYS B 101
SITE     1 AC4  4 LEU A 121  ARG A 124  ARG B 160  ARG B 198
SITE     1 AC5  5 ARG A 160  ARG A 198  LEU B 121  ARG B 124
SITE     2 AC5  5 PHE B 128
SITE     1 AC6 10 TRP B  39  ALA B  41  VAL B  47  PRO B  48
SITE     2 AC6 10 ALA B  49  LEU B  52  ARG B  64  TYR B 181
SITE     3 AC6 10 HOH B 248  HOH B 260
SITE     1 AC7  4 CYS C  42  ASP C  44  HIS C  98  CYS C 101
SITE     1 AC8  5 LEU C 121  ARG C 124  HOH C 270  ARG D 160
SITE     2 AC8  5 ARG D 198
SITE     1 AC9  8 PRO A  48  ARG A  64  HOH A 238  PRO C  48
SITE     2 AC9  8 ALA C  49  GLU C  50  ARG C  64  HOH C 268
SITE     1 BC1  4 CYS D  42  ASP D  44  HIS D  98  CYS D 101
SITE     1 BC2  6 ARG C 160  LYS C 165  ARG C 198  LEU D 121
SITE     2 BC2  6 ARG D 124  PHE D 128
SITE     1 BC3  9 TRP D  39  ALA D  41  VAL D  47  PRO D  48
SITE     2 BC3  9 ALA D  49  LEU D  52  ARG D  64  TYR D 181
SITE     3 BC3  9 HOH D 276
SITE     1 BC4  4 CYS E  42  ASP E  44  HIS E  98  CYS E 101
SITE     1 BC5  6 LEU E 121  ARG E 124  PHE E 128  HOH E 260
SITE     2 BC5  6 ARG F 160  ARG F 198
SITE     1 BC6  6 ARG E 160  LYS E 165  ARG E 198  HOH E 277
SITE     2 BC6  6 LEU F 121  ARG F 124
SITE     1 BC7  9 TRP E  39  ALA E  41  VAL E  47  PRO E  48
SITE     2 BC7  9 ALA E  49  LEU E  52  ARG E  64  TYR E 181
SITE     3 BC7  9 HOH E 253
SITE     1 BC8  4 CYS F  42  ASP F  44  HIS F  98  CYS F 101
SITE     1 BC9  9 TRP F  39  ALA F  41  VAL F  47  PRO F  48
SITE     2 BC9  9 ALA F  49  LEU F  52  ARG F  64  TYR F 181
SITE     3 BC9  9 HOH F 260
SITE     1 CC1  4 CYS G  42  ASP G  44  HIS G  98  CYS G 101
SITE     1 CC2  9 TRP G  39  ALA G  41  VAL G  47  PRO G  48
SITE     2 CC2  9 ALA G  49  ARG G  64  TYR G 181  HOH G 235
SITE     3 CC2  9 HOH G 244
SITE     1 CC3  4 CYS H  42  ASP H  44  HIS H  98  CYS H 101
SITE     1 CC4  5 LEU G 121  ARG G 124  ARG H 160  LYS H 165
SITE     2 CC4  5 ARG H 198
SITE     1 CC5  6 ARG G 160  LYS G 165  ARG G 198  LEU H 121
SITE     2 CC5  6 ARG H 124  HOH H 283
SITE     1 CC6  9 TRP H  39  ALA H  41  VAL H  47  PRO H  48
SITE     2 CC6  9 ALA H  49  LEU H  52  ARG H  64  TYR H 181
SITE     3 CC6  9 HOH H 250
SITE     1 CC7  4 CYS I  42  ASP I  44  HIS I  98  CYS I 101
SITE     1 CC8  5 ARG I 160  ARG I 198  HOH I 270  HOH I 275
SITE     2 CC8  5 ARG J 124
SITE     1 CC9  8 TRP I  39  ALA I  41  VAL I  47  ALA I  49
SITE     2 CC9  8 ARG I  64  TYR I 181  HOH I 240  HOH I 249
SITE     1 DC1  4 CYS J  42  ASP J  44  HIS J  98  CYS J 101
SITE     1 DC2  5 LEU I 121  ARG I 124  ARG J 160  LYS J 165
SITE     2 DC2  5 ARG J 198
SITE     1 DC3  9 TRP J  39  ALA J  41  VAL J  47  PRO J  48
SITE     2 DC3  9 ALA J  49  LEU J  52  ARG J  64  TYR J 181
SITE     3 DC3  9 HOH J 256
SITE     1 DC4  4 CYS K  42  ASP K  44  HIS K  98  CYS K 101
SITE     1 DC5  4 LEU K 121  ARG K 124  ARG L 160  ARG L 198
SITE     1 DC6  8 TRP K  39  ALA K  41  VAL K  47  ALA K  49
SITE     2 DC6  8 ARG K  64  TYR K 181  HOH K 236  HOH K 247
SITE     1 DC7  4 CYS L  42  ASP L  44  HIS L  98  CYS L 101
SITE     1 DC8  6 ARG K 160  LYS K 165  ARG K 198  LEU L 121
SITE     2 DC8  6 ARG L 124  HOH L 258
SITE     1 DC9  9 TRP L  39  ALA L  41  VAL L  47  PRO L  48
SITE     2 DC9  9 ALA L  49  ARG L  64  TYR L 181  HOH L 237
SITE     3 DC9  9 HOH L 245
CRYST1  229.593  144.437  104.891  90.00  94.43  90.00 C 1 2 1      48
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      0.004356  0.000000  0.000337        0.00000
SCALE2      0.000000  0.006923  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009562        0.00000
      
PROCHECK
Go to PROCHECK summary
 References