HEADER GENE REGULATION 12-JAN-10 3LD0
TITLE CRYSTAL STRUCTURE OF B.LICHENIFORMIS ANTI-TRAP PROTEIN, AN ANTAGONIST
TITLE 2 OF TRAP-RNA INTERACTIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INHIBITOR OF TRAP, REGULATED BY T-BOX (TRP) SEQUENCE RTPA;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U,
COMPND 4 V, W, X, Y, Z, 1, 2, 3, 4, 5, 6, 7, 8, 9, a, b, c, d, e, f, g, h, i,
COMPND 5 j, k, l, m;
COMPND 6 SYNONYM: YCZA;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;
SOURCE 3 ORGANISM_TAXID: 279010;
SOURCE 4 STRAIN: 5A32;
SOURCE 5 ATCC: 14580;
SOURCE 6 GENE: BL05022, BLI00308, RTPA, RTPA (YCZA), YCZA;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA BL21(DE3) COMPETENT CELLS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS ANTI-TRAP, AT, TRAP, TRYPTOPHAN RNA-BINDING ATTENUATION PROTEIN,
KEYWDS 2 TRANSCRIPTION ATTENUATION, ANTITERMINATION, TRANSCRIPTION FACTORS,
KEYWDS 3 TRYPTOPHAN BIOSYNTHESIS REGULATION, GENE REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.B.SHEVTSOV,Y.CHEN,M.N.ISUPOV,P.GOLLNICK,A.A.ANTSON
REVDAT 4 06-SEP-23 3LD0 1 REMARK LINK
REVDAT 3 13-JUL-11 3LD0 1 VERSN
REVDAT 2 31-MAR-10 3LD0 1 JRNL
REVDAT 1 23-FEB-10 3LD0 0
JRNL AUTH M.B.SHEVTSOV,Y.CHEN,M.N.ISUPOV,A.LEECH,P.GOLLNICK,A.A.ANTSON
JRNL TITL BACILLUS LICHENIFORMIS ANTI-TRAP CAN ASSEMBLE INTO TWO TYPES
JRNL TITL 2 OF DODECAMERIC PARTICLES WITH THE SAME SYMMETRY BUT INVERTED
JRNL TITL 3 ORIENTATION OF TRIMERS.
JRNL REF J.STRUCT.BIOL. V. 170 127 2010
JRNL REFN ISSN 1047-8477
JRNL PMID 20138150
JRNL DOI 10.1016/J.JSB.2010.01.013
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0008
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 127405
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1300
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9293
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19034
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 1335
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 28.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.288
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.230
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.176
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.811
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19706 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 26559 ; 1.204 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2507 ; 2.693 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 731 ;30.950 ;26.060
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3519 ; 8.451 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ; 5.755 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3079 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14356 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9655 ; 0.262 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 13813 ; 0.317 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1904 ; 0.242 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 91 ; 0.274 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 65 ; 0.323 ; 0.500
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): 13081 ; 1.842 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 20605 ; 2.705 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7060 ; 4.102 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5945 ; 6.395 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 16
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 53
REMARK 3 RESIDUE RANGE : C 201 C 253
REMARK 3 RESIDUE RANGE : B 101 B 153
REMARK 3 ORIGIN FOR THE GROUP (A): -49.9673 11.6975 18.7544
REMARK 3 T TENSOR
REMARK 3 T11: -0.0498 T22: -0.0826
REMARK 3 T33: -0.0438 T12: -0.0266
REMARK 3 T13: -0.0234 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 0.4581 L22: 0.4301
REMARK 3 L33: 0.7558 L12: -0.1408
REMARK 3 L13: -0.0373 L23: -0.1050
REMARK 3 S TENSOR
REMARK 3 S11: -0.0307 S12: -0.0165 S13: -0.0422
REMARK 3 S21: 0.0391 S22: -0.0101 S23: -0.0416
REMARK 3 S31: -0.0114 S32: 0.0100 S33: 0.0409
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 101 E 153
REMARK 3 RESIDUE RANGE : D 1 D 53
REMARK 3 RESIDUE RANGE : F 201 F 253
REMARK 3 ORIGIN FOR THE GROUP (A): -69.6016 0.2785 11.0280
REMARK 3 T TENSOR
REMARK 3 T11: -0.1294 T22: -0.0623
REMARK 3 T33: -0.0735 T12: 0.0020
REMARK 3 T13: 0.0142 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.2907 L22: 0.3165
REMARK 3 L33: 0.5416 L12: -0.1070
REMARK 3 L13: -0.0179 L23: -0.1424
REMARK 3 S TENSOR
REMARK 3 S11: -0.0134 S12: -0.0752 S13: -0.0367
REMARK 3 S21: 0.1068 S22: 0.0092 S23: 0.0154
REMARK 3 S31: 0.0376 S32: 0.0068 S33: 0.0042
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 201 I 253
REMARK 3 RESIDUE RANGE : H 101 H 152
REMARK 3 RESIDUE RANGE : G 1 G 52
REMARK 3 ORIGIN FOR THE GROUP (A): -50.5809 -12.3852 18.8402
REMARK 3 T TENSOR
REMARK 3 T11: -0.0748 T22: -0.0756
REMARK 3 T33: -0.0732 T12: 0.0265
REMARK 3 T13: -0.0179 T23: 0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 0.6656 L22: 0.5079
REMARK 3 L33: 0.4244 L12: -0.0925
REMARK 3 L13: -0.0669 L23: 0.0377
REMARK 3 S TENSOR
REMARK 3 S11: 0.0217 S12: 0.0010 S13: 0.0539
REMARK 3 S21: 0.0997 S22: -0.0011 S23: -0.0290
REMARK 3 S31: 0.0185 S32: 0.0549 S33: -0.0206
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 101 K 153
REMARK 3 RESIDUE RANGE : J 1 J 53
REMARK 3 RESIDUE RANGE : L 201 L 253
REMARK 3 ORIGIN FOR THE GROUP (A): -49.3894 -0.2398 -1.9568
REMARK 3 T TENSOR
REMARK 3 T11: -0.0855 T22: -0.0196
REMARK 3 T33: -0.0535 T12: 0.0131
REMARK 3 T13: 0.0123 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.3093 L22: 0.5755
REMARK 3 L33: 0.4487 L12: -0.2045
REMARK 3 L13: 0.1836 L23: -0.0665
REMARK 3 S TENSOR
REMARK 3 S11: 0.0301 S12: -0.0260 S13: 0.1055
REMARK 3 S21: 0.0891 S22: -0.0304 S23: -0.1049
REMARK 3 S31: -0.0448 S32: 0.1751 S33: 0.0003
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 1 M 53
REMARK 3 RESIDUE RANGE : O 201 O 253
REMARK 3 RESIDUE RANGE : N 101 N 152
REMARK 3 ORIGIN FOR THE GROUP (A): -97.2186 36.9443 57.3221
REMARK 3 T TENSOR
REMARK 3 T11: -0.0242 T22: -0.0096
REMARK 3 T33: -0.0504 T12: -0.0138
REMARK 3 T13: 0.0333 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.3170 L22: 0.9204
REMARK 3 L33: 0.6570 L12: 0.0529
REMARK 3 L13: 0.1506 L23: 0.1950
REMARK 3 S TENSOR
REMARK 3 S11: 0.0215 S12: 0.0152 S13: 0.0661
REMARK 3 S21: 0.0520 S22: -0.0084 S23: 0.0587
REMARK 3 S31: 0.0019 S32: -0.0570 S33: -0.0131
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 101 Q 153
REMARK 3 RESIDUE RANGE : P 1 P 53
REMARK 3 RESIDUE RANGE : R 201 R 253
REMARK 3 ORIGIN FOR THE GROUP (A): -98.4346 24.6456 36.7364
REMARK 3 T TENSOR
REMARK 3 T11: -0.0661 T22: -0.0708
REMARK 3 T33: -0.0533 T12: -0.0238
REMARK 3 T13: -0.0071 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 0.4613 L22: 0.7517
REMARK 3 L33: 1.0553 L12: -0.1013
REMARK 3 L13: 0.0577 L23: -0.0758
REMARK 3 S TENSOR
REMARK 3 S11: 0.0139 S12: -0.0632 S13: 0.0499
REMARK 3 S21: 0.0421 S22: -0.0166 S23: 0.0492
REMARK 3 S31: 0.0193 S32: -0.0986 S33: 0.0027
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 1 S 53
REMARK 3 RESIDUE RANGE : U 201 U 253
REMARK 3 RESIDUE RANGE : T 101 T 153
REMARK 3 ORIGIN FOR THE GROUP (A): -78.2950 36.7569 42.4913
REMARK 3 T TENSOR
REMARK 3 T11: -0.0803 T22: 0.0450
REMARK 3 T33: 0.0233 T12: -0.0084
REMARK 3 T13: 0.0294 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.2404 L22: 0.8856
REMARK 3 L33: 0.5765 L12: 0.1467
REMARK 3 L13: 0.0153 L23: 0.1462
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: 0.0323 S13: -0.0115
REMARK 3 S21: -0.0272 S22: 0.0452 S23: -0.1501
REMARK 3 S31: -0.0873 S32: 0.0742 S33: -0.0353
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : X 201 X 253
REMARK 3 RESIDUE RANGE : W 101 W 153
REMARK 3 RESIDUE RANGE : V 1 V 53
REMARK 3 ORIGIN FOR THE GROUP (A): -98.3097 48.5485 36.2222
REMARK 3 T TENSOR
REMARK 3 T11: 0.0010 T22: -0.0391
REMARK 3 T33: -0.0145 T12: 0.0152
REMARK 3 T13: -0.0121 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 0.3748 L22: 0.7228
REMARK 3 L33: 1.0812 L12: 0.1476
REMARK 3 L13: 0.0064 L23: 0.3082
REMARK 3 S TENSOR
REMARK 3 S11: -0.0140 S12: 0.0409 S13: 0.0098
REMARK 3 S21: -0.0941 S22: -0.0289 S23: 0.0409
REMARK 3 S31: -0.1189 S32: -0.0221 S33: 0.0429
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Y 1 Y 53
REMARK 3 RESIDUE RANGE : 1 201 1 253
REMARK 3 RESIDUE RANGE : Z 101 Z 152
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5512 -1.0239 19.1179
REMARK 3 T TENSOR
REMARK 3 T11: -0.0252 T22: -0.0673
REMARK 3 T33: -0.0588 T12: -0.0478
REMARK 3 T13: -0.0359 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.3883 L22: 0.5930
REMARK 3 L33: 0.8273 L12: -0.1247
REMARK 3 L13: -0.1330 L23: -0.1090
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: -0.0730 S13: -0.0707
REMARK 3 S21: 0.1068 S22: -0.0261 S23: -0.0726
REMARK 3 S31: -0.0118 S32: 0.0140 S33: 0.0251
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 3 101 3 153
REMARK 3 RESIDUE RANGE : 2 1 2 52
REMARK 3 RESIDUE RANGE : 4 201 4 252
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7479 -12.7972 10.8421
REMARK 3 T TENSOR
REMARK 3 T11: -0.1375 T22: -0.0702
REMARK 3 T33: -0.0542 T12: -0.0119
REMARK 3 T13: 0.0137 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 0.3653 L22: 0.8612
REMARK 3 L33: 0.5266 L12: -0.1182
