HEADER OXIDOREDUCTASE 13-MAR-03 1HL5
TITLE THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE
TITLE 2 DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, H, B, I, C, J, D, K, E, L, F, M, G, N, O, Q, P, S;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: EG118;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: YEP351
KEYWDS OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT,
KEYWDS 2 METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.W.STRANGE,S.ANTONYUK,M.A.HOUGH,P.DOUCETTE,J.RODRIGUEZ,P.J.HART,
AUTHOR 2 L.J.HAYWARD,J.S.VALENTINE,S.S.HASNAIN
REVDAT 3 13-JUL-11 1HL5 1 VERSN
REVDAT 2 24-FEB-09 1HL5 1 VERSN
REVDAT 1 08-MAY-03 1HL5 0
JRNL AUTH R.W.STRANGE,S.ANTONYUK,M.A.HOUGH,P.DOUCETTE,J.RODRIGUEZ,
JRNL AUTH 2 P.J.HART,L.J.HAYWARD,J.S.VALENTINE,S.S.HASNAIN
JRNL TITL THE STRUCTURE OF HOLO AND METAL-DEFICIENT WILD-TYPE HUMAN
JRNL TITL 2 CU, ZN SUPEROXIDE DISMUTASE AND ITS RELEVANCE TO FAMILIAL
JRNL TITL 3 AMYOTROPHIC LATERAL SCLEROSIS
JRNL REF J.MOL.BIOL. V. 328 877 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12729761
JRNL DOI 10.1016/S0022-2836(03)00355-3
REMARK 2
REMARK 2 RESOLUTION. 1.8 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 252571
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 13373
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 17869
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 969
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19783
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 1763
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.30000
REMARK 3 B22 (A**2) : -0.20000
REMARK 3 B33 (A**2) : -0.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.30000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.732
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20321 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 27413 ; 1.604 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2736 ; 4.679 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3480 ;18.312 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3024 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15516 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9366 ; 0.221 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 2918 ; 0.164 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 65 ; 0.086 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 121 ; 0.410 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 62 ; 0.282 ; 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): 13410 ; 0.835 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21294 ; 1.537 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6911 ; 2.558 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6119 ; 4.276 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 153
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9990 92.7450 77.5010
REMARK 3 T TENSOR
REMARK 3 T11: 0.2738 T22: 0.3268
REMARK 3 T33: 0.2285 T12: -0.0297
REMARK 3 T13: 0.0231 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.3939 L22: 1.7203
REMARK 3 L33: 2.4501 L12: 0.3695
REMARK 3 L13: -0.3914 L23: -0.6319
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: 0.0176 S13: 0.0329
REMARK 3 S21: 0.0771 S22: -0.0672 S23: -0.0479
REMARK 3 S31: 0.1542 S32: -0.0681 S33: 0.0517
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 153
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8230 80.8690 18.2360
REMARK 3 T TENSOR
REMARK 3 T11: 0.2560 T22: 0.3025
REMARK 3 T33: 0.2784 T12: 0.0048
REMARK 3 T13: 0.0016 T23: 0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 0.4364 L22: 1.0334
REMARK 3 L33: 1.9486 L12: 0.2720
REMARK 3 L13: 0.4686 L23: 0.7495
REMARK 3 S TENSOR
REMARK 3 S11: 0.0165 S12: 0.0149 S13: -0.0093
REMARK 3 S21: -0.0539 S22: 0.0235 S23: 0.0374
REMARK 3 S31: -0.0721 S32: -0.1209 S33: -0.0400
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 153
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2020 79.9080 21.0390
REMARK 3 T TENSOR
REMARK 3 T11: 0.2572 T22: 0.3237
REMARK 3 T33: 0.2667 T12: 0.0115
REMARK 3 T13: 0.0036 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.3464 L22: 0.8679
REMARK 3 L33: 1.7061 L12: 0.1293
REMARK 3 L13: 0.1464 L23: 0.3582
REMARK 3 S TENSOR
REMARK 3 S11: -0.0020 S12: 0.0380 S13: -0.0468
REMARK 3 S21: -0.0301 S22: 0.0157 S23: -0.0558
REMARK 3 S31: 0.0473 S32: 0.1287 S33: -0.0138
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 153
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0630 93.6740 74.8370
REMARK 3 T TENSOR
REMARK 3 T11: 0.2818 T22: 0.3293
REMARK 3 T33: 0.2494 T12: -0.0206
REMARK 3 T13: 0.0451 T23: 0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 0.4916 L22: 0.8767
REMARK 3 L33: 2.6184 L12: -0.0501
REMARK 3 L13: -0.5955 L23: -0.4587
REMARK 3 S TENSOR
REMARK 3 S11: 0.0509 S12: 0.0662 S13: 0.1022
REMARK 3 S21: -0.1570 S22: 0.0401 S23: -0.1000
REMARK 3 S31: 0.0299 S32: -0.1038 S33: -0.0910
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 153
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9430 120.4050 62.0100
REMARK 3 T TENSOR
REMARK 3 T11: 0.2553 T22: 0.2944
REMARK 3 T33: 0.2748 T12: -0.0007
REMARK 3 T13: -0.0046 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 0.4642 L22: 2.8620
REMARK 3 L33: 0.8262 L12: 0.2942
REMARK 3 L13: 0.2706 L23: 0.5787
REMARK 3 S TENSOR
REMARK 3 S11: -0.0397 S12: -0.0420 S13: -0.0332
REMARK 3 S21: -0.1147 S22: 0.0608 S23: -0.1131
REMARK 3 S31: 0.0056 S32: 0.0490 S33: -0.0212
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 3 F 153
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4560 111.6250 110.1710
REMARK 3 T TENSOR
REMARK 3 T11: 0.3467 T22: 0.2167
REMARK 3 T33: 0.3269 T12: 0.0330
REMARK 3 T13: -0.0607 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 0.4729 L22: 3.1975
REMARK 3 L33: 0.6928 L12: -0.8700
REMARK 3 L13: -0.2605 L23: 0.6916
REMARK 3 S TENSOR
REMARK 3 S11: -0.0166 S12: -0.0216 S13: -0.0197
REMARK 3 S21: 0.3467 S22: 0.1034 S23: -0.1312
REMARK 3 S31: 0.1893 S32: 0.0453 S33: -0.0867
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 1 G 153
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3640 148.3970 61.3980
REMARK 3 T TENSOR
REMARK 3 T11: 0.2854 T22: 0.2483
REMARK 3 T33: 0.6222 T12: 0.0851
REMARK 3 T13: -0.1576 T23: -0.2325
REMARK 3 L TENSOR
REMARK 3 L11: 1.1128 L22: 4.4067
REMARK 3 L33: 1.2002 L12: 1.7735
REMARK 3 L13: 0.8128 L23: 0.8956
REMARK 3 S TENSOR
REMARK 3 S11: -0.2732 S12: -0.3441 S13: 0.6269
REMARK 3 S21: -0.3784 S22: -0.2746 S23: 0.9741
REMARK 3 S31: -0.3241 S32: -0.1849 S33: 0.5478
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : O 1 O 153
REMARK 3 ORIGIN FOR THE GROUP (A): 40.1180 111.6310 105.0200
REMARK 3 T TENSOR
REMARK 3 T11: 0.2499 T22: 0.2039
REMARK 3 T33: 0.4878 T12: -0.0187
REMARK 3 T13: -0.0778 T23: 0.0295
REMARK 3 L TENSOR
REMARK 3 L11: 0.0761 L22: 6.0838
REMARK 3 L33: 0.8752 L12: -1.0256
REMARK 3 L13: -0.1423 L23: -0.3385
REMARK 3 S TENSOR
REMARK 3 S11: 0.0746 S12: 0.0198 S13: -0.2476
REMARK 3 S21: -0.2759 S22: 0.1527 S23: 0.8359
REMARK 3 S31: 0.1165 S32: -0.0899 S33: -0.2273
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 1 S 153
REMARK 3 ORIGIN FOR THE GROUP (A): 57.9290 121.2110 22.9610
REMARK 3 T TENSOR
REMARK 3 T11: 0.4754 T22: 0.3928
REMARK 3 T33: 0.1742 T12: 0.0564
REMARK 3 T13: 0.0342 T23: 0.0722
REMARK 3 L TENSOR
REMARK 3 L11: 4.2152 L22: 1.8234
REMARK 3 L33: 4.1287 L12: -0.9906
REMARK 3 L13: 0.0157 L23: -1.5566
REMARK 3 S TENSOR
REMARK 3 S11: -0.2512 S12: -0.7339 S13: -0.1908
REMARK 3 S21: 0.2698 S22: 0.2220 S23: -0.0985
REMARK 3 S31: -0.7130 S32: -0.2469 S33: 0.0291
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : P 1 P 153
REMARK 3 ORIGIN FOR THE GROUP (A): 38.4320 139.6630 30.5920
REMARK 3 T TENSOR
REMARK 3 T11: 0.7806 T22: 1.2086
REMARK 3 T33: 0.0690 T12: 0.8109
REMARK 3 T13: -0.1603 T23: -0.2814
REMARK 3 L TENSOR
REMARK 3 L11: 6.0487 L22: 6.4738
REMARK 3 L33: 11.4578 L12: -1.6345
REMARK 3 L13: -0.9648 L23: 2.9661
REMARK 3 S TENSOR
REMARK 3 S11: -0.3925 S12: -1.3673 S13: 0.5828
REMARK 3 S21: -0.4773 S22: -0.1079 S23: 0.4313
REMARK 3 S31: -1.2460 S32: -1.7686 S33: 0.5005
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : Q 1 Q 153
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5020 138.8560 106.5970
REMARK 3 T TENSOR
REMARK 3 T11: 0.2163 T22: 0.2577
REMARK 3 T33: 0.3483 T12: 0.0142