REMARK 3 L13: -0.0063 L23: -0.1370
REMARK 3 S TENSOR
REMARK 3 S11: 0.0040 S12: -0.0794 S13: -0.0267
REMARK 3 S21: 0.1481 S22: -0.0330 S23: 0.0672
REMARK 3 S31: -0.0423 S32: -0.0068 S33: 0.0290
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 5 1 5 53
REMARK 3 RESIDUE RANGE : 7 201 7 253
REMARK 3 RESIDUE RANGE : 6 101 6 153
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5861 -25.0315 18.8946
REMARK 3 T TENSOR
REMARK 3 T11: -0.0313 T22: -0.0561
REMARK 3 T33: -0.0388 T12: 0.0223
REMARK 3 T13: -0.0200 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 0.5848 L22: 0.6364
REMARK 3 L33: 0.5562 L12: 0.1434
REMARK 3 L13: 0.1317 L23: 0.0870
REMARK 3 S TENSOR
REMARK 3 S11: 0.0274 S12: 0.0294 S13: 0.0783
REMARK 3 S21: 0.0837 S22: -0.0483 S23: -0.1289
REMARK 3 S31: -0.0012 S32: 0.1209 S33: 0.0209
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : 9 101 9 153
REMARK 3 RESIDUE RANGE : 8 1 8 53
REMARK 3 RESIDUE RANGE : a 201 a 253
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7498 -12.9069 -1.7115
REMARK 3 T TENSOR
REMARK 3 T11: -0.1060 T22: -0.0465
REMARK 3 T33: -0.0542 T12: 0.0084
REMARK 3 T13: 0.0159 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.1071 L22: 0.7868
REMARK 3 L33: 0.5753 L12: -0.1168
REMARK 3 L13: 0.1603 L23: -0.0078
REMARK 3 S TENSOR
REMARK 3 S11: 0.0218 S12: -0.0557 S13: 0.0130
REMARK 3 S21: 0.0685 S22: -0.0242 S23: -0.0872
REMARK 3 S31: 0.0070 S32: 0.1423 S33: 0.0023
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : c 101 c 153
REMARK 3 RESIDUE RANGE : b 1 b 53
REMARK 3 RESIDUE RANGE : d 201 d 253
REMARK 3 ORIGIN FOR THE GROUP (A): -38.0368 49.5022 57.1191
REMARK 3 T TENSOR
REMARK 3 T11: 0.0180 T22: 0.0187
REMARK 3 T33: -0.0339 T12: -0.0063
REMARK 3 T13: 0.0265 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.3451 L22: 0.6584
REMARK 3 L33: 0.5621 L12: 0.1726
REMARK 3 L13: 0.0150 L23: 0.1531
REMARK 3 S TENSOR
REMARK 3 S11: 0.0249 S12: -0.0122 S13: 0.0929
REMARK 3 S21: 0.0377 S22: -0.0006 S23: 0.0598
REMARK 3 S31: -0.0147 S32: -0.0704 S33: -0.0243
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : e 1 e 53
REMARK 3 RESIDUE RANGE : g 201 g 253
REMARK 3 RESIDUE RANGE : f 101 f 153
REMARK 3 ORIGIN FOR THE GROUP (A): -38.4627 37.3785 36.5059
REMARK 3 T TENSOR
REMARK 3 T11: -0.0808 T22: -0.0649
REMARK 3 T33: -0.0508 T12: -0.0165
REMARK 3 T13: -0.0189 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 0.4130 L22: 0.7894
REMARK 3 L33: 1.1791 L12: -0.0195
REMARK 3 L13: 0.0273 L23: 0.0289
REMARK 3 S TENSOR
REMARK 3 S11: 0.0143 S12: -0.1291 S13: 0.0132
REMARK 3 S21: 0.1280 S22: 0.0084 S23: -0.0017
REMARK 3 S31: 0.0078 S32: -0.0976 S33: -0.0228
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : i 101 i 153
REMARK 3 RESIDUE RANGE : h 1 h 53
REMARK 3 RESIDUE RANGE : j 201 j 253
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3217 50.6045 42.2207
REMARK 3 T TENSOR
REMARK 3 T11: -0.0613 T22: 0.0323
REMARK 3 T33: 0.0044 T12: -0.0180
REMARK 3 T13: 0.0156 T23: -0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 0.2024 L22: 0.7215
REMARK 3 L33: 0.7574 L12: 0.0059
REMARK 3 L13: -0.0591 L23: 0.2463
REMARK 3 S TENSOR
REMARK 3 S11: -0.0153 S12: -0.0161 S13: -0.0048
REMARK 3 S21: 0.0075 S22: 0.0814 S23: -0.1108
REMARK 3 S31: -0.0986 S32: 0.0933 S33: -0.0661
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : k 1 k 53
REMARK 3 RESIDUE RANGE : m 201 m 253
REMARK 3 RESIDUE RANGE : l 101 l 152
REMARK 3 ORIGIN FOR THE GROUP (A): -40.0185 61.3846 36.2592
REMARK 3 T TENSOR
REMARK 3 T11: 0.0147 T22: -0.0186
REMARK 3 T33: -0.0074 T12: 0.0496
REMARK 3 T13: 0.0058 T23: 0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 0.2302 L22: 0.7214
REMARK 3 L33: 1.1957 L12: 0.1314
REMARK 3 L13: 0.0749 L23: 0.2901
REMARK 3 S TENSOR
REMARK 3 S11: 0.0142 S12: -0.0160 S13: 0.0266
REMARK 3 S21: -0.0261 S22: -0.0334 S23: 0.0329
REMARK 3 S31: -0.1917 S32: -0.0858 S33: 0.0192
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: NULL
REMARK 4
REMARK 4 3LD0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000057125.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JAN-05
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128724
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 38.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.28000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2BX9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL PH 8.0-8.5 BUFFER, 0.2
REMARK 280 M OF MGCL2 SALT AND 20-25 % OF POLY(ETHYLENE) GLYCOL 3350, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 49.93250
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -209.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -215.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P, Q, R, S, T, U, V,
REMARK 350 AND CHAINS: W, X
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -216.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y, Z, 1, 2, 3, 4, 5, 6, 7, 8,
REMARK 350 AND CHAINS: 9, a
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -204.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: b, c, d, e, f, g, h, i, j, k,
REMARK 350 AND CHAINS: l, m
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 GLU G 53
REMARK 465 GLU H 153
REMARK 465 GLU N 153
REMARK 465 GLU Z 153
REMARK 465 GLU 2 53
REMARK 465 GLU 4 253
REMARK 465 GLU l 153
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASN Q 114 CG OD1 ND2
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 GLU b 53 OXT GLU c 153 1.86
REMARK 500 O HOH G 55 O HOH G 617 1.86
REMARK 500 NZ LYS l 132 O HOH l 982 1.87
REMARK 500 NZ LYS P 48 OE1 GLU P 53 1.88
REMARK 500 O HOH L 420 O HOH L 673 1.89
REMARK 500 OE1 GLU W 153 O HOH W 1167 1.93
REMARK 500 O HIS O 252 O HOH O 1125 2.00
REMARK 500 O ASP H 106 O HOH H 651 2.03
REMARK 500 O HOH c 917 O HOH k 484 2.04
REMARK 500 O HOH 3 1014 O HOH 3 1062 2.05
REMARK 500 ND2 ASN B 116 ND2 ASN R 214 2.07
REMARK 500 O ILE S 51 N GLU S 53 2.08
REMARK 500 OXT GLU S 53 OXT GLU U 253 2.08
REMARK 500 OE1 GLU f 153 O HOH f 193 2.08
REMARK 500 CD2 LEU 2 44 CE2 PHE 3 146 2.08
REMARK 500 O HOH F 635 O HOH F 636 2.10
REMARK 500 O HOH 4 406 O HOH 4 699 2.11
REMARK 500 O HOH l 981 O HOH l 982 2.13
REMARK 500 NZ LYS i 148 O HOH i 1299 2.13
REMARK 500 ND2 ASN Z 114 O HOH Z 1226 2.13
REMARK 500 OD1 ASP D 6 O HOH D 1079 2.13
REMARK 500 O HOH M 841 O HOH O 843 2.14
REMARK 500 O GLU l 121 O HOH l 1101 2.15
REMARK 500 OE1 GLU e 53 OE1 GLU g 253 2.15
REMARK 500 O HOH F 477 O HOH F 630 2.15
REMARK 500 O HOH P 491 O HOH P 1141 2.15
REMARK 500 NZ LYS S 48 O HOH S 856 2.16
REMARK 500 O ILE 9 151 OE2 GLU 9 153 2.16
REMARK 500 O ILE J 51 N GLU J 53 2.16
REMARK 500 O ILE A 51 O HOH A 1070 2.16
REMARK 500 O ILE C 251 O HOH C 1072 2.16
REMARK 500 O HOH D 1079 O HOH L 525 2.17
REMARK 500 O ILE K 151 OE1 GLU K 153 2.17
REMARK 500 O HOH E 154 O HOH E 774 2.17
REMARK 500 OE2 GLU Q 153 O ILE V 51 2.17
REMARK 500 O ILE V 51 N GLU V 53 2.17
REMARK 500 OE2 GLU W 153 O HOH W 1083 2.18
REMARK 500 CG2 THR U 210 O HOH U 1191 2.18
REMARK 500 O HOH W 893 O HOH W 1244 2.18
REMARK 500 OD1 ASP f 106 O HOH f 293 2.18
REMARK 500 O HOH A 998 O HOH J 999 2.18
REMARK 500 O PRO 1 227 O HOH 1 681 2.19
REMARK 500 O HOH 2 700 O HOH 5 1318 2.19
REMARK 500 NZ LYS U 232 O HOH U 852 2.19
REMARK 500 O LYS j 248 N HIS j 252 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH N 1069 O HOH T 1217 2446 2.02
REMARK 500 O HOH c 352 O HOH i 964 2546 2.05
REMARK 500 O HOH K 1162 O HOH L 1085 2445 2.14
REMARK 500 O HOH D 741 O HOH K 1164 2455 2.16
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 GLU A 22 139.65 -27.09
REMARK 500 HIS A 52 -23.06 60.69
REMARK 500 GLU B 122 141.07 -37.10
REMARK 500 HIS B 152 66.73 26.79
REMARK 500 GLU C 221 59.93 -143.78
REMARK 500 GLU C 222 136.03 -24.00
REMARK 500 HIS C 252 -47.81 91.28
REMARK 500 GLU D 22 135.99 -39.33
REMARK 500 HIS D 52 -51.44 71.24
REMARK 500 HIS E 152 -39.76 64.40
REMARK 500 PRO F 223 30.58 -92.87
REMARK 500 HIS F 252 -19.14 76.97
REMARK 500 GLU G 22 134.79 -33.49
REMARK 500 GLU H 122 134.62 -34.04
REMARK 500 GLU I 221 60.91 -150.78
REMARK 500 GLU I 222 133.21 -22.64
REMARK 500 HIS I 252 -59.93 55.16
REMARK 500 GLU J 21 55.63 -146.80
REMARK 500 GLU J 22 127.64 -18.79
REMARK 500 HIS J 52 -51.04 56.88
REMARK 500 GLU K 122 135.14 -35.15
REMARK 500 HIS K 152 -59.25 61.49
REMARK 500 GLU L 222 136.92 -38.34
REMARK 500 HIS L 252 -62.81 88.51
REMARK 500 GLU M 22 130.54 -17.56
REMARK 500 HIS M 52 -47.32 63.96
REMARK 500 GLU N 122 136.86 -31.84
REMARK 500 GLU O 222 134.96 -27.21
REMARK 500 HIS O 252 -45.36 62.51
REMARK 500 GLU P 22 128.19 -8.34
REMARK 500 GLU Q 121 56.86 -141.62
REMARK 500 GLU Q 122 133.21 -18.87
REMARK 500 HIS Q 152 12.90 59.48
REMARK 500 GLU R 222 135.76 -32.59
REMARK 500 HIS R 252 -55.31 65.44
REMARK 500 GLU S 22 134.56 -33.36
REMARK 500 HIS S 52 -52.33 46.36
REMARK 500 GLU T 122 140.76 -35.04
REMARK 500 PRO T 123 31.21 -91.81
REMARK 500 HIS T 152 -51.86 64.30
REMARK 500 GLU U 222 137.63 -36.42
REMARK 500 HIS U 252 -42.05 69.48
REMARK 500 GLU V 22 133.59 -26.09
REMARK 500 HIS V 52 -44.34 51.93
REMARK 500 GLU W 122 135.88 -27.51
REMARK 500 HIS W 152 -63.99 76.02
REMARK 500 GLU X 222 135.20 -27.37
REMARK 500 GLU Y 22 134.94 -33.58
REMARK 500 HIS Y 52 -43.61 60.66
REMARK 500 GLU Z 121 59.36 -140.78
REMARK 500
REMARK 500 THIS ENTRY HAS 104 RAMACHANDRAN OUTLIERS.