REMARK 3 T13: 0.0220 T23: 0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 1.3408 L22: 6.2236
REMARK 3 L33: 1.1933 L12: -2.4308
REMARK 3 L13: 0.3864 L23: -1.4006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0852 S12: 0.0309 S13: -0.3318
REMARK 3 S21: 0.1640 S22: 0.2546 S23: 0.5813
REMARK 3 S31: -0.0673 S32: -0.0760 S33: -0.1694
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 153
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3140 79.5130 101.4640
REMARK 3 T TENSOR
REMARK 3 T11: 0.3363 T22: 0.3116
REMARK 3 T33: 0.2280 T12: -0.0757
REMARK 3 T13: 0.0272 T23: 0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 0.7127 L22: 1.3878
REMARK 3 L33: 2.1333 L12: 0.5072
REMARK 3 L13: -0.7318 L23: -0.9628
REMARK 3 S TENSOR
REMARK 3 S11: -0.1679 S12: 0.0920 S13: 0.0556
REMARK 3 S21: -0.2056 S22: 0.1427 S23: -0.0094
REMARK 3 S31: 0.3755 S32: -0.1983 S33: 0.0253
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 153
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3570 93.9820 42.8170
REMARK 3 T TENSOR
REMARK 3 T11: 0.2748 T22: 0.2988
REMARK 3 T33: 0.2817 T12: -0.0076
REMARK 3 T13: 0.0376 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 0.5541 L22: 1.1616
REMARK 3 L33: 1.1983 L12: 0.3217
REMARK 3 L13: 0.1261 L23: 0.5121
REMARK 3 S TENSOR
REMARK 3 S11: 0.0836 S12: -0.0690 S13: 0.0100
REMARK 3 S21: 0.0553 S22: -0.0486 S23: 0.0149
REMARK 3 S31: -0.1109 S32: -0.0794 S33: -0.0350
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 153
REMARK 3 ORIGIN FOR THE GROUP (A): 43.0100 93.5360 45.2220
REMARK 3 T TENSOR
REMARK 3 T11: 0.2429 T22: 0.3125
REMARK 3 T33: 0.2646 T12: 0.0004
REMARK 3 T13: 0.0045 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.6400 L22: 1.1254
REMARK 3 L33: 2.0804 L12: 0.2251
REMARK 3 L13: 0.3216 L23: 0.6816
REMARK 3 S TENSOR
REMARK 3 S11: 0.0013 S12: -0.0196 S13: 0.0683
REMARK 3 S21: 0.0852 S22: -0.0039 S23: 0.0047
REMARK 3 S31: 0.0269 S32: 0.0291 S33: 0.0026
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 153
REMARK 3 ORIGIN FOR THE GROUP (A): -2.3960 80.0770 98.5420
REMARK 3 T TENSOR
REMARK 3 T11: 0.2647 T22: 0.2987
REMARK 3 T33: 0.2771 T12: -0.0088
REMARK 3 T13: -0.0144 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 0.4975 L22: 1.2445
REMARK 3 L33: 1.5452 L12: 0.2732
REMARK 3 L13: -0.3589 L23: -0.4334
REMARK 3 S TENSOR
REMARK 3 S11: -0.0106 S12: 0.0381 S13: -0.0258
REMARK 3 S21: -0.0029 S22: 0.1030 S23: 0.0164
REMARK 3 S31: 0.0964 S32: -0.1063 S33: -0.0925
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 2 L 153
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9600 148.0460 62.4030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2947 T22: 0.2789
REMARK 3 T33: 0.2908 T12: -0.0273
REMARK 3 T13: -0.0225 T23: -0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 0.7298 L22: 2.5633
REMARK 3 L33: 0.6707 L12: 0.8405
REMARK 3 L13: 0.0257 L23: 0.6937
REMARK 3 S TENSOR
REMARK 3 S11: -0.0812 S12: 0.0371 S13: 0.0803
REMARK 3 S21: -0.2901 S22: 0.0942 S23: -0.0203
REMARK 3 S31: -0.0679 S32: 0.0490 S33: -0.0130
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : M 2 M 153
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2370 139.6470 110.6090
REMARK 3 T TENSOR
REMARK 3 T11: 0.2764 T22: 0.2448
REMARK 3 T33: 0.3060 T12: 0.0229
REMARK 3 T13: -0.0236 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.5893 L22: 3.2359
REMARK 3 L33: 0.7857 L12: -0.2782
REMARK 3 L13: -0.1541 L23: 0.3645
REMARK 3 S TENSOR
REMARK 3 S11: 0.0038 S12: 0.0075 S13: -0.0058
REMARK 3 S21: 0.2012 S22: -0.0117 S23: -0.1268
REMARK 3 S31: 0.0239 S32: 0.0224 S33: 0.0079
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : N 1 N 153
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3360 120.9760 59.7200
REMARK 3 T TENSOR
REMARK 3 T11: 0.2026 T22: 0.3138
REMARK 3 T33: 0.2948 T12: -0.0036
REMARK 3 T13: 0.0290 T23: -0.0780
REMARK 3 L TENSOR
REMARK 3 L11: 1.9343 L22: 3.5719
REMARK 3 L33: 1.6670 L12: 1.5771
REMARK 3 L13: 0.5156 L23: 0.3822
REMARK 3 S TENSOR
REMARK 3 S11: -0.0159 S12: -0.3621 S13: 0.2038
REMARK 3 S21: -0.1528 S22: -0.1964 S23: 0.2927
REMARK 3 S31: 0.0223 S32: -0.1673 S33: 0.2122
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DISORDERED REGIONS IN MONOMERS O AND
REMARK 3 G WERE MODELED STEREOCHEMICALLY
REMARK 4
REMARK 4 1HL5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-MAR-03.
REMARK 100 THE PDBE ID CODE IS EBI-12308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 265996
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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 1SOS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CA ACETATE, 15% PEG 3350,
REMARK 280 0.1 M TRIS PH 8.0
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 86.19000
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, 5, 6, 7, 8, 9
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I
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 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, J
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 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, K
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 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, 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 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, N
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 BIOMOLECULE: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, Q
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 BIOMOLECULE: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: P, S
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 GLY E 108
REMARK 465 ASP E 109
REMARK 465 ALA F 1
REMARK 465 THR F 2
REMARK 465 GLN F 22
REMARK 465 LYS F 23
REMARK 465 GLU F 24
REMARK 465 SER F 25
REMARK 465 ASN F 26
REMARK 465 GLY F 27
REMARK 465 ALA L 1
REMARK 465 ALA M 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS C 30 NZ
REMARK 470 ASP D 11 CG OD1 OD2
REMARK 470 GLN D 15 OE1
REMARK 470 GLU D 24 CG CD OE1 OE2
REMARK 470 LYS D 30 NZ
REMARK 470 LYS D 70 CD CE NZ
REMARK 470 LYS D 122 CE NZ
REMARK 470 LYS D 136 CE NZ
REMARK 470 LYS E 3 CE NZ
REMARK 470 GLN E 15 OE1 NE2
REMARK 470 LYS E 23 CE NZ
REMARK 470 LYS E 70 NZ
REMARK 470 LYS E 75 CE NZ
REMARK 470 GLU E 77 OE1 OE2
REMARK 470 LYS E 91 NZ
REMARK 470 SER E 107 OG
REMARK 470 GLU E 132 CD OE1 OE2
REMARK 470 LYS F 3 N CA CB CG CD CE NZ
REMARK 470 GLN F 15 CD OE1 NE2
REMARK 470 GLU F 21 C O CD OE1 OE2
REMARK 470 LYS F 36 CG CD CE NZ
REMARK 470 LYS F 70 CD CE NZ
REMARK 470 LYS J 23 CD CE NZ
REMARK 470 LYS J 30 CE NZ
REMARK 470 LYS J 128 NZ
REMARK 470 LYS J 136 CE NZ
REMARK 470 GLN K 15 CD OE1 NE2
REMARK 470 LYS K 136 NZ
REMARK 470 LYS L 3 CD CE NZ
REMARK 470 LYS L 9 NZ
REMARK 470 GLN L 15 CD OE1 NE2
REMARK 470 LYS L 91 CE NZ
REMARK 470 THR M 2 N CA CB OG1 CG2
REMARK 470 GLN M 15 OE1 NE2
REMARK 470 GLU M 24 CA CB CG CD OE1 OE2
REMARK 470 SER M 25 CB OG
REMARK 470 ASN M 26 CB CG OD1 ND2
REMARK 470 LYS M 30 CE NZ
REMARK 470 LYS M 36 CE NZ
REMARK 470 LYS M 70 CD CE NZ
REMARK 470 LYS M 75 CD CE NZ
REMARK 470 LYS M 136 NZ
REMARK 470 LYS P 75 CE NZ
REMARK 470 LYS P 122 NZ
REMARK 470 GLU P 132 CA CB CG CD OE1 OE2
REMARK 470 LYS S 70 CE NZ
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 OD1 ASN B 53 O HOH B 2071 1.76
REMARK 500 NH1 ARG B 69 OE1 GLU B 78 2.06
REMARK 500 NH2 ARG B 69 OE2 GLU B 77 2.07
REMARK 500 NZ LYS J 3 OD2 ASP S 92 1.97
REMARK 500 O GLN J 153 OD1 ASP S 92 1.68
REMARK 500 OE1 GLU K 100 O HOH K 2100 2.19
REMARK 500 OE2 GLU N 133 O HOH N 2076 2.08
REMARK 500 O GLU O 24 N ASN O 26 2.18
REMARK 500 NH2 ARG O 79 OD1 ASP O 101 2.17
REMARK 500 O HOH A 2080 O HOH A 2081 2.12
REMARK 500 O HOH J 2046 O HOH J 2109 2.10
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 NZ LYS B 122 OE2 GLU M 40 1546 1.92
REMARK 500 O THR M 54 OE2 GLU S 132 1456 1.86
REMARK 500 O HOH H 2064 O HOH C 2120 1556 2.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 96 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 109 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 VAL B 31 CG1 - CB - CG2 ANGL. DEV. = 10.7 DEGREES
REMARK 500 ASP B 109 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP C 101 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 VAL D 31 CG1 - CB - CG2 ANGL. DEV. = 11.2 DEGREES