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 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 SG
REMARK 620 2 CYS A 15 SG 110.0
REMARK 620 3 CYS A 26 SG 114.7 112.1
REMARK 620 4 CYS A 29 SG 110.9 102.7 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 53 O
REMARK 620 2 GLU B 153 O 90.0
REMARK 620 3 GLU C 253 O 124.8 109.8
REMARK 620 4 GLU C 253 OXT 90.7 77.4 48.4
REMARK 620 5 HOH C1000 O 108.6 121.8 103.3 151.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 112 SG
REMARK 620 2 CYS B 115 SG 106.1
REMARK 620 3 CYS B 126 SG 115.6 113.7
REMARK 620 4 CYS B 129 SG 114.3 102.0 104.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 212 SG
REMARK 620 2 CYS C 215 SG 102.1
REMARK 620 3 CYS C 226 SG 116.1 115.7
REMARK 620 4 CYS C 229 SG 113.6 100.5 107.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 12 SG
REMARK 620 2 CYS D 15 SG 105.4
REMARK 620 3 CYS D 26 SG 117.1 114.0
REMARK 620 4 CYS D 29 SG 110.1 104.4 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 54 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 53 O
REMARK 620 2 GLU D 53 OXT 54.2
REMARK 620 3 HOH D 500 O 91.3 132.6
REMARK 620 4 GLU E 153 O 106.5 82.7 143.1
REMARK 620 5 GLU E 153 OXT 121.7 126.7 98.0 45.1
REMARK 620 6 GLU F 253 O 137.6 84.8 113.3 74.7 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 112 SG
REMARK 620 2 CYS E 115 SG 105.8
REMARK 620 3 CYS E 126 SG 115.0 114.0
REMARK 620 4 CYS E 129 SG 111.0 104.9 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 212 SG
REMARK 620 2 CYS F 215 SG 104.0
REMARK 620 3 CYS F 226 SG 113.4 112.5
REMARK 620 4 CYS F 229 SG 115.3 106.0 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 12 SG
REMARK 620 2 CYS G 15 SG 106.4
REMARK 620 3 CYS G 26 SG 115.6 112.5
REMARK 620 4 CYS G 29 SG 111.6 103.6 106.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 112 SG
REMARK 620 2 CYS H 115 SG 102.3
REMARK 620 3 CYS H 126 SG 118.2 113.3
REMARK 620 4 CYS H 129 SG 113.0 104.6 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I 3 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU I 253 O
REMARK 620 2 GLU I 253 OXT 47.2
REMARK 620 3 HOH I1335 O 129.4 82.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 212 SG
REMARK 620 2 CYS I 215 SG 105.9
REMARK 620 3 CYS I 226 SG 120.4 110.9
REMARK 620 4 CYS I 229 SG 114.5 100.4 103.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 12 SG
REMARK 620 2 CYS J 15 SG 96.6
REMARK 620 3 CYS J 26 SG 123.8 113.7
REMARK 620 4 CYS J 29 SG 113.2 97.8 108.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG J 54 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU J 53 O
REMARK 620 2 GLU K 153 O 83.8
REMARK 620 3 HOH K 671 O 126.4 101.2
REMARK 620 4 GLU L 253 O 111.9 110.8 115.4
REMARK 620 5 GLU L 253 OXT 67.4 100.2 155.6 44.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN K 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 112 SG
REMARK 620 2 CYS K 115 SG 107.1
REMARK 620 3 CYS K 126 SG 112.6 113.2
REMARK 620 4 CYS K 129 SG 111.8 104.9 107.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 212 SG
REMARK 620 2 CYS L 215 SG 106.5
REMARK 620 3 CYS L 226 SG 116.0 116.2
REMARK 620 4 CYS L 229 SG 109.9 102.1 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN M 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 12 SG
REMARK 620 2 CYS M 15 SG 98.8
REMARK 620 3 CYS M 26 SG 122.7 119.9
REMARK 620 4 CYS M 29 SG 107.9 104.7 101.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG O 5 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU M 53 O
REMARK 620 2 GLU O 253 O 104.9
REMARK 620 3 HOH O 842 O 117.6 102.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN N 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 112 SG
REMARK 620 2 CYS N 115 SG 106.9
REMARK 620 3 CYS N 126 SG 118.9 109.4
REMARK 620 4 CYS N 129 SG 110.5 104.6 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN O 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS O 212 SG
REMARK 620 2 CYS O 215 SG 106.3
REMARK 620 3 CYS O 226 SG 113.6 117.8
REMARK 620 4 CYS O 229 SG 108.6 109.4 100.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN P 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS P 12 SG
REMARK 620 2 CYS P 15 SG 106.5
REMARK 620 3 CYS P 26 SG 124.5 107.4
REMARK 620 4 CYS P 29 SG 110.5 97.7 106.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG R 6 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU P 53 O
REMARK 620 2 GLU Q 153 O 79.2
REMARK 620 3 GLU R 253 O 82.3 83.4
REMARK 620 4 HOH R 559 O 140.1 136.4 113.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN Q 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 112 SG
REMARK 620 2 CYS Q 115 SG 106.9
REMARK 620 3 CYS Q 126 SG 116.0 112.2
REMARK 620 4 CYS Q 129 SG 111.2 105.5 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN R 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 212 SG
REMARK 620 2 CYS R 215 SG 105.7
REMARK 620 3 CYS R 226 SG 116.9 110.9
REMARK 620 4 CYS R 229 SG 112.5 106.5 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN S 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 12 SG
REMARK 620 2 CYS S 15 SG 107.6
REMARK 620 3 CYS S 26 SG 119.1 112.2
REMARK 620 4 CYS S 29 SG 109.6 99.9 106.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG S 54 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU S 53 O
REMARK 620 2 GLU S 53 OXT 45.1
REMARK 620 3 GLU T 153 O 107.7 117.4
REMARK 620 4 GLU U 253 O 124.1 86.2 120.6
REMARK 620 5 GLU U 253 OXT 88.4 44.0 101.8 57.1
REMARK 620 6 HOH U1209 O 100.8 128.5 108.9 89.3 143.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN T 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS T 112 SG
REMARK 620 2 CYS T 115 SG 99.5
REMARK 620 3 CYS T 126 SG 130.1 105.9
REMARK 620 4 CYS T 129 SG 118.2 103.4 96.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN U 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS U 212 SG
REMARK 620 2 CYS U 215 SG 103.9
REMARK 620 3 CYS U 226 SG 118.3 118.1
REMARK 620 4 CYS U 229 SG 107.8 103.3 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN V 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS V 12 SG
REMARK 620 2 CYS V 15 SG 104.3
REMARK 620 3 CYS V 26 SG 115.6 115.0
REMARK 620 4 CYS V 29 SG 110.8 103.7 106.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG V 54 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU V 53 O
REMARK 620 2 GLU V 53 OXT 48.1
REMARK 620 3 HOH V 460 O 101.5 135.1
REMARK 620 4 GLU W 153 O 110.8 65.1 115.1
REMARK 620 5 GLU X 253 O 105.7 85.3 139.4 82.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN W 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS W 112 SG
REMARK 620 2 CYS W 115 SG 98.4
REMARK 620 3 CYS W 126 SG 128.0 112.2
REMARK 620 4 CYS W 129 SG 103.6 103.9 108.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN X 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS X 212 SG
REMARK 620 2 CYS X 215 SG 99.8
REMARK 620 3 CYS X 226 SG 118.3 119.4
REMARK 620 4 CYS X 229 SG 114.5 102.3 102.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN Y 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Y 12 SG
REMARK 620 2 CYS Y 15 SG 105.1
REMARK 620 3 CYS Y 26 SG 114.2 114.0
REMARK 620 4 CYS Y 29 SG 112.5 104.0 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 1 9 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU Y 53 O
REMARK 620 2 GLU 1 253 O 117.3
REMARK 620 3 HOH 3 798 O 115.4 105.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN Z 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Z 112 SG
REMARK 620 2 CYS Z 115 SG 105.5
REMARK 620 3 CYS Z 126 SG 115.9 112.5
REMARK 620 4 CYS Z 129 SG 110.5 102.2 109.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN 1 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS 1 212 SG
REMARK 620 2 CYS 1 215 SG 106.8
REMARK 620 3 CYS 1 226 SG 120.3 114.3
REMARK 620 4 CYS 1 229 SG 111.3 99.1 103.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 3 10 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH 1 810 O
REMARK 620 2 GLU 3 153 O 119.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN 2 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS 2 12 SG
REMARK 620 2 CYS 2 15 SG 103.1
REMARK 620 3 CYS 2 26 SG 118.2 112.8
REMARK 620 4 CYS 2 29 SG 112.7 105.9 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN 3 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS 3 112 SG
REMARK 620 2 CYS 3 115 SG 104.9
REMARK 620 3 CYS 3 126 SG 116.9 113.0
REMARK 620 4 CYS 3 129 SG 110.0 106.6 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN 4 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS 4 212 SG
REMARK 620 2 CYS 4 215 SG 105.0
REMARK 620 3 CYS 4 226 SG 121.9 111.4
REMARK 620 4 CYS 4 229 SG 112.8 101.1 102.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN 5 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS 5 12 SG
REMARK 620 2 CYS 5 15 SG 105.0
REMARK 620 3 CYS 5 26 SG 113.5 113.6
REMARK 620 4 CYS 5 29 SG 111.4 105.3 107.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 5 54 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU 5 53 OXT
REMARK 620 2 GLU 5 53 O 61.7
REMARK 620 3 HOH 5 566 O 144.2 87.0
REMARK 620 4 GLU 6 153 O 82.2 124.0 104.4
REMARK 620 5 GLU 7 253 O 114.3 110.9 91.9 123.0
REMARK 620 6 GLU 7 253 OXT 66.1 107.6 146.1 92.8 54.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN 6 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS 6 112 SG
REMARK 620 2 CYS 6 115 SG 106.2
REMARK 620 3 CYS 6 126 SG 117.1 114.4
REMARK 620 4 CYS 6 129 SG 113.1 101.3 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN 7 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS 7 212 SG
REMARK 620 2 CYS 7 215 SG 112.4
REMARK 620 3 CYS 7 226 SG 116.4 114.2
REMARK 620 4 CYS 7 229 SG 111.9 98.3 101.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN 8 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS 8 12 SG
REMARK 620 2 CYS 8 15 SG 102.1
REMARK 620 3 CYS 8 26 SG 120.0 113.5
REMARK 620 4 CYS 8 29 SG 116.7 101.3 102.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 8 54 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU 8 53 O
REMARK 620 2 GLU 8 53 OXT 55.4
REMARK 620 3 HOH 8 832 O 103.6 158.7
REMARK 620 4 GLU 9 153 O 117.5 83.6 106.4
REMARK 620 5 GLU a 253 O 124.8 91.8 105.0 98.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN 9 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS 9 112 SG
REMARK 620 2 CYS 9 115 SG 107.4
REMARK 620 3 CYS 9 126 SG 113.3 114.1
REMARK 620 4 CYS 9 129 SG 110.6 105.1 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN a 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS a 212 SG
REMARK 620 2 CYS a 215 SG 105.4
REMARK 620 3 CYS a 226 SG 114.8 115.1
REMARK 620 4 CYS a 229 SG 110.6 105.2 105.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN b 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS b 12 SG
REMARK 620 2 CYS b 15 SG 101.8
REMARK 620 3 CYS b 26 SG 120.7 121.0
REMARK 620 4 CYS b 29 SG 113.1 100.7 98.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG b 54 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU b 53 O
REMARK 620 2 GLU b 53 OXT 50.3
REMARK 620 3 GLU c 153 OXT 54.1 100.1
REMARK 620 4 GLU c 153 O 102.0 112.3 62.6
REMARK 620 5 HOH c 907 O 142.3 94.0 141.3 78.6
REMARK 620 6 GLU d 253 O 133.1 141.9 107.0 103.8 81.3
REMARK 620 7 GLU d 253 OXT 104.4 94.5 125.9 150.7 88.2 47.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN c 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS c 112 SG
REMARK 620 2 CYS c 115 SG 109.9
REMARK 620 3 CYS c 126 SG 116.9 112.6
REMARK 620 4 CYS c 129 SG 108.5 101.9 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN d 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS d 212 SG
REMARK 620 2 CYS d 215 SG 104.0
REMARK 620 3 CYS d 226 SG 116.8 114.5
REMARK 620 4 CYS d 229 SG 112.4 106.1 102.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN e 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS e 12 SG