REMARK 500 ARG D 79 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG D 79 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG F 79 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG F 79 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP F 101 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP G 83 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP I 96 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP I 101 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP I 109 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP L 76 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP L 92 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP M 109 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP M 124 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG N 79 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP O 83 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG Q 79 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG Q 79 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ASP Q 101 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 65 65.58 -154.33
REMARK 500 ASN C 26 -4.95 67.09
REMARK 500 ASN D 26 4.68 58.69
REMARK 500 ASN D 65 65.73 -151.65
REMARK 500 ASN E 26 -0.19 70.71
REMARK 500 ASN E 65 67.36 -151.64
REMARK 500 ASN G 65 73.36 -160.29
REMARK 500 ASN G 131 155.03 1.84
REMARK 500 SER G 142 156.12 -49.95
REMARK 500 ASN H 65 60.76 -150.80
REMARK 500 ASN K 26 5.04 59.47
REMARK 500 SER O 25 35.77 -49.53
REMARK 500 ASN O 26 -5.59 169.07
REMARK 500 ASN O 65 77.53 -153.18
REMARK 500 ASP P 90 -169.18 -79.64
REMARK 500 THR Q 2 129.50 -23.76
REMARK 500 GLU Q 24 -122.30 -116.15
REMARK 500 ASN S 65 55.60 -150.09
REMARK 500 ARG S 115 -167.74 -101.87
REMARK 500 SER S 142 153.02 -44.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 THR G 2 23.5 L L OUTSIDE RANGE
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 CU A 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 120 NE2
REMARK 620 2 HIS A 46 ND1 95.8
REMARK 620 3 HIS A 48 NE2 111.6 132.5
REMARK 620 4 HIS A 63 NE2 141.3 78.0 99.7
REMARK 620 5 HOH A2047 O 83.1 124.2 97.8 70.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 46 ND1
REMARK 620 2 HIS B 63 NE2 76.3
REMARK 620 3 HOH B2083 O 117.6 65.9
REMARK 620 4 HIS B 48 NE2 131.2 100.0 103.8
REMARK 620 5 HIS B 120 NE2 93.8 141.8 87.8 113.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU C 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 46 ND1
REMARK 620 2 HIS C 48 NE2 133.8
REMARK 620 3 HIS C 120 NE2 96.9 112.4
REMARK 620 4 HOH C2074 O 118.2 99.2 86.5
REMARK 620 5 HIS C 63 NE2 78.0 97.2 141.3 64.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU D 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 63 NE2
REMARK 620 2 HOH D2049 O 64.1
REMARK 620 3 HIS D 46 ND1 77.2 120.0
REMARK 620 4 HIS D 48 NE2 96.4 95.6 134.3
REMARK 620 5 HIS D 120 NE2 138.9 82.9 101.3 111.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU E 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E2052 O
REMARK 620 2 HIS E 46 ND1 120.3
REMARK 620 3 HIS E 120 NE2 85.9 94.0
REMARK 620 4 HIS E 63 NE2 66.6 79.6 142.4
REMARK 620 5 HIS E 48 NE2 98.5 134.0 113.7 96.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU F 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F2040 O
REMARK 620 2 HIS F 46 ND1 121.4
REMARK 620 3 HIS F 63 NE2 66.2 77.9
REMARK 620 4 HIS F 120 NE2 86.8 96.0 142.0
REMARK 620 5 HIS F 48 NE2 94.5 136.3 97.6 111.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU G 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 63 NE2
REMARK 620 2 HIS G 48 NE2 93.1
REMARK 620 3 HOH G2022 O 56.6 96.2
REMARK 620 4 HIS G 46 ND1 75.7 132.7 113.3
REMARK 620 5 HIS G 120 NE2 146.2 116.6 101.7 93.4
REMARK 620 6 HOH G2010 O 127.8 66.3 161.2 84.7 81.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU H 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 46 ND1
REMARK 620 2 HIS H 120 NE2 94.3
REMARK 620 3 HOH H2050 O 127.2 88.0
REMARK 620 4 HIS H 48 NE2 138.5 110.9 87.4
REMARK 620 5 HIS H 63 NE2 82.7 141.5 65.0 95.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU I 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 46 ND1
REMARK 620 2 HIS I 48 NE2 137.8
REMARK 620 3 HIS I 63 NE2 76.6 97.9
REMARK 620 4 HIS I 120 NE2 95.9 112.1 140.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU J 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J 120 NE2
REMARK 620 2 HOH J2064 O 84.1
REMARK 620 3 HIS J 48 NE2 112.8 99.1
REMARK 620 4 HIS J 46 ND1 96.3 119.3 134.1
REMARK 620 5 HIS J 63 NE2 142.7 68.7 96.9 76.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU K 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K 48 NE2
REMARK 620 2 HIS K 46 ND1 133.0
REMARK 620 3 HIS K 63 NE2 97.4 79.3
REMARK 620 4 HIS K 120 NE2 111.2 95.6 144.0
REMARK 620 5 HOH K2063 O 98.0 122.8 68.5 85.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU L 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L 120 NE2
REMARK 620 2 HIS L 46 ND1 100.0
REMARK 620 3 HIS L 48 NE2 115.9 134.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU M 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS M 120 NE2
REMARK 620 2 HOH M2041 O 86.0
REMARK 620 3 HIS M 48 NE2 110.5 96.4
REMARK 620 4 HIS M 46 ND1 95.7 120.3 136.5
REMARK 620 5 HIS M 63 NE2 142.6 66.4 97.7 78.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU N 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 46 ND1
REMARK 620 2 HIS N 48 NE2 137.0
REMARK 620 3 HIS N 63 NE2 77.4 94.4
REMARK 620 4 HIS N 120 NE2 95.9 114.9 140.2
REMARK 620 5 HOH N2038 O 116.3 96.3 63.9 85.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU O 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 63 NE2
REMARK 620 2 HIS O 46 ND1 77.5
REMARK 620 3 HIS O 120 NE2 136.6 98.7
REMARK 620 4 HIS O 48 NE2 99.0 144.3 106.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU P 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 48 NE2
REMARK 620 2 HIS P 46 ND1 155.5
REMARK 620 3 HIS P 120 NE2 92.3 96.5
REMARK 620 4 HIS P 63 NE2 105.4 87.7 126.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU Q 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Q 48 NE2
REMARK 620 2 HIS Q 46 ND1 132.7
REMARK 620 3 HIS Q 63 NE2 98.7 78.5
REMARK 620 4 HOH Q2040 O 98.2 121.5 65.4
REMARK 620 5 HIS Q 120 NE2 112.3 99.0 137.4 81.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU S 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS S 120 NE2
REMARK 620 2 HIS S 48 NE2 116.0
REMARK 620 3 HIS S 46 ND1 97.6 130.3
REMARK 620 4 HIS S 63 NE2 137.4 93.6 83.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 63 ND1
REMARK 620 2 ASP A 83 OD1 104.7
REMARK 620 3 HIS A 71 ND1 106.6 95.7
REMARK 620 4 HIS A 80 ND1 112.5 114.1 121.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 71 ND1
REMARK 620 2 HIS B 80 ND1 120.6
REMARK 620 3 ASP B 83 OD1 96.0 114.4
REMARK 620 4 HIS B 63 ND1 106.5 111.8 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 71 ND1
REMARK 620 2 HIS C 63 ND1 107.7
REMARK 620 3 ASP C 83 OD1 95.7 104.5
REMARK 620 4 HIS C 80 ND1 120.6 111.5 114.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 71 ND1
REMARK 620 2 HIS D 80 ND1 123.1
REMARK 620 3 HIS D 63 ND1 103.4 111.7
REMARK 620 4 ASP D 83 OD1 96.1 115.3 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 71 ND1
REMARK 620 2 HIS E 80 ND1 120.4
REMARK 620 3 ASP E 83 OD1 98.0 114.3
REMARK 620 4 HIS E 63 ND1 106.0 113.5 102.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 63 ND1
REMARK 620 2 HIS F 71 ND1 107.1
REMARK 620 3 HIS F 80 ND1 108.5 121.4
REMARK 620 4 ASP F 83 OD1 107.1 94.8 116.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 63 ND1
REMARK 620 2 HIS G 80 ND1 108.3
REMARK 620 3 HIS G 71 ND1 107.2 121.2
REMARK 620 4 ASP G 83 OD1 105.7 118.8 94.0
REMARK 620 5 ASP G 83 OD2 156.9 91.7 70.0 52.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 63 ND1
REMARK 620 2 HIS H 80 ND1 110.2
REMARK 620 3 ASP H 83 OD1 107.0 112.6
REMARK 620 4 HIS H 71 ND1 105.1 123.3 97.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 80 ND1
REMARK 620 2 ASP I 83 OD1 114.7
REMARK 620 3 HIS I 63 ND1 108.5 103.4
REMARK 620 4 HIS I 71 ND1 123.3 98.2 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN J 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J 63 ND1
REMARK 620 2 HIS J 71 ND1 109.0
REMARK 620 3 HIS J 80 ND1 110.7 118.0
REMARK 620 4 ASP J 83 OD1 108.1 98.2 111.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN K 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K 63 ND1
REMARK 620 2 HIS K 71 ND1 107.6
REMARK 620 3 HIS K 80 ND1 110.8 121.1
REMARK 620 4 ASP K 83 OD1 105.3 98.0 112.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN L 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L 63 ND1
REMARK 620 2 HIS L 71 ND1 105.9
REMARK 620 3 ASP L 83 OD1 105.0 97.9
REMARK 620 4 HIS L 80 ND1 112.7 119.1 114.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN M 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS M 63 ND1
REMARK 620 2 HIS M 71 ND1 106.5
REMARK 620 3 HIS M 80 ND1 112.8 122.2
REMARK 620 4 ASP M 83 OD1 104.5 96.0 112.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN N 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 71 ND1
REMARK 620 2 ASP N 83 OD1 98.3
REMARK 620 3 HIS N 63 ND1 109.9 102.5
REMARK 620 4 HIS N 80 ND1 120.9 114.2 109.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN O 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 71 ND1
REMARK 620 2 ASP O 83 OD1 98.4
REMARK 620 3 HIS O 63 ND1 106.4 105.9
REMARK 620 4 HIS O 80 ND1 121.0 109.4 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN P 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 63 ND1
REMARK 620 2 HIS P 80 ND1 103.2
REMARK 620 3 HIS P 71 ND1 104.6 118.9
REMARK 620 4 ASP P 83 OD1 106.6 123.4 98.4
REMARK 620 5 ASP P 83 OD2 158.6 89.2 83.7 52.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN Q 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Q 71 ND1
REMARK 620 2 HIS Q 80 ND1 118.7
REMARK 620 3 ASP Q 83 OD1 99.3 112.2
REMARK 620 4 HIS Q 63 ND1 110.2 111.0 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN S 155 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS S 63 ND1
REMARK 620 2 HIS S 71 ND1 102.8
REMARK 620 3 ASP S 83 OD1 105.8 90.8
REMARK 620 4 HIS S 80 ND1 108.8 125.2 120.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 156 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 26 O
REMARK 620 2 ASN C 26 OD1 64.4
REMARK 620 3 SER C 102 O 132.5 160.6
REMARK 620 4 HOH C2035 O 63.4 117.2 72.7
REMARK 620 5 HOH C2038 O 75.7 113.1 83.5 84.9
REMARK 620 6 HOH C2106 O 139.6 91.0 69.7 107.5 144.6
REMARK 620 7 HOH C2037 O 131.6 83.4 87.9 159.4 86.0 70.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 156 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D2072 O
REMARK 620 2 ASN D 26 O 138.0
REMARK 620 3 ASN D 26 OD1 79.2 73.6
REMARK 620 4 SER D 102 O 87.4 123.1 163.2
REMARK 620 5 HOH A2063 O 82.1 128.6 90.3 77.6
REMARK 620 6 HOH D2024 O 81.8 76.6 107.3 80.6 153.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA O 156 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER H 102 O
REMARK 620 2 HOH H2084 O 85.7
REMARK 620 3 HOH H2085 O 84.3 80.7
REMARK 620 4 ASN H 26 OD1 160.5 77.3 102.0
REMARK 620 5 HOH H2081 O 73.9 79.8 151.6 93.5
REMARK 620 6 ASN H 26 O 130.5 133.6 76.6 68.9 131.6
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700
REMARK 700 THE SHEETS PRESENTED AS "PA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 156
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 156
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU H 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU I 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU J 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU K 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU L 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU M 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN M 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU N 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU O 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN O 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA O 156
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU P 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU Q 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN Q 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU S 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN S 155
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AZV RELATED DB: PDB
REMARK 900 FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)
REMARK 900 RELATED ID: 1BA9 RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED MONOMERIC
REMARK 900 SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES
REMARK 900 RELATED ID: 1DSW RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF A MONOMERIC,
REMARK 900 REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE
REMARK 900 DISMUTASE BEARING THE SAMECHARGE AS THE
REMARK 900 NATIVE PROTEIN
REMARK 900 RELATED ID: 1FUN RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH LYS 136
REMARK 900 REPLACED BY GLU, CYS 6 REPLACED BY ALA
REMARK 900 AND CYS 111 REPLACED BY SER (K136E, C6A,
REMARK 900 C111S)
REMARK 900 RELATED ID: 1HL4 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF APO TYPE HUMAN CU, ZN
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1KMG RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF MONOMERIC COPPER-
REMARK 900 FREE SUPEROXIDEDISMUTASE
REMARK 900 RELATED ID: 1L3N RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED DIMERIC
REMARK 900 COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF
REMARK 900 DIMERIZATION
REMARK 900 RELATED ID: 1MFM RELATED DB: PDB
REMARK 900 MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q
REMARK 900 AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 1N18 RELATED DB: PDB
REMARK 900 THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE
REMARK 900 DISMUTASE, C6A,C111S
REMARK 900 RELATED ID: 1N19 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HSOD A4V MUTANT
REMARK 900 RELATED ID: 1SOS RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH CYS 6
REMARK 900 REPLACED BY ALA AND CYS 111 REPLACED BY
REMARK 900 SER (C6A, C111S)
REMARK 900 RELATED ID: 1SPD RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 4SOD RELATED DB: PDB
REMARK 900 CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS
REMARK 900 6 REPLACED BY ALA AND CYS 111 REPLACED
REMARK 900 BY SER (C6A,C111S) WITH AN 18-RESIDUE
REMARK 900 HEPARIN-BINDING PEPTIDE FUSED TO THE C-
REMARK 900 TERMINUS (THEORETICAL MODEL)
DBREF 1HL5 A 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 B 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 C 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 D 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 E 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 F 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 G 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 H 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 I 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 J 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 K 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 L 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 M 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 N 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 O 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 P 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 Q 1 153 UNP P00441 SODC_HUMAN 2 154
DBREF 1HL5 S 1 153 UNP P00441 SODC_HUMAN 2 154