REMARK 620 2 CYS e 15 SG 97.5
REMARK 620 3 CYS e 26 SG 128.3 106.7
REMARK 620 4 CYS e 29 SG 113.4 91.3 111.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG g 14 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU e 53 O
REMARK 620 2 HOH e1293 O 91.8
REMARK 620 3 GLU f 153 O 110.2 111.9
REMARK 620 4 GLU g 253 O 117.7 94.4 124.0
REMARK 620 5 GLU g 253 OXT 72.5 130.0 118.1 56.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN f 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS f 112 SG
REMARK 620 2 CYS f 115 SG 104.7
REMARK 620 3 CYS f 126 SG 116.9 112.6
REMARK 620 4 CYS f 129 SG 112.1 104.7 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN g 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS g 212 SG
REMARK 620 2 CYS g 215 SG 104.7
REMARK 620 3 CYS g 226 SG 116.1 112.7
REMARK 620 4 CYS g 229 SG 109.8 105.7 107.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN h 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS h 12 SG
REMARK 620 2 CYS h 15 SG 110.9
REMARK 620 3 CYS h 26 SG 115.3 112.1
REMARK 620 4 CYS h 29 SG 111.7 101.7 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG h 54 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU h 53 O
REMARK 620 2 GLU h 53 OXT 56.6
REMARK 620 3 GLU i 153 O 120.9 126.3
REMARK 620 4 GLU j 253 O 106.8 126.6 106.1
REMARK 620 5 GLU j 253 OXT 70.5 123.7 95.7 50.9
REMARK 620 6 HOH j 555 O 136.1 85.1 98.1 77.6 128.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN i 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS i 112 SG
REMARK 620 2 CYS i 115 SG 99.8
REMARK 620 3 CYS i 126 SG 124.9 113.1
REMARK 620 4 CYS i 129 SG 112.1 104.2 101.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN j 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS j 212 SG
REMARK 620 2 CYS j 215 SG 101.2
REMARK 620 3 CYS j 226 SG 125.8 110.4
REMARK 620 4 CYS j 229 SG 113.1 100.7 103.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN k 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS k 12 SG
REMARK 620 2 CYS k 15 SG 105.6
REMARK 620 3 CYS k 26 SG 119.2 112.3
REMARK 620 4 CYS k 29 SG 109.8 106.2 103.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG k 54 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU k 53 O
REMARK 620 2 GLU m 253 O 109.9
REMARK 620 3 HOH m 557 O 119.6 118.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN l 160 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS l 112 SG
REMARK 620 2 CYS l 115 SG 102.1
REMARK 620 3 CYS l 126 SG 119.6 111.6
REMARK 620 4 CYS l 129 SG 111.0 106.3 105.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN m 260 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS m 212 SG
REMARK 620 2 CYS m 215 SG 102.8
REMARK 620 3 CYS m 226 SG 121.4 109.8
REMARK 620 4 CYS m 229 SG 110.0 102.0 109.0
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 I 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN M 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN O 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN Q 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN R 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN S 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN T 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN U 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN V 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN W 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN X 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN Y 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN Z 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 1 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 2 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 3 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 4 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 5 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 6 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 7 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 8 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 9 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN a 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN b 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN c 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN d 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN e 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN f 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN g 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN h 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN i 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN j 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN k 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN l 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN m 260
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG O 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG S 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG V 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 1 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 3 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 5 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 8 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG b 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG g 14
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG h 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG k 54
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BX9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF B.SUBTILIS ANTI-TRAP PROTEIN, AN ANTAGONIST OF
REMARK 900 TRAP-RNA INTERACTIONS
REMARK 900 RELATED ID: 3LCZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF B.LICHENIFORMIS ANTI-TRAP PROTEIN, AN
REMARK 900 ANTAGONIST OF TRAP-RNA INTERACTIONS
DBREF 3LD0 A 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 B 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 C 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 D 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 E 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 F 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 G 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 H 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 I 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 J 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 K 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 L 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 M 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 N 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 O 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 P 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 Q 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 R 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 S 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 T 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 U 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 V 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 W 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 X 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 Y 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 Z 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 1 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 2 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 3 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 4 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 5 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 6 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 7 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 8 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 9 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 a 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 b 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 c 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 d 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 e 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 f 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 g 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 h 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 i 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 j 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 k 1 53 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 l 101 153 UNP Q65NU7 Q65NU7_BACLD 1 53
DBREF 3LD0 m 201 253 UNP Q65NU7 Q65NU7_BACLD 1 53
SEQADV 3LD0 LEU A 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE A 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS A 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU B 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE B 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS B 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU C 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE C 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS C 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU D 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE D 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS D 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU E 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE E 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS E 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU F 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE F 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS F 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU G 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE G 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS G 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU H 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE H 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS H 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU I 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE I 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS I 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU J 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE J 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS J 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU K 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE K 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS K 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU L 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE L 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS L 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU M 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE M 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS M 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU N 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE N 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS N 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU O 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE O 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS O 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU P 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE P 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS P 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU Q 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE Q 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS Q 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU R 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE R 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS R 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU S 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE S 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS S 