SEQRES 1 A 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 A 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 A 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 A 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 A 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 A 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 A 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 A 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 A 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 A 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 A 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 A 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 B 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 B 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 B 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 B 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 B 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 B 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 B 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 B 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 B 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 B 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 B 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 B 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 C 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 C 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 C 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 C 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 C 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 C 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 C 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 C 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 C 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 C 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 C 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 C 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 D 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 D 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 D 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 D 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 D 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 D 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 D 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 D 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 D 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 D 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 D 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 D 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 E 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 E 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 E 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 E 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 E 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 E 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 E 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 E 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 E 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 E 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 E 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 E 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 F 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 F 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 F 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 F 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 F 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 F 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 F 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 F 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 F 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 F 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 F 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 F 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 G 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 G 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 G 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 G 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 G 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 G 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 G 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 G 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 G 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 G 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 G 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 G 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 H 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 H 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 H 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 H 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 H 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 H 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 H 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 H 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 H 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 H 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 H 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 H 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 I 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 I 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 I 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 I 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 I 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 I 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 I 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 I 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 I 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 I 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 I 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 I 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 J 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 J 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 J 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 J 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 J 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 J 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 J 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 J 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 J 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 J 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 J 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 J 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 K 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 K 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 K 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 K 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 K 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 K 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 K 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 K 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 K 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 K 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 K 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 K 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 L 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 L 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 L 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 L 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 L 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 L 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 L 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 L 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 L 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 L 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 L 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 L 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 M 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 M 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 M 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 M 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 M 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 M 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 M 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 M 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 M 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 M 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 M 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 M 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 N 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 N 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 N 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 N 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 N 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 N 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 N 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 N 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 N 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 N 