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU T 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE T 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS T 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU U 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE U 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS U 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU V 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE V 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS V 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU W 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE W 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS W 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU X 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE X 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS X 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU Y 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE Y 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS Y 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU Z 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE Z 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS Z 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU 1 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE 1 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS 1 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU 2 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE 2 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS 2 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU 3 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE 3 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS 3 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU 4 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE 4 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS 4 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU 5 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE 5 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS 5 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU 6 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE 6 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS 6 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU 7 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE 7 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS 7 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU 8 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE 8 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS 8 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU 9 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE 9 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS 9 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU a 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE a 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS a 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU b 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE b 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS b 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU c 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE c 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS c 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU d 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE d 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS d 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU e 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE e 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS e 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU f 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE f 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS f 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU g 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE g 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS g 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU h 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE h 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS h 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU i 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE i 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS i 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU j 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE j 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS j 252 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU k 30 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE k 51 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS k 52 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU l 130 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE l 151 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS l 152 UNP Q65NU7 ASN 52 VARIANT
SEQADV 3LD0 LEU m 230 UNP Q65NU7 SER 30 VARIANT
SEQADV 3LD0 ILE m 251 UNP Q65NU7 LEU 51 VARIANT
SEQADV 3LD0 HIS m 252 UNP Q65NU7 ASN 52 VARIANT
SEQRES 1 A 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 A 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 A 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 A 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 A 53 GLU
SEQRES 1 B 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 B 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 B 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 B 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 B 53 GLU
SEQRES 1 C 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 C 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 C 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 C 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 C 53 GLU
SEQRES 1 D 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 D 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 D 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 D 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 D 53 GLU
SEQRES 1 E 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 E 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 E 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 E 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 E 53 GLU
SEQRES 1 F 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 F 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 F 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 F 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 F 53 GLU
SEQRES 1 G 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 G 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 G 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 G 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 G 53 GLU
SEQRES 1 H 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 H 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 H 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 H 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 H 53 GLU
SEQRES 1 I 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 I 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 I 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 I 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 I 53 GLU
SEQRES 1 J 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 J 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 J 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 J 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 J 53 GLU
SEQRES 1 K 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 K 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 K 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 K 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 K 53 GLU
SEQRES 1 L 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 L 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 L 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 L 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 L 53 GLU
SEQRES 1 M 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 M 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 M 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 M 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 M 53 GLU
SEQRES 1 N 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 N 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 N 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 N 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 N 53 GLU
SEQRES 1 O 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 O 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 O 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 O 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 O 53 GLU
SEQRES 1 P 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 P 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 P 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 P 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 P 53 GLU
SEQRES 1 Q 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 Q 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 Q 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 Q 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 Q 53 GLU
SEQRES 1 R 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 R 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 R 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 R 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 R 53 GLU
SEQRES 1 S 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 S 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 S 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 S 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 S 53 GLU
SEQRES 1 T 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 T 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 T 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 T 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 T 53 GLU
SEQRES 1 U 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 U 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 U 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 U 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 U 53 GLU
SEQRES 1 V 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 V 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 V 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 V 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 V 53 GLU
SEQRES 1 W 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 W 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 W 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 W 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 W 53 GLU
SEQRES 1 X 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 X 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 X 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 X 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 X 53 GLU
SEQRES 1 Y 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 Y 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 Y 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 Y 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 Y 53 GLU
SEQRES 1 Z 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 Z 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 Z 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 Z 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 Z 53 GLU
SEQRES 1 1 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 1 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 1 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 1 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 1 53 GLU
SEQRES 1 2 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 2 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 2 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 2 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 2 53 GLU
SEQRES 1 3 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 3 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 3 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 3 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 3 53 GLU
SEQRES 1 4 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 4 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 4 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 4 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 4 53 GLU
SEQRES 1 5 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 5 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 5 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 5 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 5 53 GLU
SEQRES 1 6 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 6 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 6 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 6 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 6 53 GLU
SEQRES 1 7 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 7 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 7 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 7 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 7 53 GLU
SEQRES 1 8 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 8 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 8 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 8 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 8 53 GLU
SEQRES 1 9 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 9 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 9 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 9 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 9 53 GLU
SEQRES 1 a 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 a 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 a 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 a 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 a 53 GLU
SEQRES 1 b 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 b 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 b 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 b 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 b 53 GLU
SEQRES 1 c 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 c 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 c 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 c 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 c 53 GLU
SEQRES 1 d 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 d 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 d 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 d 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 d 53 GLU
SEQRES 1 e 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 e 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 e 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 e 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 e 53 GLU
SEQRES 1 f 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 f 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 f 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 f 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 f 53 GLU
SEQRES 1 g 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 g 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 g 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 g 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 g 53 GLU
SEQRES 1 h 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 h 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 h 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 h 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 h 53 GLU
SEQRES 1 i 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 i 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 i 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 i 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 i 53 GLU
SEQRES 1 j 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 j 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 j 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 j 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 j 53 GLU
SEQRES 1 k 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 k 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 k 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 k 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 k 53 GLU
SEQRES 1 l 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 l 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 l 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 l 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 l 53 GLU
SEQRES 1 m 53 MET VAL ILE ALA THR ASP ASP LEU GLU THR THR CYS PRO
SEQRES 2 m 53 ASN CYS ASN GLY SER GLY ARG GLU GLU PRO GLU PRO CYS
SEQRES 3 m 53 PRO LYS CYS LEU GLY LYS GLY VAL ILE LEU THR ALA GLN
SEQRES 4 m 53 GLY SER THR LEU LEU HIS PHE ILE LYS LYS HIS ILE HIS
SEQRES 5 m 53 GLU
HET ZN A 60 1
HET ZN B 160 1
HET MG B 1 1
HET ZN C 260 1
HET ZN D 60 1
HET MG D 54 1
HET ZN E 160 1
HET ZN F 260 1
HET ZN G 60 1
HET ZN H 160 1
HET ZN I 260 1
HET MG I 3 1
HET ZN J 60 1
HET MG J 54 1
HET ZN K 160 1
HET ZN L 260 1
HET ZN M 60 1
HET ZN N 160 1
HET ZN O 260 1
HET MG O 5 1
HET ZN P 60 1
HET ZN Q 160 1
HET ZN R 260 1
HET MG R 6 1
HET ZN S 60 1
HET MG S 54 1
HET ZN T 160 1
HET ZN U 260 1
HET ZN V 60 1
HET MG V 54 1
HET ZN W 160 1
HET ZN X 260 1
HET ZN Y 60 1
HET ZN Z 160 1
HET ZN 1 260 1
HET MG 1 9 1
HET ZN 2 60 1
HET ZN 3 160 1
HET MG 3 10 1
HET ZN 4 260 1
HET ZN 5 60 1
HET MG 5 54 1
HET ZN 6 160 1
HET ZN 7 260 1
HET ZN 8 60 1
HET MG 8 54 1
HET ZN 9 160 1
HET ZN a 260 1
HET ZN b 60 1
HET MG b 54 1
HET ZN c 160 1
HET ZN d 260 1
HET ZN e 60 1
HET ZN f 160 1
HET ZN g 260 1
HET MG g 14 1
HET ZN h 60 1
HET MG h 54 1
HET ZN i 160 1
HET ZN j 260 1
HET ZN k 60 1
HET MG k 54 1
HET ZN l 160 1
HET ZN m 260 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 49 ZN 48(ZN 2+)
FORMUL 51 MG 16(MG 2+)
FORMUL 13 HOH *1335(H2 O)
HELIX 1 1 ALA A 4 LEU A 8 1 5
HELIX 2 2 THR A 37 HIS A 52 1 16
HELIX 3 3 ALA B 104 LEU B 108 1 5
HELIX 4 4 THR B 137 HIS B 152 1 16
HELIX 5 5 ALA C 204 LEU C 208 1 5
HELIX 6 6 THR C 237 HIS C 252 1 16
HELIX 7 7 ALA D 4 LEU D 8 1 5
HELIX 8 8 THR D 37 HIS D 52 1 16
HELIX 9 9 ALA E 104 LEU E 108 1 5
HELIX 10 10 THR E 137 HIS E 152 1 16
HELIX 11 11 ALA F 204 ASP F 207 5 4
HELIX 12 12 THR F 237 HIS F 252 1 16
HELIX 13 13 ALA G 4 LEU G 8 1 5
HELIX 14 14 THR G 37 HIS G 52 1 16
HELIX 15 15 ALA H 104 ASP H 107 5 4
HELIX 16 16 THR H 137 HIS H 152 1 16
HELIX 17 17 ALA I 204 LEU I 208 1 5
HELIX 18 18 THR I 237 HIS I 252 1 16
HELIX 19 19 ALA J 4 LEU J 8 1 5
HELIX 20 20 THR J 37 HIS J 52 1 16
HELIX 21 21 ALA K 104 ASP K 107 5 4
HELIX 22 22 THR K 137 HIS K 152 1 16
HELIX 23 23 ALA L 204 LEU L 208 1 5
HELIX 24 24 THR L 237 HIS L 252 1 16
HELIX 25 25 ALA M 4 ASP M 7 5 4
HELIX 26 26 THR M 37 HIS M 52 1 16
HELIX 27 27 ALA N 104 LEU N 108 1 5
HELIX 28 28 THR N 137 HIS N 152 1 16
HELIX 29 29 ALA O 204 LEU O 208 1 5
HELIX 30 30 THR O 237 HIS O 252 1 16
HELIX 31 31 ALA P 4 LEU P 8 1 5
HELIX 32 32 THR P 37 HIS P 52 1 16
HELIX 33 33 ALA Q 104 ASP Q 107 5 4
HELIX 34 34 THR Q 137 HIS Q 152 1 16
HELIX 35 35 ALA R 204 LEU R 208 1 5
HELIX 36 36 THR R 237 HIS R 252 1 16
HELIX 37 37 ALA S 4 ASP S 7 5 4
HELIX 38 38 THR S 37 HIS S 52 1 16
HELIX 39 39 ALA T 104 LEU T 108 1 5
HELIX 40 40 THR T 137 HIS T 152 1 16
HELIX 41 41 ALA U 204 LEU U 208 1 5
HELIX 42 42 THR U 237 HIS U 252 1 16
HELIX 43 43 ALA V 4 LEU V 8 1 5
HELIX 44 44 THR V 37 HIS V 52 1 16
HELIX 45 45 ALA W 104 ASP W 107 5 4
HELIX 46 46 THR W 137 HIS W 152 1 16
HELIX 47 47 ALA X 204 ASP X 207 5 4
HELIX 48 48 THR X 237 HIS X 252 1 16
HELIX 49 49 ALA Y 4 LEU Y 8 1 5
HELIX 50 50 THR Y 37 HIS Y 52 1 16
HELIX 51 51 ALA Z 104 LEU Z 108 1 5
HELIX 52 52 THR Z 137 HIS Z 152 1 16
HELIX 53 53 ALA 1 204 ASP 1 207 5 4
HELIX 54 54 THR 1 237 ILE 1 251 1 15
HELIX 55 55 ALA 2 4 ASP 2 7 5 4
HELIX 56 56 THR 2 37 HIS 2 52 1 16
HELIX 57 57 ALA 3 104 LEU 3 108 1 5
HELIX 58 58 THR 3 137 HIS 3 152 1 16
HELIX 59 59 ALA 4 204 ASP 4 207 5 4
HELIX 60 60 THR 4 237 HIS 4 252 1 16
HELIX 61 61 ALA 5 4 LEU 5 8 1 5
HELIX 62 62 THR 5 37 HIS 5 52 1 16
HELIX 63 63 ALA 6 104 LEU 6 108 1 5
HELIX 64 64 THR 6 137 HIS 6 152 1 16
HELIX 65 65 ALA 7 204 LEU 7 208 1 5
HELIX 66 66 THR 7 237 HIS 7 252 1 16
HELIX 67 67 ALA 8 4 LEU 8 8 1 5
HELIX 68 68 THR 8 37 HIS 8 52 1 16
HELIX 69 69 ALA 9 104 ASP 9 107 5 4
HELIX 70 70 THR 9 137 HIS 9 152 1 16
HELIX 71 71 ALA a 204 LEU a 208 1 5
HELIX 72 72 THR a 237 HIS a 252 1 16
HELIX 73 73 ALA b 4 ASP b 7 5 4
HELIX 74 74 THR b 37 HIS b 52 1 16
HELIX 75 75 ALA c 104 LEU c 108 1 5
HELIX 76 76 THR c 137 HIS c 152 1 16
HELIX 77 77 ALA d 204 LEU d 208 1 5
HELIX 78 78 THR d 237 HIS d 252 1 16
HELIX 79 79 ALA e 4 LEU e 8 1 5
HELIX 80 80 THR e 37 HIS e 52 1 16
HELIX 81 81 ALA f 104 LEU f 108 1 5
HELIX 82 82 THR f 137 HIS f 152 1 16
HELIX 83 83 ALA g 204 LEU g 208 1 5
HELIX 84 84 THR g 237 HIS g 252 1 16
HELIX 85 85 ALA h 4 LEU h 8 1 5
HELIX 86 86 THR h 37 HIS h 52 1 16
HELIX 87 87 ALA i 104 LEU i 108 1 5
HELIX 88 88 THR i 137 HIS i 152 1 16
HELIX 89 89 ALA j 204 ASP j 207 5 4
HELIX 90 90 THR j 237 HIS j 252 1 16
HELIX 91 91 ALA k 4 LEU k 8 1 5
HELIX 92 92 THR k 37 HIS k 52 1 16
HELIX 93 93 ALA l 104 LEU l 108 1 5
HELIX 94 94 THR l 137 ILE l 151 1 15
HELIX 95 95 ALA m 204 ASP m 207 5 4
HELIX 96 96 THR m 237 HIS m 252 1 16
SHEET 1 A 2 GLU A 9 THR A 11 0
SHEET 2 A 2 VAL A 34 LEU A 36 -1 O ILE A 35 N THR A 10
SHEET 1 B 2 ARG A 20 GLU A 21 0
SHEET 2 B 2 GLU A 24 PRO A 25 -1 O GLU A 24 N GLU A 21
SHEET 1 C 2 GLU B 109 THR B 111 0
SHEET 2 C 2 VAL B 134 LEU B 136 -1 O ILE B 135 N THR B 110
SHEET 1 D 2 ARG B 120 GLU B 121 0
SHEET 2 D 2 GLU B 124 PRO B 125 -1 O GLU B 124 N GLU B 121
SHEET 1 E 2 GLU C 209 THR C 211 0
SHEET 2 E 2 VAL C 234 LEU C 236 -1 O ILE C 235 N THR C 210
SHEET 1 F 2 ARG C 220 GLU C 221 0
SHEET 2 F 2 GLU C 224 PRO C 225 -1 O GLU C 224 N GLU C 221
SHEET 1 G 2 GLU D 9 THR D 11 0
SHEET 2 G 2 VAL D 34 LEU D 36 -1 O ILE D 35 N THR D 10
SHEET 1 H 2 ARG D 20 GLU D 21 0
SHEET 2 H 2 GLU D 24 PRO D 25 -1 O GLU D 24 N GLU D 21
SHEET 1 I 2 GLU E 109 THR E 111 0
SHEET 2 I 2 VAL E 134 LEU E 136 -1 O ILE E 135 N THR E 110
SHEET 1 J 2 ARG E 120 GLU E 121 0
SHEET 2 J 2 GLU E 124 PRO E 125 -1 O GLU E 124 N GLU E 121
SHEET 1 K 2 GLU F 209 THR F 211 0
SHEET 2 K 2 VAL F 234 LEU F 236 -1 O ILE F 235 N THR F 210
SHEET 1 L 2 ARG F 220 GLU F 221 0
SHEET 2 L 2 GLU F 224 PRO F 225 -1 O GLU F 224 N GLU F 221
SHEET 1 M 2 GLU G 9 THR G 11 0
SHEET 2 M 2 VAL G 34 LEU G 36 -1 O ILE G 35 N THR G 10
SHEET 1 N 2 ARG G 20 GLU G 21 0
SHEET 2 N 2 GLU G 24 PRO G 25 -1 O GLU G 24 N GLU G 21
SHEET 1 O 2 GLU H 109 THR H 111 0
SHEET 2 O 2 VAL H 134 LEU H 136 -1 O ILE H 135 N THR H 110
SHEET 1 P 2 ARG H 120 GLU H 121 0
SHEET 2 P 2 GLU H 124 PRO H 125 -1 O GLU H 124 N GLU H 121
SHEET 1 Q 2 GLU I 209 THR I 211 0
SHEET 2 Q 2 VAL I 234 LEU I 236 -1 O ILE I 235 N THR I 210
SHEET 1 R 2 ARG I 220 GLU I 221 0
SHEET 2 R 2 GLU I 224 PRO I 225 -1 O GLU I 224 N GLU I 221
SHEET 1 S 2 GLU J 9 THR J 11 0
SHEET 2 S 2 VAL J 34 LEU J 36 -1 O ILE J 35 N THR J 10
SHEET 1 T 2 ARG J 20 GLU J 21 0
SHEET 2 T 2 GLU J 24 PRO J 25 -1 O GLU J 24 N GLU J 21
SHEET 1 U 2 GLU K 109 THR K 111 0
SHEET 2 U 2 VAL K 134 LEU K 136 -1 O ILE K 135 N THR K 110
SHEET 1 V 2 ARG K 120 GLU K 121 0
SHEET 2 V 2 GLU K 124 PRO K 125 -1 O GLU K 124 N GLU K 121
SHEET 1 W 2 GLU L 209 THR L 211 0
SHEET 2 W 2 VAL L 234 LEU L 236 -1 O ILE L 235 N THR L 210
SHEET 1 X 2 ARG L 220 GLU L 221 0
SHEET 2 X 2 GLU L 224 PRO L 225 -1 O GLU L 224 N GLU L 221
SHEET 1 Y 2 GLU M 9 THR M 11 0
SHEET 2 Y 2 VAL M 34 LEU M 36 -1 O ILE M 35 N THR M 10
SHEET 1 Z 2 ARG M 20 GLU M 21 0
SHEET 2 Z 2 GLU M 24 PRO M 25 -1 O GLU M 24 N GLU M 21
SHEET 1 AA 2 GLU N 109 THR N 111 0