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 N 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 N 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 O 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 O 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 O 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 O 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 O 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 O 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 O 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 O 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 O 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 O 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 O 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 O 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 P 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 P 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 P 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 P 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 P 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 P 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 P 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 P 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 P 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 P 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 P 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 P 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 Q 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 Q 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 Q 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 Q 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 Q 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 Q 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 Q 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 Q 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 Q 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 Q 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 Q 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 Q 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
SEQRES 1 S 153 ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO
SEQRES 2 S 153 VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN
SEQRES 3 S 153 GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR
SEQRES 4 S 153 GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP
SEQRES 5 S 153 ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN
SEQRES 6 S 153 PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU
SEQRES 7 S 153 ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS
SEQRES 8 S 153 ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE
SEQRES 9 S 153 SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU
SEQRES 10 S 153 VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY
SEQRES 11 S 153 ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG
SEQRES 12 S 153 LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN
HET CU A 154 1
HET ZN A 155 1
HET CU B 154 1
HET ZN B 155 1
HET CU C 154 1
HET ZN C 155 1
HET CA C 156 1
HET CU D 154 1
HET ZN D 155 1
HET CA D 156 1
HET CU E 154 1
HET ZN E 155 1
HET CU F 154 1
HET ZN F 155 1
HET CU G 154 1
HET ZN G 155 1
HET CU H 154 1
HET ZN H 155 1
HET CU I 154 1
HET ZN I 155 1
HET CU J 154 1
HET ZN J 155 1
HET CU K 154 1
HET ZN K 155 1
HET CU L 154 1
HET ZN L 155 1
HET CU M 154 1
HET ZN M 155 1
HET CU N 154 1
HET ZN N 155 1
HET CU O 154 1
HET ZN O 155 1
HET CA O 156 1
HET CU P 154 1
HET ZN P 155 1
HET CU Q 154 1
HET ZN Q 155 1
HET CU S 154 1
HET ZN S 155 1
HETNAM CU COPPER (II) ION
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 19 CU 18(CU 2+)
FORMUL 20 ZN 18(ZN 2+)
FORMUL 25 CA 3(CA 2+)
FORMUL 58 HOH *1763(H2 O)
HELIX 1 1 ALA A 55 GLY A 61 5 7
HELIX 2 2 GLU A 133 GLY A 138 1 6
HELIX 3 3 ALA B 55 ALA B 60 5 6
HELIX 4 4 GLU B 133 GLY B 138 1 6
HELIX 5 5 ALA C 55 GLY C 61 5 7
HELIX 6 6 GLU C 133 GLY C 138 1 6
HELIX 7 7 ALA D 55 GLY D 61 5 7
HELIX 8 8 GLU D 133 GLY D 138 1 6
HELIX 9 9 ALA E 55 GLY E 61 5 7
HELIX 10 10 GLU E 133 GLY E 138 1 6
HELIX 11 11 ALA F 55 GLY F 61 5 7
HELIX 12 12 GLU F 133 GLY F 138 1 6
HELIX 13 13 ALA G 55 GLY G 61 5 7
HELIX 14 14 SER G 107 HIS G 110 5 4
HELIX 15 15 ASN G 131 THR G 137 1 7
HELIX 16 16 ALA H 55 GLY H 61 5 7
HELIX 17 17 SER H 107 HIS H 110 5 4
HELIX 18 18 GLU H 133 GLY H 138 1 6
HELIX 19 19 ALA I 55 GLY I 61 5 7
HELIX 20 20 GLU I 133 GLY I 138 1 6
HELIX 21 21 ALA J 55 GLY J 61 5 7
HELIX 22 22 SER J 107 HIS J 110 5 4
HELIX 23 23 GLU J 133 GLY J 138 1 6
HELIX 24 24 ALA K 55 GLY K 61 5 7
HELIX 25 25 GLU K 133 GLY K 138 1 6
HELIX 26 26 ALA L 55 GLY L 61 5 7
HELIX 27 27 GLU L 133 GLY L 138 1 6
HELIX 28 28 GLY M 56 GLY M 61 5 6
HELIX 29 29 GLU M 133 GLY M 138 1 6
HELIX 30 30 ALA N 55 GLY N 61 5 7
HELIX 31 31 GLU N 133 GLY N 138 1 6
HELIX 32 32 ALA O 55 GLY O 61 5 7
HELIX 33 33 GLU O 133 GLY O 138 1 6
HELIX 34 34 ALA P 55 GLY P 61 5 7
HELIX 35 35 GLU P 133 GLY P 138 1 6
HELIX 36 36 ALA Q 55 GLY Q 61 5 7
HELIX 37 37 GLU Q 133 GLY Q 138 1 6
HELIX 38 38 ALA S 55 GLY S 61 5 7
HELIX 39 39 GLU S 133 GLY S 138 1 6
SHEET 1 AA 5 ALA A 95 ASP A 101 0
SHEET 2 AA 5 VAL A 29 LYS A 36 -1 O VAL A 29 N ASP A 101
SHEET 3 AA 5 GLN A 15 GLN A 22 -1 O GLN A 15 N LYS A 36
SHEET 4 AA 5 THR A 2 LYS A 9 -1 O THR A 2 N GLN A 22
SHEET 5 AA 5 GLY A 150 ILE A 151 -1 O GLY A 150 N VAL A 5
SHEET 1 AB 4 ASP A 83 ALA A 89 0
SHEET 2 AB 4 GLY A 41 HIS A 48 -1 O GLY A 41 N ALA A 89
SHEET 3 AB 4 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 4 AB 4 ARG A 143 VAL A 148 -1 N LEU A 144 O VAL A 119
SHEET 1 BA 5 ALA B 95 ASP B 101 0
SHEET 2 BA 5 VAL B 29 LYS B 36 -1 O VAL B 29 N ASP B 101
SHEET 3 BA 5 GLN B 15 GLN B 22 -1 O GLN B 15 N LYS B 36
SHEET 4 BA 5 THR B 2 LEU B 8 -1 O THR B 2 N GLN B 22
SHEET 5 BA 5 GLY B 150 ILE B 151 -1 O GLY B 150 N VAL B 5
SHEET 1 BB 4 ASP B 83 ALA B 89 0
SHEET 2 BB 4 GLY B 41 HIS B 48 -1 O GLY B 41 N ALA B 89
SHEET 3 BB 4 THR B 116 HIS B 120 -1 O THR B 116 N HIS B 48
SHEET 4 BB 4 ARG B 143 VAL B 148 -1 N LEU B 144 O VAL B 119
SHEET 1 CA 5 ALA C 95 ASP C 101 0
SHEET 2 CA 5 VAL C 29 LYS C 36 -1 O VAL C 29 N ASP C 101
SHEET 3 CA 5 GLN C 15 GLN C 22 -1 O GLN C 15 N LYS C 36
SHEET 4 CA 5 THR C 2 LEU C 8 -1 O THR C 2 N GLN C 22
SHEET 5 CA 5 GLY C 150 ILE C 151 -1 O GLY C 150 N VAL C 5
SHEET 1 CB 4 ASP C 83 ALA C 89 0
SHEET 2 CB 4 GLY C 41 HIS C 48 -1 O GLY C 41 N ALA C 89
SHEET 3 CB 4 THR C 116 HIS C 120 -1 O THR C 116 N HIS C 48
SHEET 4 CB 4 ARG C 143 VAL C 148 -1 N LEU C 144 O VAL C 119
SHEET 1 DA 5 ALA D 95 ASP D 101 0
SHEET 2 DA 5 VAL D 29 LYS D 36 -1 O VAL D 29 N ASP D 101
SHEET 3 DA 5 GLN D 15 GLN D 22 -1 O GLN D 15 N LYS D 36
SHEET 4 DA 5 THR D 2 LEU D 8 -1 O THR D 2 N GLN D 22
SHEET 5 DA 5 GLY D 150 ILE D 151 -1 O GLY D 150 N VAL D 5
SHEET 1 DB 4 ASP D 83 ALA D 89 0
SHEET 2 DB 4 GLY D 41 HIS D 48 -1 O GLY D 41 N ALA D 89
SHEET 3 DB 4 THR D 116 HIS D 120 -1 O THR D 116 N HIS D 48
SHEET 4 DB 4 ARG D 143 VAL D 148 -1 N LEU D 144 O VAL D 119
SHEET 1 EA 5 ALA E 95 ASP E 101 0
SHEET 2 EA 5 VAL E 29 LYS E 36 -1 O VAL E 29 N ASP E 101
SHEET 3 EA 5 GLN E 15 GLN E 22 -1 O GLN E 15 N LYS E 36
SHEET 4 EA 5 THR E 2 LEU E 8 -1 O THR E 2 N GLN E 22
SHEET 5 EA 5 GLY E 150 ILE E 151 -1 O GLY E 150 N VAL E 5
SHEET 1 EB 4 ASP E 83 ALA E 89 0
SHEET 2 EB 4 GLY E 41 HIS E 48 -1 O GLY E 41 N ALA E 89
SHEET 3 EB 4 THR E 116 HIS E 120 -1 O THR E 116 N HIS E 48
SHEET 4 EB 4 ARG E 143 VAL E 148 -1 N LEU E 144 O VAL E 119
SHEET 1 FA 9 LYS F 3 LYS F 9 0
SHEET 2 FA 9 GLN F 15 GLU F 21 -1 O GLY F 16 N LEU F 8
SHEET 3 FA 9 VAL F 29 LYS F 36 -1 O LYS F 30 N GLU F 21
SHEET 4 FA 9 ALA F 95 ASP F 101 -1 O ALA F 95 N ILE F 35
SHEET 5 FA 9 ASP F 83 ALA F 89 -1 O THR F 88 N ASP F 96
SHEET 6 FA 9 GLY F 41 HIS F 48 -1 O GLY F 41 N ALA F 89
SHEET 7 FA 9 THR F 116 HIS F 120 -1 O THR F 116 N HIS F 48
SHEET 8 FA 9 ARG F 143 ILE F 151 -1 N LEU F 144 O VAL F 119
SHEET 9 FA 9 LYS F 3 LYS F 9 -1 O VAL F 5 N GLY F 150
SHEET 1 GA 5 ALA G 95 ASP G 101 0
SHEET 2 GA 5 VAL G 29 LYS G 36 -1 O VAL G 29 N ASP G 101
SHEET 3 GA 5 GLN G 15 GLN G 22 -1 O GLN G 15 N LYS G 36
SHEET 4 GA 5 THR G 2 LEU G 8 -1 O THR G 2 N GLN G 22
SHEET 5 GA 5 GLY G 150 ALA G 152 -1 O GLY G 150 N VAL G 5
SHEET 1 GB 4 ASP G 83 ALA G 89 0
SHEET 2 GB 4 GLY G 41 HIS G 48 -1 O GLY G 41 N ALA G 89