SHEET 2 AA 2 VAL N 134 LEU N 136 -1 O ILE N 135 N THR N 110
SHEET 1 AB 2 ARG N 120 GLU N 121 0
SHEET 2 AB 2 GLU N 124 PRO N 125 -1 O GLU N 124 N GLU N 121
SHEET 1 AC 2 GLU O 209 THR O 211 0
SHEET 2 AC 2 VAL O 234 LEU O 236 -1 O ILE O 235 N THR O 210
SHEET 1 AD 2 ARG O 220 GLU O 221 0
SHEET 2 AD 2 GLU O 224 PRO O 225 -1 O GLU O 224 N GLU O 221
SHEET 1 AE 2 GLU P 9 THR P 11 0
SHEET 2 AE 2 VAL P 34 LEU P 36 -1 O ILE P 35 N THR P 10
SHEET 1 AF 2 ARG P 20 GLU P 21 0
SHEET 2 AF 2 GLU P 24 PRO P 25 -1 O GLU P 24 N GLU P 21
SHEET 1 AG 2 GLU Q 109 THR Q 111 0
SHEET 2 AG 2 VAL Q 134 LEU Q 136 -1 O ILE Q 135 N THR Q 110
SHEET 1 AH 2 ARG Q 120 GLU Q 121 0
SHEET 2 AH 2 GLU Q 124 PRO Q 125 -1 O GLU Q 124 N GLU Q 121
SHEET 1 AI 2 GLU R 209 THR R 211 0
SHEET 2 AI 2 VAL R 234 LEU R 236 -1 O ILE R 235 N THR R 210
SHEET 1 AJ 2 ARG R 220 GLU R 221 0
SHEET 2 AJ 2 GLU R 224 PRO R 225 -1 O GLU R 224 N GLU R 221
SHEET 1 AK 2 GLU S 9 THR S 11 0
SHEET 2 AK 2 VAL S 34 LEU S 36 -1 O ILE S 35 N THR S 10
SHEET 1 AL 2 ARG S 20 GLU S 21 0
SHEET 2 AL 2 GLU S 24 PRO S 25 -1 O GLU S 24 N GLU S 21
SHEET 1 AM 2 GLU T 109 THR T 111 0
SHEET 2 AM 2 VAL T 134 LEU T 136 -1 O ILE T 135 N THR T 110
SHEET 1 AN 2 ARG T 120 GLU T 121 0
SHEET 2 AN 2 GLU T 124 PRO T 125 -1 O GLU T 124 N GLU T 121
SHEET 1 AO 2 GLU U 209 THR U 211 0
SHEET 2 AO 2 VAL U 234 LEU U 236 -1 O ILE U 235 N THR U 210
SHEET 1 AP 2 ARG U 220 GLU U 221 0
SHEET 2 AP 2 GLU U 224 PRO U 225 -1 O GLU U 224 N GLU U 221
SHEET 1 AQ 2 GLU V 9 THR V 11 0
SHEET 2 AQ 2 VAL V 34 LEU V 36 -1 O ILE V 35 N THR V 10
SHEET 1 AR 2 ARG V 20 GLU V 21 0
SHEET 2 AR 2 GLU V 24 PRO V 25 -1 O GLU V 24 N GLU V 21
SHEET 1 AS 2 GLU W 109 THR W 111 0
SHEET 2 AS 2 VAL W 134 LEU W 136 -1 O ILE W 135 N THR W 110
SHEET 1 AT 2 ARG W 120 GLU W 121 0
SHEET 2 AT 2 GLU W 124 PRO W 125 -1 O GLU W 124 N GLU W 121
SHEET 1 AU 2 GLU X 209 THR X 211 0
SHEET 2 AU 2 VAL X 234 LEU X 236 -1 O ILE X 235 N THR X 210
SHEET 1 AV 2 ARG X 220 GLU X 221 0
SHEET 2 AV 2 GLU X 224 PRO X 225 -1 O GLU X 224 N GLU X 221
SHEET 1 AW 2 GLU Y 9 THR Y 11 0
SHEET 2 AW 2 VAL Y 34 LEU Y 36 -1 O ILE Y 35 N THR Y 10
SHEET 1 AX 2 ARG Y 20 GLU Y 21 0
SHEET 2 AX 2 GLU Y 24 PRO Y 25 -1 O GLU Y 24 N GLU Y 21
SHEET 1 AY 2 GLU Z 109 THR Z 111 0
SHEET 2 AY 2 VAL Z 134 LEU Z 136 -1 O ILE Z 135 N THR Z 110
SHEET 1 AZ 2 ARG Z 120 GLU Z 121 0
SHEET 2 AZ 2 GLU Z 124 PRO Z 125 -1 O GLU Z 124 N GLU Z 121
SHEET 1 BA 2 GLU 1 209 THR 1 211 0
SHEET 2 BA 2 VAL 1 234 LEU 1 236 -1 O ILE 1 235 N THR 1 210
SHEET 1 BB 2 ARG 1 220 GLU 1 221 0
SHEET 2 BB 2 GLU 1 224 PRO 1 225 -1 O GLU 1 224 N GLU 1 221
SHEET 1 BC 2 GLU 2 9 THR 2 11 0
SHEET 2 BC 2 VAL 2 34 LEU 2 36 -1 O ILE 2 35 N THR 2 10
SHEET 1 BD 2 ARG 2 20 GLU 2 21 0
SHEET 2 BD 2 GLU 2 24 PRO 2 25 -1 O GLU 2 24 N GLU 2 21
SHEET 1 BE 2 GLU 3 109 THR 3 111 0
SHEET 2 BE 2 VAL 3 134 LEU 3 136 -1 O ILE 3 135 N THR 3 110
SHEET 1 BF 2 ARG 3 120 GLU 3 121 0
SHEET 2 BF 2 GLU 3 124 PRO 3 125 -1 O GLU 3 124 N GLU 3 121
SHEET 1 BG 2 GLU 4 209 THR 4 211 0
SHEET 2 BG 2 VAL 4 234 LEU 4 236 -1 O ILE 4 235 N THR 4 210
SHEET 1 BH 2 ARG 4 220 GLU 4 221 0
SHEET 2 BH 2 GLU 4 224 PRO 4 225 -1 O GLU 4 224 N GLU 4 221
SHEET 1 BI 2 GLU 5 9 THR 5 11 0
SHEET 2 BI 2 VAL 5 34 LEU 5 36 -1 O ILE 5 35 N THR 5 10
SHEET 1 BJ 2 ARG 5 20 GLU 5 21 0
SHEET 2 BJ 2 GLU 5 24 PRO 5 25 -1 O GLU 5 24 N GLU 5 21
SHEET 1 BK 2 GLU 6 109 THR 6 111 0
SHEET 2 BK 2 VAL 6 134 LEU 6 136 -1 O ILE 6 135 N THR 6 110
SHEET 1 BL 2 ARG 6 120 GLU 6 121 0
SHEET 2 BL 2 GLU 6 124 PRO 6 125 -1 O GLU 6 124 N GLU 6 121
SHEET 1 BM 2 GLU 7 209 THR 7 211 0
SHEET 2 BM 2 VAL 7 234 LEU 7 236 -1 O ILE 7 235 N THR 7 210
SHEET 1 BN 2 ARG 7 220 GLU 7 221 0
SHEET 2 BN 2 GLU 7 224 PRO 7 225 -1 O GLU 7 224 N GLU 7 221
SHEET 1 BO 2 GLU 8 9 THR 8 11 0
SHEET 2 BO 2 VAL 8 34 LEU 8 36 -1 O ILE 8 35 N THR 8 10
SHEET 1 BP 2 ARG 8 20 GLU 8 21 0
SHEET 2 BP 2 GLU 8 24 PRO 8 25 -1 O GLU 8 24 N GLU 8 21
SHEET 1 BQ 2 GLU 9 109 THR 9 111 0
SHEET 2 BQ 2 VAL 9 134 LEU 9 136 -1 O ILE 9 135 N THR 9 110
SHEET 1 BR 2 ARG 9 120 GLU 9 121 0
SHEET 2 BR 2 GLU 9 124 PRO 9 125 -1 O GLU 9 124 N GLU 9 121
SHEET 1 BS 2 GLU a 209 THR a 211 0
SHEET 2 BS 2 VAL a 234 LEU a 236 -1 O ILE a 235 N THR a 210
SHEET 1 BT 2 ARG a 220 GLU a 221 0
SHEET 2 BT 2 GLU a 224 PRO a 225 -1 O GLU a 224 N GLU a 221
SHEET 1 BU 2 GLU b 9 THR b 11 0
SHEET 2 BU 2 VAL b 34 LEU b 36 -1 O ILE b 35 N THR b 10
SHEET 1 BV 2 ARG b 20 GLU b 21 0
SHEET 2 BV 2 GLU b 24 PRO b 25 -1 O GLU b 24 N GLU b 21
SHEET 1 BW 2 GLU c 109 THR c 111 0
SHEET 2 BW 2 VAL c 134 LEU c 136 -1 O ILE c 135 N THR c 110
SHEET 1 BX 2 ARG c 120 GLU c 121 0
SHEET 2 BX 2 GLU c 124 PRO c 125 -1 O GLU c 124 N GLU c 121
SHEET 1 BY 2 GLU d 209 THR d 211 0
SHEET 2 BY 2 VAL d 234 LEU d 236 -1 O ILE d 235 N THR d 210
SHEET 1 BZ 2 ARG d 220 GLU d 221 0
SHEET 2 BZ 2 GLU d 224 PRO d 225 -1 O GLU d 224 N GLU d 221
SHEET 1 CA 2 GLU e 9 THR e 11 0
SHEET 2 CA 2 VAL e 34 LEU e 36 -1 O ILE e 35 N THR e 10
SHEET 1 CB 2 ARG e 20 GLU e 21 0
SHEET 2 CB 2 GLU e 24 PRO e 25 -1 O GLU e 24 N GLU e 21
SHEET 1 CC 2 GLU f 109 THR f 111 0
SHEET 2 CC 2 VAL f 134 LEU f 136 -1 O ILE f 135 N THR f 110
SHEET 1 CD 2 ARG f 120 GLU f 121 0
SHEET 2 CD 2 GLU f 124 PRO f 125 -1 O GLU f 124 N GLU f 121
SHEET 1 CE 2 GLU g 209 THR g 211 0
SHEET 2 CE 2 VAL g 234 LEU g 236 -1 O ILE g 235 N THR g 210
SHEET 1 CF 2 ARG g 220 GLU g 221 0
SHEET 2 CF 2 GLU g 224 PRO g 225 -1 O GLU g 224 N GLU g 221
SHEET 1 CG 2 GLU h 9 THR h 11 0
SHEET 2 CG 2 VAL h 34 LEU h 36 -1 O ILE h 35 N THR h 10
SHEET 1 CH 2 ARG h 20 GLU h 21 0
SHEET 2 CH 2 GLU h 24 PRO h 25 -1 O GLU h 24 N GLU h 21
SHEET 1 CI 2 GLU i 109 THR i 111 0
SHEET 2 CI 2 VAL i 134 LEU i 136 -1 O ILE i 135 N THR i 110
SHEET 1 CJ 2 ARG i 120 GLU i 121 0
SHEET 2 CJ 2 GLU i 124 PRO i 125 -1 O GLU i 124 N GLU i 121
SHEET 1 CK 2 GLU j 209 THR j 211 0
SHEET 2 CK 2 VAL j 234 LEU j 236 -1 O ILE j 235 N THR j 210
SHEET 1 CL 2 ARG j 220 GLU j 221 0
SHEET 2 CL 2 GLU j 224 PRO j 225 -1 O GLU j 224 N GLU j 221
SHEET 1 CM 2 GLU k 9 THR k 11 0
SHEET 2 CM 2 VAL k 34 LEU k 36 -1 O ILE k 35 N THR k 10
SHEET 1 CN 2 ARG k 20 GLU k 21 0
SHEET 2 CN 2 GLU k 24 PRO k 25 -1 O GLU k 24 N GLU k 21
SHEET 1 CO 2 GLU l 109 THR l 111 0
SHEET 2 CO 2 VAL l 134 LEU l 136 -1 O ILE l 135 N THR l 110
SHEET 1 CP 2 ARG l 120 GLU l 121 0
SHEET 2 CP 2 GLU l 124 PRO l 125 -1 O GLU l 124 N GLU l 121
SHEET 1 CQ 2 GLU m 209 THR m 211 0
SHEET 2 CQ 2 VAL m 234 LEU m 236 -1 O ILE m 235 N THR m 210
SHEET 1 CR 2 ARG m 220 GLU m 221 0
SHEET 2 CR 2 GLU m 224 PRO m 225 -1 O GLU m 224 N GLU m 221
LINK SG CYS A 12 ZN ZN A 60 1555 1555 2.32
LINK SG CYS A 15 ZN ZN A 60 1555 1555 2.35
LINK SG CYS A 26 ZN ZN A 60 1555 1555 2.32
LINK SG CYS A 29 ZN ZN A 60 1555 1555 2.36
LINK O GLU A 53 MG MG B 1 1555 1555 2.66
LINK MG MG B 1 O GLU B 153 1555 1555 2.21
LINK MG MG B 1 O GLU C 253 1555 1555 2.17
LINK MG MG B 1 OXT GLU C 253 1555 1555 2.82
LINK MG MG B 1 O HOH C1000 1555 1555 2.49
LINK SG CYS B 112 ZN ZN B 160 1555 1555 2.30
LINK SG CYS B 115 ZN ZN B 160 1555 1555 2.34
LINK SG CYS B 126 ZN ZN B 160 1555 1555 2.33
LINK SG CYS B 129 ZN ZN B 160 1555 1555 2.37
LINK SG CYS C 212 ZN ZN C 260 1555 1555 2.33
LINK SG CYS C 215 ZN ZN C 260 1555 1555 2.33
LINK SG CYS C 226 ZN ZN C 260 1555 1555 2.34
LINK SG CYS C 229 ZN ZN C 260 1555 1555 2.33
LINK SG CYS D 12 ZN ZN D 60 1555 1555 2.31
LINK SG CYS D 15 ZN ZN D 60 1555 1555 2.35
LINK SG CYS D 26 ZN ZN D 60 1555 1555 2.33
LINK SG CYS D 29 ZN ZN D 60 1555 1555 2.34
LINK O GLU D 53 MG MG D 54 1555 1555 2.20
LINK OXT GLU D 53 MG MG D 54 1555 1555 2.43
LINK MG MG D 54 O HOH D 500 1555 1555 2.38
LINK MG MG D 54 O GLU E 153 1555 1555 2.19
LINK MG MG D 54 OXT GLU E 153 1555 1555 3.00
LINK MG MG D 54 O GLU F 253 1555 1555 2.15
LINK SG CYS E 112 ZN ZN E 160 1555 1555 2.31
LINK SG CYS E 115 ZN ZN E 160 1555 1555 2.35
LINK SG CYS E 126 ZN ZN E 160 1555 1555 2.33
LINK SG CYS E 129 ZN ZN E 160 1555 1555 2.39
LINK SG CYS F 212 ZN ZN F 260 1555 1555 2.34
LINK SG CYS F 215 ZN ZN F 260 1555 1555 2.35
LINK SG CYS F 226 ZN ZN F 260 1555 1555 2.34
LINK SG CYS F 229 ZN ZN F 260 1555 1555 2.34
LINK SG CYS G 12 ZN ZN G 60 1555 1555 2.32
LINK SG CYS G 15 ZN ZN G 60 1555 1555 2.34
LINK SG CYS G 26 ZN ZN G 60 1555 1555 2.33
LINK SG CYS G 29 ZN ZN G 60 1555 1555 2.35
LINK SG CYS H 112 ZN ZN H 160 1555 1555 2.30
LINK SG CYS H 115 ZN ZN H 160 1555 1555 2.33
LINK SG CYS H 126 ZN ZN H 160 1555 1555 2.32
LINK SG CYS H 129 ZN ZN H 160 1555 1555 2.36
LINK MG MG I 3 O GLU I 253 1555 1555 2.17
LINK MG MG I 3 OXT GLU I 253 1555 1555 2.89
LINK MG MG I 3 O HOH I1335 1555 1555 2.52
LINK SG CYS I 212 ZN ZN I 260 1555 1555 2.34
LINK SG CYS I 215 ZN ZN I 260 1555 1555 2.33
LINK SG CYS I 226 ZN ZN I 260 1555 1555 2.34
LINK SG CYS I 229 ZN ZN I 260 1555 1555 2.34
LINK SG CYS J 12 ZN ZN J 60 1555 1555 2.35
LINK SG CYS J 15 ZN ZN J 60 1555 1555 2.34
LINK SG CYS J 26 ZN ZN J 60 1555 1555 2.35
LINK SG CYS J 29 ZN ZN J 60 1555 1555 2.34
LINK O GLU J 53 MG MG J 54 1555 1555 2.18
LINK MG MG J 54 O GLU K 153 1555 1555 2.17
LINK MG MG J 54 O HOH K 671 1555 1555 2.54
LINK MG MG J 54 O GLU L 253 1555 1555 2.19
LINK MG MG J 54 OXT GLU L 253 1555 1555 3.00
LINK SG CYS K 112 ZN ZN K 160 1555 1555 2.32
LINK SG CYS K 115 ZN ZN K 160 1555 1555 2.35
LINK SG CYS K 126 ZN ZN K 160 1555 1555 2.33
LINK SG CYS K 129 ZN ZN K 160 1555 1555 2.36
LINK SG CYS L 212 ZN ZN L 260 1555 1555 2.33
LINK SG CYS L 215 ZN ZN L 260 1555 1555 2.31
LINK SG CYS L 226 ZN ZN L 260 1555 1555 2.33
LINK SG CYS L 229 ZN ZN L 260 1555 1555 2.36
LINK SG CYS M 12 ZN ZN M 60 1555 1555 2.33
LINK SG CYS M 15 ZN ZN M 60 1555 1555 2.33
LINK SG CYS M 26 ZN ZN M 60 1555 1555 2.34
LINK SG CYS M 29 ZN ZN M 60 1555 1555 2.34
LINK O GLU M 53 MG MG O 5 1555 1555 2.17
LINK SG CYS N 112 ZN ZN N 160 1555 1555 2.34
LINK SG CYS N 115 ZN ZN N 160 1555 1555 2.34
LINK SG CYS N 126 ZN ZN N 160 1555 1555 2.32
LINK SG CYS N 129 ZN ZN N 160 1555 1555 2.36
LINK MG MG O 5 O GLU O 253 1555 1555 2.16
LINK MG MG O 5 O HOH O 842 1555 1555 2.02
LINK SG CYS O 212 ZN ZN O 260 1555 1555 2.33
LINK SG CYS O 215 ZN ZN O 260 1555 1555 2.34
LINK SG CYS O 226 ZN ZN O 260 1555 1555 2.33
LINK SG CYS O 229 ZN ZN O 260 1555 1555 2.35
LINK SG CYS P 12 ZN ZN P 60 1555 1555 2.33
LINK SG CYS P 15 ZN ZN P 60 1555 1555 2.32
LINK SG CYS P 26 ZN ZN P 60 1555 1555 2.33
LINK SG CYS P 29 ZN ZN P 60 1555 1555 2.35
LINK O GLU P 53 MG MG R 6 1555 1555 2.20
LINK SG CYS Q 112 ZN ZN Q 160 1555 1555 2.34
LINK SG CYS Q 115 ZN ZN Q 160 1555 1555 2.33
LINK SG CYS Q 126 ZN ZN Q 160 1555 1555 2.32
LINK SG CYS Q 129 ZN ZN Q 160 1555 1555 2.37
LINK O GLU Q 153 MG MG R 6 1555 1555 2.20
LINK MG MG R 6 O GLU R 253 1555 1555 2.17
LINK MG MG R 6 O HOH R 559 1555 1555 2.48
LINK SG CYS R 212 ZN ZN R 260 1555 1555 2.32
LINK SG CYS R 215 ZN ZN R 260 1555 1555 2.33
LINK SG CYS R 226 ZN ZN R 260 1555 1555 2.33
LINK SG CYS R 229 ZN ZN R 260 1555 1555 2.37
LINK SG CYS S 12 ZN ZN S 60 1555 1555 2.33
LINK SG CYS S 15 ZN ZN S 60 1555 1555 2.33
LINK SG CYS S 26 ZN ZN S 60 1555 1555 2.33
LINK SG CYS S 29 ZN ZN S 60 1555 1555 2.37
LINK O GLU S 53 MG MG S 54 1555 1555 2.17
LINK OXT GLU S 53 MG MG S 54 1555 1555 2.99
LINK MG MG S 54 O GLU T 153 1555 1555 2.19
LINK MG MG S 54 O GLU U 253 1555 1555 2.21
LINK MG MG S 54 OXT GLU U 253 1555 1555 2.21
LINK MG MG S 54 O HOH U1209 1555 1555 2.24
LINK SG CYS T 112 ZN ZN T 160 1555 1555 2.32
LINK SG CYS T 115 ZN ZN T 160 1555 1555 2.34
LINK SG CYS T 126 ZN ZN T 160 1555 1555 2.33
LINK SG CYS T 129 ZN ZN T 160 1555 1555 2.35
LINK SG CYS U 212 ZN ZN U 260 1555 1555 2.34
LINK SG CYS U 215 ZN ZN U 260 1555 1555 2.34
LINK SG CYS U 226 ZN ZN U 260 1555 1555 2.32
LINK SG CYS U 229 ZN ZN U 260 1555 1555 2.36
LINK SG CYS V 12 ZN ZN V 60 1555 1555 2.30
LINK SG CYS V 15 ZN ZN V 60 1555 1555 2.35
LINK SG CYS V 26 ZN ZN V 60 1555 1555 2.33
LINK SG CYS V 29 ZN ZN V 60 1555 1555 2.34
LINK O GLU V 53 MG MG V 54 1555 1555 2.20