SHEET 3 GB 4 THR G 116 HIS G 120 -1 O THR G 116 N HIS G 48
SHEET 4 GB 4 ARG G 143 VAL G 148 -1 N LEU G 144 O VAL G 119
SHEET 1 HA 5 ALA H 95 ASP H 101 0
SHEET 2 HA 5 VAL H 29 LYS H 36 -1 O VAL H 29 N ASP H 101
SHEET 3 HA 5 GLN H 15 GLN H 22 -1 O GLN H 15 N LYS H 36
SHEET 4 HA 5 THR H 2 LEU H 8 -1 O THR H 2 N GLN H 22
SHEET 5 HA 5 GLY H 150 ILE H 151 -1 O GLY H 150 N VAL H 5
SHEET 1 HB 4 ASP H 83 ALA H 89 0
SHEET 2 HB 4 GLY H 41 HIS H 48 -1 O GLY H 41 N ALA H 89
SHEET 3 HB 4 THR H 116 HIS H 120 -1 O THR H 116 N HIS H 48
SHEET 4 HB 4 ARG H 143 VAL H 148 -1 N LEU H 144 O VAL H 119
SHEET 1 IA 5 ALA I 95 ASP I 101 0
SHEET 2 IA 5 VAL I 29 LYS I 36 -1 O VAL I 29 N ASP I 101
SHEET 3 IA 5 GLN I 15 GLN I 22 -1 O GLN I 15 N LYS I 36
SHEET 4 IA 5 THR I 2 LEU I 8 -1 O THR I 2 N GLN I 22
SHEET 5 IA 5 GLY I 150 ILE I 151 -1 O GLY I 150 N VAL I 5
SHEET 1 IB 4 ASP I 83 ALA I 89 0
SHEET 2 IB 4 GLY I 41 HIS I 48 -1 O GLY I 41 N ALA I 89
SHEET 3 IB 4 THR I 116 HIS I 120 -1 O THR I 116 N HIS I 48
SHEET 4 IB 4 ARG I 143 VAL I 148 -1 N LEU I 144 O VAL I 119
SHEET 1 JA 5 ALA J 95 ASP J 101 0
SHEET 2 JA 5 VAL J 29 LYS J 36 -1 O VAL J 29 N ASP J 101
SHEET 3 JA 5 GLN J 15 GLN J 22 -1 O GLN J 15 N LYS J 36
SHEET 4 JA 5 THR J 2 LEU J 8 -1 O THR J 2 N GLN J 22
SHEET 5 JA 5 GLY J 150 ILE J 151 -1 O GLY J 150 N VAL J 5
SHEET 1 JB 4 ASP J 83 ALA J 89 0
SHEET 2 JB 4 GLY J 41 HIS J 48 -1 O GLY J 41 N ALA J 89
SHEET 3 JB 4 THR J 116 HIS J 120 -1 O THR J 116 N HIS J 48
SHEET 4 JB 4 ARG J 143 VAL J 148 -1 N LEU J 144 O VAL J 119
SHEET 1 KA 5 ALA K 95 ASP K 101 0
SHEET 2 KA 5 VAL K 29 LYS K 36 -1 O VAL K 29 N ASP K 101
SHEET 3 KA 5 GLN K 15 GLN K 22 -1 O GLN K 15 N LYS K 36
SHEET 4 KA 5 THR K 2 LYS K 9 -1 O THR K 2 N GLN K 22
SHEET 5 KA 5 GLY K 150 ILE K 151 -1 O GLY K 150 N VAL K 5
SHEET 1 KB 4 ASP K 83 ALA K 89 0
SHEET 2 KB 4 GLY K 41 HIS K 48 -1 O GLY K 41 N ALA K 89
SHEET 3 KB 4 THR K 116 HIS K 120 -1 O THR K 116 N HIS K 48
SHEET 4 KB 4 ARG K 143 VAL K 148 -1 N LEU K 144 O VAL K 119
SHEET 1 LA 5 ALA L 95 ASP L 101 0
SHEET 2 LA 5 VAL L 29 LYS L 36 -1 O VAL L 29 N ASP L 101
SHEET 3 LA 5 GLN L 15 GLN L 22 -1 O GLN L 15 N LYS L 36
SHEET 4 LA 5 LYS L 3 LEU L 8 -1 O ALA L 4 N PHE L 20
SHEET 5 LA 5 GLY L 150 ILE L 151 -1 O GLY L 150 N VAL L 5
SHEET 1 LB 4 ASP L 83 ALA L 89 0
SHEET 2 LB 4 GLY L 41 HIS L 48 -1 O GLY L 41 N ALA L 89
SHEET 3 LB 4 THR L 116 HIS L 120 -1 O THR L 116 N HIS L 48
SHEET 4 LB 4 ARG L 143 VAL L 148 -1 N LEU L 144 O VAL L 119
SHEET 1 MA 5 ALA M 95 ASP M 101 0
SHEET 2 MA 5 VAL M 29 LYS M 36 -1 O VAL M 29 N ASP M 101
SHEET 3 MA 5 GLN M 15 GLN M 22 -1 O GLN M 15 N LYS M 36
SHEET 4 MA 5 THR M 2 LEU M 8 -1 O THR M 2 N GLN M 22
SHEET 5 MA 5 GLY M 150 ILE M 151 -1 O GLY M 150 N VAL M 5
SHEET 1 MB 4 ASP M 83 ALA M 89 0
SHEET 2 MB 4 GLY M 41 HIS M 48 -1 O GLY M 41 N ALA M 89
SHEET 3 MB 4 THR M 116 HIS M 120 -1 O THR M 116 N HIS M 48
SHEET 4 MB 4 ARG M 143 VAL M 148 -1 N LEU M 144 O VAL M 119
SHEET 1 NA 5 ALA N 95 ASP N 101 0
SHEET 2 NA 5 VAL N 29 LYS N 36 -1 O VAL N 29 N ASP N 101
SHEET 3 NA 5 GLN N 15 GLN N 22 -1 O GLN N 15 N LYS N 36
SHEET 4 NA 5 LYS N 3 LEU N 8 -1 O ALA N 4 N PHE N 20
SHEET 5 NA 5 GLY N 150 ILE N 151 -1 O GLY N 150 N VAL N 5
SHEET 1 NB 4 ASP N 83 ALA N 89 0
SHEET 2 NB 4 GLY N 41 HIS N 48 -1 O GLY N 41 N ALA N 89
SHEET 3 NB 4 THR N 116 HIS N 120 -1 O THR N 116 N HIS N 48
SHEET 4 NB 4 ARG N 143 VAL N 148 -1 N LEU N 144 O VAL N 119
SHEET 1 OA 5 ALA O 95 ASP O 101 0
SHEET 2 OA 5 VAL O 29 LYS O 36 -1 O VAL O 29 N ASP O 101
SHEET 3 OA 5 GLN O 15 GLU O 21 -1 O GLN O 15 N LYS O 36
SHEET 4 OA 5 LYS O 3 LEU O 8 -1 O ALA O 4 N PHE O 20
SHEET 5 OA 5 GLY O 150 ILE O 151 -1 O GLY O 150 N VAL O 5
SHEET 1 OB 4 ASP O 83 ALA O 89 0
SHEET 2 OB 4 GLY O 41 HIS O 48 -1 O GLY O 41 N ALA O 89
SHEET 3 OB 4 THR O 116 HIS O 120 -1 O THR O 116 N HIS O 48
SHEET 4 OB 4 ARG O 143 VAL O 148 -1 N LEU O 144 O VAL O 119
SHEET 1 PA 9 THR P 2 LYS P 9 0
SHEET 2 PA 9 GLN P 15 GLN P 22 -1 O GLY P 16 N LEU P 8
SHEET 3 PA 9 VAL P 29 LYS P 36 -1 O LYS P 30 N GLU P 21
SHEET 4 PA 9 ALA P 95 ASP P 101 -1 O ALA P 95 N ILE P 35
SHEET 5 PA 9 ASP P 83 ALA P 89 -1 O THR P 88 N ASP P 96
SHEET 6 PA 9 GLY P 41 HIS P 48 -1 O GLY P 41 N ALA P 89
SHEET 7 PA 9 THR P 116 HIS P 120 -1 O THR P 116 N HIS P 48
SHEET 8 PA 9 ARG P 143 ILE P 151 -1 N LEU P 144 O VAL P 119
SHEET 9 PA 9 THR P 2 LYS P 9 -1 O VAL P 5 N GLY P 150
SHEET 1 QA 5 ALA Q 95 ASP Q 101 0
SHEET 2 QA 5 VAL Q 29 LYS Q 36 -1 O VAL Q 29 N ASP Q 101
SHEET 3 QA 5 GLN Q 15 GLU Q 21 -1 O GLN Q 15 N LYS Q 36
SHEET 4 QA 5 LYS Q 3 LEU Q 8 -1 O ALA Q 4 N PHE Q 20
SHEET 5 QA 5 GLY Q 150 ILE Q 151 -1 O GLY Q 150 N VAL Q 5
SHEET 1 QB 4 ASP Q 83 ALA Q 89 0
SHEET 2 QB 4 GLY Q 41 HIS Q 48 -1 O GLY Q 41 N ALA Q 89
SHEET 3 QB 4 THR Q 116 HIS Q 120 -1 O THR Q 116 N HIS Q 48
SHEET 4 QB 4 ARG Q 143 VAL Q 148 -1 N LEU Q 144 O VAL Q 119
SHEET 1 SA 5 ALA S 95 ASP S 101 0
SHEET 2 SA 5 VAL S 29 LYS S 36 -1 O VAL S 29 N ASP S 101
SHEET 3 SA 5 GLN S 15 GLN S 22 -1 O GLN S 15 N LYS S 36
SHEET 4 SA 5 THR S 2 LEU S 8 -1 O THR S 2 N GLN S 22
SHEET 5 SA 5 GLY S 150 ALA S 152 -1 O GLY S 150 N VAL S 5
SHEET 1 SB 4 ASP S 83 ALA S 89 0
SHEET 2 SB 4 GLY S 41 HIS S 48 -1 O GLY S 41 N ALA S 89
SHEET 3 SB 4 THR S 116 HIS S 120 -1 O THR S 116 N HIS S 48
SHEET 4 SB 4 ARG S 143 VAL S 148 -1 N LEU S 144 O VAL S 119
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.13
SSBOND 2 CYS B 57 CYS B 146 1555 1555 2.21
SSBOND 3 CYS C 57 CYS C 146 1555 1555 2.21
SSBOND 4 CYS D 57 CYS D 146 1555 1555 2.16
SSBOND 5 CYS E 57 CYS E 146 1555 1555 2.17
SSBOND 6 CYS F 57 CYS F 146 1555 1555 2.16
SSBOND 7 CYS G 57 CYS G 146 1555 1555 2.12
SSBOND 8 CYS H 57 CYS H 146 1555 1555 2.11
SSBOND 9 CYS I 57 CYS I 146 1555 1555 2.17
SSBOND 10 CYS J 57 CYS J 146 1555 1555 2.17
SSBOND 11 CYS K 57 CYS K 146 1555 1555 2.18
SSBOND 12 CYS L 57 CYS L 146 1555 1555 2.14
SSBOND 13 CYS M 57 CYS M 146 1555 1555 2.15
SSBOND 14 CYS N 57 CYS N 146 1555 1555 2.15
SSBOND 15 CYS O 57 CYS O 146 1555 1555 2.11
SSBOND 16 CYS P 57 CYS P 146 1555 1555 2.04
SSBOND 17 CYS Q 57 CYS Q 146 1555 1555 2.13
SSBOND 18 CYS S 57 CYS S 146 1555 1555 2.06
LINK CU CU A 154 NE2 HIS A 120 1555 1555 2.12
LINK CU CU A 154 ND1 HIS A 46 1555 1555 2.14
LINK CU CU A 154 NE2 HIS A 48 1555 1555 2.13
LINK CU CU A 154 NE2 HIS A 63 1555 1555 2.46
LINK CU CU A 154 O HOH A2047 1555 1555 2.65
LINK ZN ZN A 155 ND1 HIS A 63 1555 1555 2.02
LINK ZN ZN A 155 OD1 ASP A 83 1555 1555 1.90
LINK ZN ZN A 155 ND1 HIS A 71 1555 1555 1.99
LINK ZN ZN A 155 ND1 HIS A 80 1555 1555 2.00
LINK CU CU B 154 NE2 HIS B 120 1555 1555 2.12
LINK CU CU B 154 ND1 HIS B 46 1555 1555 2.12
LINK CU CU B 154 NE2 HIS B 63 1555 1555 2.60
LINK CU CU B 154 O HOH B2083 1555 1555 2.47
LINK CU CU B 154 NE2 HIS B 48 1555 1555 2.11
LINK ZN ZN B 155 ND1 HIS B 71 1555 1555 2.02
LINK ZN ZN B 155 ND1 HIS B 80 1555 1555 2.01
LINK ZN ZN B 155 OD1 ASP B 83 1555 1555 1.94
LINK ZN ZN B 155 ND1 HIS B 63 1555 1555 1.99
LINK CU CU C 154 ND1 HIS C 46 1555 1555 2.13
LINK CU CU C 154 NE2 HIS C 48 1555 1555 2.11
LINK CU CU C 154 NE2 HIS C 120 1555 1555 2.19
LINK CU CU C 154 O HOH C2074 1555 1555 2.52
LINK CU CU C 154 NE2 HIS C 63 1555 1555 2.72
LINK ZN ZN C 155 ND1 HIS C 71 1555 1555 2.05
LINK ZN ZN C 155 ND1 HIS C 63 1555 1555 1.94
LINK ZN ZN C 155 OD1 ASP C 83 1555 1555 1.97
LINK ZN ZN C 155 ND1 HIS C 80 1555 1555 2.08
LINK CA CA C 156 O HOH C2037 1555 1555 2.20
LINK CA CA C 156 O HOH C2106 1555 1555 2.69
LINK CA CA C 156 O HOH C2038 1555 1555 2.43
LINK CA CA C 156 O HOH C2035 1555 1555 2.35
LINK CA CA C 156 O SER C 102 1555 1555 2.49
LINK CA CA C 156 O ASN C 26 1555 1555 2.50
LINK CA CA C 156 OD1 ASN C 26 1555 1555 2.44
LINK CU CU D 154 NE2 HIS D 48 1555 1555 2.07
LINK CU CU D 154 NE2 HIS D 120 1555 1555 2.14
LINK CU CU D 154 NE2 HIS D 63 1555 1555 2.60
LINK CU CU D 154 O HOH D2049 1555 1555 2.70
LINK CU CU D 154 ND1 HIS D 46 1555 1555 2.17
LINK ZN ZN D 155 ND1 HIS D 71 1555 1555 2.06
LINK ZN ZN D 155 ND1 HIS D 80 1555 1555 1.99
LINK ZN ZN D 155 ND1 HIS D 63 1555 1555 2.02
LINK ZN ZN D 155 OD1 ASP D 83 1555 1555 1.89
LINK CA CA D 156 O SER D 102 1555 1555 2.59
LINK CA CA D 156 O HOH D2072 1555 1555 2.34
LINK CA CA D 156 O ASN D 26 1555 1555 2.73
LINK CA CA D 156 OD1 ASN D 26 1555 1555 2.45
LINK CA CA D 156 O HOH D2024 1555 1555 2.43