LINK OXT GLU V 53 MG MG V 54 1555 1555 2.78
LINK MG MG V 54 O HOH V 460 1555 1555 2.40
LINK MG MG V 54 O GLU W 153 1555 1555 2.16
LINK MG MG V 54 O GLU X 253 1555 1555 2.17
LINK SG CYS W 112 ZN ZN W 160 1555 1555 2.32
LINK SG CYS W 115 ZN ZN W 160 1555 1555 2.32
LINK SG CYS W 126 ZN ZN W 160 1555 1555 2.33
LINK SG CYS W 129 ZN ZN W 160 1555 1555 2.37
LINK SG CYS X 212 ZN ZN X 260 1555 1555 2.33
LINK SG CYS X 215 ZN ZN X 260 1555 1555 2.33
LINK SG CYS X 226 ZN ZN X 260 1555 1555 2.34
LINK SG CYS X 229 ZN ZN X 260 1555 1555 2.35
LINK SG CYS Y 12 ZN ZN Y 60 1555 1555 2.30
LINK SG CYS Y 15 ZN ZN Y 60 1555 1555 2.35
LINK SG CYS Y 26 ZN ZN Y 60 1555 1555 2.34
LINK SG CYS Y 29 ZN ZN Y 60 1555 1555 2.37
LINK O GLU Y 53 MG MG 1 9 1555 1555 2.19
LINK SG CYS Z 112 ZN ZN Z 160 1555 1555 2.31
LINK SG CYS Z 115 ZN ZN Z 160 1555 1555 2.34
LINK SG CYS Z 126 ZN ZN Z 160 1555 1555 2.33
LINK SG CYS Z 129 ZN ZN Z 160 1555 1555 2.34
LINK MG MG 1 9 O GLU 1 253 1555 1555 2.18
LINK MG MG 1 9 O HOH 3 798 1555 1555 2.78
LINK SG CYS 1 212 ZN ZN 1 260 1555 1555 2.33
LINK SG CYS 1 215 ZN ZN 1 260 1555 1555 2.33
LINK SG CYS 1 226 ZN ZN 1 260 1555 1555 2.34
LINK SG CYS 1 229 ZN ZN 1 260 1555 1555 2.34
LINK O HOH 1 810 MG MG 3 10 1555 1555 2.82
LINK SG CYS 2 12 ZN ZN 2 60 1555 1555 2.31
LINK SG CYS 2 15 ZN ZN 2 60 1555 1555 2.37
LINK SG CYS 2 26 ZN ZN 2 60 1555 1555 2.32
LINK SG CYS 2 29 ZN ZN 2 60 1555 1555 2.33
LINK MG MG 3 10 O GLU 3 153 1555 1555 2.19
LINK SG CYS 3 112 ZN ZN 3 160 1555 1555 2.33
LINK SG CYS 3 115 ZN ZN 3 160 1555 1555 2.36
LINK SG CYS 3 126 ZN ZN 3 160 1555 1555 2.33
LINK SG CYS 3 129 ZN ZN 3 160 1555 1555 2.36
LINK SG CYS 4 212 ZN ZN 4 260 1555 1555 2.31
LINK SG CYS 4 215 ZN ZN 4 260 1555 1555 2.32
LINK SG CYS 4 226 ZN ZN 4 260 1555 1555 2.33
LINK SG CYS 4 229 ZN ZN 4 260 1555 1555 2.35
LINK SG CYS 5 12 ZN ZN 5 60 1555 1555 2.32
LINK SG CYS 5 15 ZN ZN 5 60 1555 1555 2.34
LINK SG CYS 5 26 ZN ZN 5 60 1555 1555 2.34
LINK SG CYS 5 29 ZN ZN 5 60 1555 1555 2.37
LINK OXT GLU 5 53 MG MG 5 54 1555 1555 1.91
LINK O GLU 5 53 MG MG 5 54 1555 1555 2.18
LINK MG MG 5 54 O HOH 5 566 1555 1555 2.28
LINK MG MG 5 54 O GLU 6 153 1555 1555 2.19
LINK MG MG 5 54 O GLU 7 253 1555 1555 2.19
LINK MG MG 5 54 OXT GLU 7 253 1555 1555 2.43
LINK SG CYS 6 112 ZN ZN 6 160 1555 1555 2.34
LINK SG CYS 6 115 ZN ZN 6 160 1555 1555 2.33
LINK SG CYS 6 126 ZN ZN 6 160 1555 1555 2.34
LINK SG CYS 6 129 ZN ZN 6 160 1555 1555 2.35
LINK SG CYS 7 212 ZN ZN 7 260 1555 1555 2.33
LINK SG CYS 7 215 ZN ZN 7 260 1555 1555 2.32
LINK SG CYS 7 226 ZN ZN 7 260 1555 1555 2.34
LINK SG CYS 7 229 ZN ZN 7 260 1555 1555 2.35
LINK SG CYS 8 12 ZN ZN 8 60 1555 1555 2.35
LINK SG CYS 8 15 ZN ZN 8 60 1555 1555 2.34
LINK SG CYS 8 26 ZN ZN 8 60 1555 1555 2.34
LINK SG CYS 8 29 ZN ZN 8 60 1555 1555 2.36
LINK O GLU 8 53 MG MG 8 54 1555 1555 2.19
LINK OXT GLU 8 53 MG MG 8 54 1555 1555 2.36
LINK MG MG 8 54 O HOH 8 832 1555 1555 2.08
LINK MG MG 8 54 O GLU 9 153 1555 1555 2.17
LINK MG MG 8 54 O GLU a 253 1555 1555 2.22
LINK SG CYS 9 112 ZN ZN 9 160 1555 1555 2.34
LINK SG CYS 9 115 ZN ZN 9 160 1555 1555 2.33
LINK SG CYS 9 126 ZN ZN 9 160 1555 1555 2.34
LINK SG CYS 9 129 ZN ZN 9 160 1555 1555 2.35
LINK SG CYS a 212 ZN ZN a 260 1555 1555 2.33
LINK SG CYS a 215 ZN ZN a 260 1555 1555 2.33
LINK SG CYS a 226 ZN ZN a 260 1555 1555 2.33
LINK SG CYS a 229 ZN ZN a 260 1555 1555 2.37
LINK SG CYS b 12 ZN ZN b 60 1555 1555 2.33
LINK SG CYS b 15 ZN ZN b 60 1555 1555 2.35
LINK SG CYS b 26 ZN ZN b 60 1555 1555 2.34
LINK SG CYS b 29 ZN ZN b 60 1555 1555 2.37
LINK O GLU b 53 MG MG b 54 1555 1555 2.18
LINK OXT GLU b 53 MG MG b 54 1555 1555 2.67
LINK MG MG b 54 OXT GLU c 153 1555 1555 1.86
LINK MG MG b 54 O GLU c 153 1555 1555 2.17
LINK MG MG b 54 O HOH c 907 1555 1555 2.16
LINK MG MG b 54 O GLU d 253 1555 1555 2.17
LINK MG MG b 54 OXT GLU d 253 1555 1555 2.83
LINK SG CYS c 112 ZN ZN c 160 1555 1555 2.31
LINK SG CYS c 115 ZN ZN c 160 1555 1555 2.36
LINK SG CYS c 126 ZN ZN c 160 1555 1555 2.34
LINK SG CYS c 129 ZN ZN c 160 1555 1555 2.36
LINK SG CYS d 212 ZN ZN d 260 1555 1555 2.32
LINK SG CYS d 215 ZN ZN d 260 1555 1555 2.37
LINK SG CYS d 226 ZN ZN d 260 1555 1555 2.32
LINK SG CYS d 229 ZN ZN d 260 1555 1555 2.35
LINK SG CYS e 12 ZN ZN e 60 1555 1555 2.34
LINK SG CYS e 15 ZN ZN e 60 1555 1555 2.32
LINK SG CYS e 26 ZN ZN e 60 1555 1555 2.34
LINK SG CYS e 29 ZN ZN e 60 1555 1555 2.34
LINK O GLU e 53 MG MG g 14 1555 1555 2.17
LINK O HOH e1293 MG MG g 14 1555 1555 2.52
LINK SG CYS f 112 ZN ZN f 160 1555 1555 2.31
LINK SG CYS f 115 ZN ZN f 160 1555 1555 2.34
LINK SG CYS f 126 ZN ZN f 160 1555 1555 2.32
LINK SG CYS f 129 ZN ZN f 160 1555 1555 2.36
LINK O GLU f 153 MG MG g 14 1555 1555 2.19
LINK MG MG g 14 O GLU g 253 1555 1555 2.20
LINK MG MG g 14 OXT GLU g 253 1555 1555 2.24
LINK SG CYS g 212 ZN ZN g 260 1555 1555 2.32
LINK SG CYS g 215 ZN ZN g 260 1555 1555 2.32
LINK SG CYS g 226 ZN ZN g 260 1555 1555 2.35
LINK SG CYS g 229 ZN ZN g 260 1555 1555 2.36
LINK SG CYS h 12 ZN ZN h 60 1555 1555 2.32
LINK SG CYS h 15 ZN ZN h 60 1555 1555 2.35
LINK SG CYS h 26 ZN ZN h 60 1555 1555 2.34
LINK SG CYS h 29 ZN ZN h 60 1555 1555 2.35
LINK O GLU h 53 MG MG h 54 1555 1555 2.20
LINK OXT GLU h 53 MG MG h 54 1555 1555 2.26
LINK MG MG h 54 O GLU i 153 1555 1555 2.19
LINK MG MG h 54 O GLU j 253 1555 1555 2.17
LINK MG MG h 54 OXT GLU j 253 1555 1555 2.66
LINK MG MG h 54 O HOH j 555 1555 1555 2.42
LINK SG CYS i 112 ZN ZN i 160 1555 1555 2.33
LINK SG CYS i 115 ZN ZN i 160 1555 1555 2.35
LINK SG CYS i 126 ZN ZN i 160 1555 1555 2.32
LINK SG CYS i 129 ZN ZN i 160 1555 1555 2.35
LINK SG CYS j 212 ZN ZN j 260 1555 1555 2.32
LINK SG CYS j 215 ZN ZN j 260 1555 1555 2.35
LINK SG CYS j 226 ZN ZN j 260 1555 1555 2.32
LINK SG CYS j 229 ZN ZN j 260 1555 1555 2.37
LINK SG CYS k 12 ZN ZN k 60 1555 1555 2.32
LINK SG CYS k 15 ZN ZN k 60 1555 1555 2.33
LINK SG CYS k 26 ZN ZN k 60 1555 1555 2.33
LINK SG CYS k 29 ZN ZN k 60 1555 1555 2.36
LINK O GLU k 53 MG MG k 54 1555 1555 2.16
LINK MG MG k 54 O GLU m 253 1555 1555 2.20
LINK MG MG k 54 O HOH m 557 1555 1555 2.42
LINK SG CYS l 112 ZN ZN l 160 1555 1555 2.33
LINK SG CYS l 115 ZN ZN l 160 1555 1555 2.34
LINK SG CYS l 126 ZN ZN l 160 1555 1555 2.33
LINK SG CYS l 129 ZN ZN l 160 1555 1555 2.35
LINK SG CYS m 212 ZN ZN m 260 1555 1555 2.33
LINK SG CYS m 215 ZN ZN m 260 1555 1555 2.35
LINK SG CYS m 226 ZN ZN m 260 1555 1555 2.34
LINK SG CYS m 229 ZN ZN m 260 1555 1555 2.35
CISPEP 1 GLU A 22 PRO A 23 0 1.56
CISPEP 2 GLU B 122 PRO B 123 0 0.74
CISPEP 3 GLU C 222 PRO C 223 0 -1.16
CISPEP 4 GLU D 22 PRO D 23 0 0.55
CISPEP 5 GLU E 122 PRO E 123 0 0.35
CISPEP 6 GLU F 222 PRO F 223 0 1.31
CISPEP 7 GLU G 22 PRO G 23 0 2.74
CISPEP 8 GLU H 122 PRO H 123 0 -0.17
CISPEP 9 GLU I 222 PRO I 223 0 -2.26
CISPEP 10 GLU J 22 PRO J 23 0 1.70
CISPEP 11 GLU K 122 PRO K 123 0 1.18
CISPEP 12 GLU L 222 PRO L 223 0 1.72
CISPEP 13 GLU M 22 PRO M 23 0 0.91
CISPEP 14 GLU N 122 PRO N 123 0 1.10
CISPEP 15 GLU O 222 PRO O 223 0 0.71
CISPEP 16 GLU P 22 PRO P 23 0 -0.37
CISPEP 17 GLU Q 122 PRO Q 123 0 1.30
CISPEP 18 GLU R 222 PRO R 223 0 1.94
CISPEP 19 GLU S 22 PRO S 23 0 1.90
CISPEP 20 GLU T 122 PRO T 123 0 -0.16
CISPEP 21 GLU U 222 PRO U 223 0 -0.60
CISPEP 22 GLU V 22 PRO V 23 0 0.61
CISPEP 23 GLU W 122 PRO W 123 0 0.14
CISPEP 24 GLU X 222 PRO X 223 0 0.61
CISPEP 25 GLU Y 22 PRO Y 23 0 -0.02
CISPEP 26 GLU Z 122 PRO Z 123 0 1.26
CISPEP 27 GLU 1 222 PRO 1 223 0 -0.06
CISPEP 28 GLU 2 22 PRO 2 23 0 1.09
CISPEP 29 GLU 3 122 PRO 3 123 0 1.78
CISPEP 30 GLU 4 222 PRO 4 223 0 0.21
CISPEP 31 GLU 5 22 PRO 5 23 0 1.72
CISPEP 32 GLU 6 122 PRO 6 123 0 1.14
CISPEP 33 GLU 7 222 PRO 7 223 0 -0.99
CISPEP 34 GLU 8 22 PRO 8 23 0 2.84
CISPEP 35 GLU 9 122 PRO 9 123 0 1.29
CISPEP 36 GLU a 222 PRO a 223 0 2.28
CISPEP 37 GLU b 22 PRO b 23 0 -0.96
CISPEP 38 GLU c 122 PRO c 123 0 1.88
CISPEP 39 GLU d 222 PRO d 223 0 0.98
CISPEP 40 GLU e 22 PRO e 23 0 0.43
CISPEP 41 GLU f 122 PRO f 123 0 -0.96
CISPEP 42 GLU g 222 PRO g 223 0 1.05
CISPEP 43 GLU h 22 PRO h 23 0 1.94
CISPEP 44 GLU i 122 PRO i 123 0 0.17
CISPEP 45 GLU j 222 PRO j 223 0 0.14
CISPEP 46 GLU k 22 PRO k 23 0 -0.18
CISPEP 47 GLU l 122 PRO l 123 0 -0.03
CISPEP 48 GLU m 222 PRO m 223 0 -0.05
SITE 1 AC1 4 CYS I 212 CYS I 215 CYS I 226 CYS I 229
SITE 1 AC2 4 CYS G 12 CYS G 15 CYS G 26 CYS G 29
SITE 1 AC3 4 CYS A 12 CYS A 15 CYS A 26 CYS A 29
SITE 1 AC4 4 CYS B 112 CYS B 115 CYS B 126 CYS B 129
SITE 1 AC5 4 CYS C 212 CYS C 215 CYS C 226 CYS C 229
SITE 1 AC6 4 CYS D 12 CYS D 15 CYS D 26 CYS D 29
SITE 1 AC7 4 CYS E 112 CYS E 115 CYS E 126 CYS E 129
SITE 1 AC8 4 CYS F 212 CYS F 215 CYS F 226 CYS F 229
SITE 1 AC9 4 CYS J 12 CYS J 15 CYS J 26 CYS J 29
SITE 1 BC1 4 CYS K 112 CYS K 115 CYS K 126 CYS K 129
SITE 1 BC2 4 CYS L 212 CYS L 215 CYS L 226 CYS L 229
SITE 1 BC3 4 CYS M 12 CYS M 15 CYS M 26 CYS M 29
SITE 1 BC4 4 CYS N 112 CYS N 115 CYS N 126 CYS N 129
SITE 1 BC5 4 CYS O 212 CYS O 215 CYS O 226 CYS O 229
SITE 1 BC6 4 CYS P 12 CYS P 15 CYS P 26 CYS P 29
SITE 1 BC7 4 CYS Q 112 CYS Q 115 CYS Q 126 CYS Q 129
SITE 1 BC8 4 CYS R 212 CYS R 215 CYS R 226 CYS R 229
SITE 1 BC9 4 CYS S 12 CYS S 15 CYS S 26 CYS S 29
SITE 1 CC1 4 CYS T 112 CYS T 115 CYS T 126 CYS T 129
SITE 1 CC2 4 CYS U 212 CYS U 215 CYS U 226 CYS U 229
SITE 1 CC3 4 CYS V 12 CYS V 15 CYS V 26 CYS V 29
SITE 1 CC4 4 CYS W 112 CYS W 115 CYS W 126 CYS W 129
SITE 1 CC5 4 CYS X 212 CYS X 215 CYS X 226 CYS X 229
SITE 1 CC6 4 CYS Y 12 CYS Y 15 CYS Y 26 CYS Y 29
SITE 1 CC7 4 CYS Z 112 CYS Z 115 CYS Z 126 CYS Z 129
SITE 1 CC8 4 CYS 1 212 CYS 1 215 CYS 1 226 CYS 1 229
SITE 1 CC9 4 CYS 2 12 CYS 2 15 CYS 2 26 CYS 2 29
SITE 1 DC1 4 CYS 3 112 CYS 3 115 CYS 3 126 CYS 3 129
SITE 1 DC2 4 CYS 4 212 CYS 4 215 CYS 4 226 CYS 4 229
SITE 1 DC3 4 CYS 5 12 CYS 5 15 CYS 5 26 CYS 5 29
SITE 1 DC4 4 CYS 6 112 CYS 6 115 CYS 6 126 CYS 6 129
SITE 1 DC5 4 CYS 7 212 CYS 7 215 CYS 7 226 CYS 7 229
SITE 1 DC6 4 CYS 8 12 CYS 8 15 CYS 8 26 CYS 8 29
SITE 1 DC7 4 CYS 9 112 CYS 9 115 CYS 9 126 CYS 9 129
SITE 1 DC8 4 CYS a 212 CYS a 215 CYS a 226 CYS a 229
SITE 1 DC9 4 CYS b 12 CYS b 15 CYS b 26 CYS b 29
SITE 1 EC1 4 CYS c 112 CYS c 115 CYS c 126 CYS c 129
SITE 1 EC2 4 CYS d 212 CYS d 215 CYS d 226 CYS d 229
SITE 1 EC3 4 CYS e 12 CYS e 15 CYS e 26 CYS e 29
SITE 1 EC4 4 CYS f 112 CYS f 115 CYS f 126 CYS f 129
SITE 1 EC5 4 CYS g 212 CYS g 215 CYS g 226 CYS g 229
SITE 1 EC6 4 CYS h 12 CYS h 15 CYS h 26 CYS h 29
SITE 1 EC7 4 CYS i 112 CYS i 115 CYS i 126 CYS i 129
SITE 1 EC8 4 CYS j 212 CYS j 215 CYS j 226 CYS j 229
SITE 1 EC9 4 CYS k 12 CYS k 15 CYS k 26 CYS k 29
SITE 1 FC1 4 CYS l 112 CYS l 115 CYS l 126 CYS l 129
SITE 1 FC2 4 CYS m 212 CYS m 215 CYS m 226 CYS m 229
SITE 1 FC3 4 CYS H 112 CYS H 115 CYS H 126 CYS H 129
SITE 1 FC4 4 GLU A 53 GLU B 153 GLU C 253 HOH C1000
SITE 1 FC5 4 GLU D 53 HOH D 500 GLU E 153 GLU F 253
SITE 1 FC6 2 GLU I 253 HOH I1335
SITE 1 FC7 4 GLU J 53 GLU K 153 HOH K 671 GLU L 253
SITE 1 FC8 3 GLU M 53 GLU O 253 HOH O 842
SITE 1 FC9 5 GLU P 53 ILE Q 151 GLU Q 153 GLU R 253
SITE 2 FC9 5 HOH R 559
SITE 1 GC1 4 GLU S 53 GLU T 153 GLU U 253 HOH U1209
SITE 1 GC2 4 GLU V 53 HOH V 460 GLU W 153 GLU X 253
SITE 1 GC3 3 GLU 1 253 HOH 3 798 GLU Y 53
SITE 1 GC4 2 HOH 1 810 GLU 3 153
SITE 1 GC5 4 GLU 5 53 HOH 5 566 GLU 6 153 GLU 7 253
SITE 1 GC6 4 GLU 8 53 HOH 8 832 GLU 9 153 GLU a 253
SITE 1 GC7 4 GLU b 53 GLU c 153 HOH c 907 GLU d 253
SITE 1 GC8 5 GLU e 53 HOH e1293 GLU f 153 ILE g 251
SITE 2 GC8 5 GLU g 253
SITE 1 GC9 4 GLU h 53 GLU i 153 GLU j 253 HOH j 555
SITE 1 HC1 3 GLU k 53 GLU m 253 HOH m 557
CRYST1 118.544 99.865 123.178 90.00 117.61 90.00 P 1 21 1 96
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 0.008436 0.000000 0.004411 0.00000
SCALE2 0.000000 0.010014 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009161 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