LINK CA CA D 156 O HOH A2063 1555 1455 2.43
LINK CU CU E 154 O HOH E2052 1555 1555 2.66
LINK CU CU E 154 ND1 HIS E 46 1555 1555 2.15
LINK CU CU E 154 NE2 HIS E 120 1555 1555 2.16
LINK CU CU E 154 NE2 HIS E 63 1555 1555 2.52
LINK CU CU E 154 NE2 HIS E 48 1555 1555 2.10
LINK ZN ZN E 155 ND1 HIS E 71 1555 1555 2.00
LINK ZN ZN E 155 ND1 HIS E 80 1555 1555 2.00
LINK ZN ZN E 155 OD1 ASP E 83 1555 1555 1.95
LINK ZN ZN E 155 ND1 HIS E 63 1555 1555 2.02
LINK CU CU F 154 NE2 HIS F 63 1555 1555 2.51
LINK CU CU F 154 NE2 HIS F 120 1555 1555 2.14
LINK CU CU F 154 NE2 HIS F 48 1555 1555 2.09
LINK CU CU F 154 O HOH F2040 1555 1555 2.72
LINK CU CU F 154 ND1 HIS F 46 1555 1555 2.04
LINK ZN ZN F 155 ND1 HIS F 63 1555 1555 2.02
LINK ZN ZN F 155 ND1 HIS F 71 1555 1555 2.08
LINK ZN ZN F 155 ND1 HIS F 80 1555 1555 1.95
LINK ZN ZN F 155 OD1 ASP F 83 1555 1555 1.93
LINK CU CU G 154 NE2 HIS G 63 1555 1555 2.70
LINK CU CU G 154 NE2 HIS G 48 1555 1555 2.14
LINK CU CU G 154 O HOH G2022 1555 1555 2.01
LINK CU CU G 154 ND1 HIS G 46 1555 1555 2.05
LINK CU CU G 154 NE2 HIS G 120 1555 1555 1.96
LINK CU CU G 154 O HOH G2010 1555 1555 1.96
LINK ZN ZN G 155 OD1 ASP G 83 1555 1555 1.86
LINK ZN ZN G 155 ND1 HIS G 71 1555 1555 2.10
LINK ZN ZN G 155 ND1 HIS G 80 1555 1555 1.95
LINK ZN ZN G 155 ND1 HIS G 63 1555 1555 2.10
LINK ZN ZN G 155 OD2 ASP G 83 1555 1555 2.67
LINK CU CU H 154 ND1 HIS H 46 1555 1555 2.13
LINK CU CU H 154 NE2 HIS H 120 1555 1555 2.11
LINK CU CU H 154 NE2 HIS H 63 1555 1555 2.52
LINK CU CU H 154 NE2 HIS H 48 1555 1555 2.10
LINK CU CU H 154 O HOH H2050 1555 1555 2.74
LINK ZN ZN H 155 OD1 ASP H 83 1555 1555 1.98
LINK ZN ZN H 155 ND1 HIS H 71 1555 1555 2.06
LINK ZN ZN H 155 ND1 HIS H 80 1555 1555 1.86
LINK ZN ZN H 155 ND1 HIS H 63 1555 1555 2.03
LINK CU CU I 154 NE2 HIS I 63 1555 1555 2.67
LINK CU CU I 154 ND1 HIS I 46 1555 1555 2.12
LINK CU CU I 154 NE2 HIS I 120 1555 1555 2.03
LINK CU CU I 154 NE2 HIS I 48 1555 1555 2.11
LINK ZN ZN I 155 ND1 HIS I 80 1555 1555 2.09
LINK ZN ZN I 155 ND1 HIS I 71 1555 1555 2.06
LINK ZN ZN I 155 OD1 ASP I 83 1555 1555 2.01
LINK ZN ZN I 155 ND1 HIS I 63 1555 1555 1.94
LINK CU CU J 154 NE2 HIS J 63 1555 1555 2.61
LINK CU CU J 154 ND1 HIS J 46 1555 1555 2.15
LINK CU CU J 154 NE2 HIS J 48 1555 1555 2.09
LINK CU CU J 154 O HOH J2064 1555 1555 2.63
LINK CU CU J 154 NE2 HIS J 120 1555 1555 2.14
LINK ZN ZN J 155 OD1 ASP J 83 1555 1555 2.01
LINK ZN ZN J 155 ND1 HIS J 63 1555 1555 1.95
LINK ZN ZN J 155 ND1 HIS J 71 1555 1555 2.07
LINK ZN ZN J 155 ND1 HIS J 80 1555 1555 2.00
LINK CU CU K 154 O HOH K2063 1555 1555 2.65
LINK CU CU K 154 NE2 HIS K 120 1555 1555 2.15
LINK CU CU K 154 NE2 HIS K 63 1555 1555 2.48
LINK CU CU K 154 ND1 HIS K 46 1555 1555 2.11
LINK CU CU K 154 NE2 HIS K 48 1555 1555 2.11
LINK ZN ZN K 155 ND1 HIS K 63 1555 1555 1.98
LINK ZN ZN K 155 ND1 HIS K 71 1555 1555 2.12
LINK ZN ZN K 155 ND1 HIS K 80 1555 1555 2.03
LINK ZN ZN K 155 OD1 ASP K 83 1555 1555 1.90
LINK CU CU L 154 NE2 HIS L 48 1555 1555 2.05
LINK CU CU L 154 ND1 HIS L 46 1555 1555 2.09
LINK CU CU L 154 NE2 HIS L 120 1555 1555 2.02
LINK ZN ZN L 155 ND1 HIS L 63 1555 1555 2.00
LINK ZN ZN L 155 ND1 HIS L 71 1555 1555 2.06
LINK ZN ZN L 155 OD1 ASP L 83 1555 1555 1.90
LINK ZN ZN L 155 ND1 HIS L 80 1555 1555 1.98
LINK CU CU M 154 NE2 HIS M 63 1555 1555 2.53
LINK CU CU M 154 ND1 HIS M 46 1555 1555 2.11
LINK CU CU M 154 NE2 HIS M 48 1555 1555 2.11
LINK CU CU M 154 O HOH M2041 1555 1555 2.62
LINK CU CU M 154 NE2 HIS M 120 1555 1555 2.10
LINK ZN ZN M 155 ND1 HIS M 63 1555 1555 1.95
LINK ZN ZN M 155 ND1 HIS M 71 1555 1555 2.06
LINK ZN ZN M 155 ND1 HIS M 80 1555 1555 2.05
LINK ZN ZN M 155 OD1 ASP M 83 1555 1555 1.91
LINK CU CU N 154 O HOH N2038 1555 1555 2.65
LINK CU CU N 154 NE2 HIS N 120 1555 1555 2.04
LINK CU CU N 154 NE2 HIS N 63 1555 1555 2.72
LINK CU CU N 154 NE2 HIS N 48 1555 1555 2.07
LINK CU CU N 154 ND1 HIS N 46 1555 1555 2.12
LINK ZN ZN N 155 ND1 HIS N 71 1555 1555 1.99
LINK ZN ZN N 155 OD1 ASP N 83 1555 1555 2.02
LINK ZN ZN N 155 ND1 HIS N 63 1555 1555 1.96
LINK ZN ZN N 155 ND1 HIS N 80 1555 1555 2.18
LINK CU CU O 154 NE2 HIS O 48 1555 1555 2.18
LINK CU CU O 154 NE2 HIS O 120 1555 1555 2.10
LINK CU CU O 154 ND1 HIS O 46 1555 1555 2.19
LINK CU CU O 154 NE2 HIS O 63 1555 1555 2.60
LINK ZN ZN O 155 OD1 ASP O 83 1555 1555 1.92
LINK ZN ZN O 155 ND1 HIS O 63 1555 1555 2.03
LINK ZN ZN O 155 ND1 HIS O 80 1555 1555 2.19
LINK ZN ZN O 155 ND1 HIS O 71 1555 1555 1.95
LINK CA CA O 156 O SER H 102 1555 1555 2.45
LINK CA CA O 156 O HOH H2085 1555 1555 2.40
LINK CA CA O 156 OD1 ASN H 26 1555 1555 2.61
LINK CA CA O 156 O HOH H2081 1555 1555 2.44
LINK CA CA O 156 O HOH H2084 1555 1555 2.40
LINK CA CA O 156 O ASN H 26 1555 1555 2.69
LINK CU CU P 154 NE2 HIS P 63 1555 1555 2.33
LINK CU CU P 154 NE2 HIS P 120 1555 1555 2.57
LINK CU CU P 154 ND1 HIS P 46 1555 1555 2.07
LINK CU CU P 154 NE2 HIS P 48 1555 1555 2.12
LINK ZN ZN P 155 OD2 ASP P 83 1555 1555 2.72
LINK ZN ZN P 155 OD1 ASP P 83 1555 1555 1.81
LINK ZN ZN P 155 ND1 HIS P 71 1555 1555 2.08
LINK ZN ZN P 155 ND1 HIS P 80 1555 1555 2.18
LINK ZN ZN P 155 ND1 HIS P 63 1555 1555 2.15
LINK CU CU Q 154 NE2 HIS Q 120 1555 1555 2.12
LINK CU CU Q 154 O HOH Q2040 1555 1555 2.74
LINK CU CU Q 154 NE2 HIS Q 63 1555 1555 2.63
LINK CU CU Q 154 ND1 HIS Q 46 1555 1555 2.08
LINK CU CU Q 154 NE2 HIS Q 48 1555 1555 2.06
LINK ZN ZN Q 155 ND1 HIS Q 63 1555 1555 1.92
LINK ZN ZN Q 155 OD1 ASP Q 83 1555 1555 1.93
LINK ZN ZN Q 155 ND1 HIS Q 80 1555 1555 2.08
LINK ZN ZN Q 155 ND1 HIS Q 71 1555 1555 2.03
LINK CU CU S 154 NE2 HIS S 63 1555 1555 2.52
LINK CU CU S 154 ND1 HIS S 46 1555 1555 2.18
LINK CU CU S 154 NE2 HIS S 48 1555 1555 2.02
LINK CU CU S 154 NE2 HIS S 120 1555 1555 2.20
LINK ZN ZN S 155 ND1 HIS S 80 1555 1555 2.05
LINK ZN ZN S 155 OD1 ASP S 83 1555 1555 2.00
LINK ZN ZN S 155 ND1 HIS S 71 1555 1555 2.11
LINK ZN ZN S 155 ND1 HIS S 63 1555 1555 2.10
SITE 1 AC1 5 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 2 AC1 5 HOH A2047
SITE 1 AC2 5 HIS A 63 HIS A 71 HIS A 80 ASP A 83
SITE 2 AC2 5 LYS A 136
SITE 1 AC3 5 HIS B 46 HIS B 48 HIS B 63 HIS B 120
SITE 2 AC3 5 HOH B2083
SITE 1 AC4 4 HIS B 63 HIS B 71 HIS B 80 ASP B 83
SITE 1 AC5 5 HIS C 46 HIS C 48 HIS C 63 HIS C 120
SITE 2 AC5 5 HOH C2074
SITE 1 AC6 4 HIS C 63 HIS C 71 HIS C 80 ASP C 83
SITE 1 AC7 6 ASN C 26 SER C 102 HOH C2035 HOH C2037
SITE 2 AC7 6 HOH C2038 HOH C2106
SITE 1 AC8 5 HIS D 46 HIS D 48 HIS D 63 HIS D 120
SITE 2 AC8 5 HOH D2049
SITE 1 AC9 4 HIS D 63 HIS D 71 HIS D 80 ASP D 83
SITE 1 BC1 5 HOH A2063 ASN D 26 SER D 102 HOH D2024
SITE 2 BC1 5 HOH D2072
SITE 1 BC2 5 HIS E 46 HIS E 48 HIS E 63 HIS E 120
SITE 2 BC2 5 HOH E2052
SITE 1 BC3 4 HIS E 63 HIS E 71 HIS E 80 ASP E 83
SITE 1 BC4 5 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 2 BC4 5 HOH F2040
SITE 1 BC5 4 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 1 BC6 6 HIS G 46 HIS G 48 HIS G 63 HIS G 120
SITE 2 BC6 6 HOH G2010 HOH G2022
SITE 1 BC7 5 HIS G 63 HIS G 71 HIS G 80 ASP G 83
SITE 2 BC7 5 LYS G 136
SITE 1 BC8 5 HIS H 46 HIS H 48 HIS H 63 HIS H 120
SITE 2 BC8 5 HOH H2050
SITE 1 BC9 4 HIS H 63 HIS H 71 HIS H 80 ASP H 83
SITE 1 CC1 5 HIS I 46 HIS I 48 HIS I 63 HIS I 120
SITE 2 CC1 5 HOH I2069
SITE 1 CC2 4 HIS I 63 HIS I 71 HIS I 80 ASP I 83
SITE 1 CC3 5 HIS J 46 HIS J 48 HIS J 63 HIS J 120
SITE 2 CC3 5 HOH J2064
SITE 1 CC4 4 HIS J 63 HIS J 71 HIS J 80 ASP J 83
SITE 1 CC5 5 HIS K 46 HIS K 48 HIS K 63 HIS K 120
SITE 2 CC5 5 HOH K2063
SITE 1 CC6 5 HIS K 63 HIS K 71 HIS K 80 ASP K 83
SITE 2 CC6 5 LYS K 136
SITE 1 CC7 4 HIS L 46 HIS L 48 HIS L 63 HIS L 120
SITE 1 CC8 4 HIS L 63 HIS L 71 HIS L 80 ASP L 83
SITE 1 CC9 5 HIS M 46 HIS M 48 HIS M 63 HIS M 120
SITE 2 CC9 5 HOH M2041
SITE 1 DC1 5 HIS M 63 HIS M 71 HIS M 80 ASP M 83
SITE 2 DC1 5 LYS M 136
SITE 1 DC2 5 HIS N 46 HIS N 48 HIS N 63 HIS N 120
SITE 2 DC2 5 HOH N2038
SITE 1 DC3 4 HIS N 63 HIS N 71 HIS N 80 ASP N 83
SITE 1 DC4 4 HIS O 46 HIS O 48 HIS O 63 HIS O 120
SITE 1 DC5 5 HIS O 63 HIS O 71 HIS O 80 ASP O 83
SITE 2 DC5 5 LYS O 136
SITE 1 DC6 5 ASN H 26 SER H 102 HOH H2081 HOH H2084
SITE 2 DC6 5 HOH H2085
SITE 1 DC7 4 HIS P 46 HIS P 48 HIS P 63 HIS P 120
SITE 1 DC8 4 HIS P 63 HIS P 71 HIS P 80 ASP P 83
SITE 1 DC9 5 HIS Q 46 HIS Q 48 HIS Q 63 HIS Q 120
SITE 2 DC9 5 HOH Q2040
SITE 1 EC1 4 HIS Q 63 HIS Q 71 HIS Q 80 ASP Q 83
SITE 1 EC2 4 HIS S 46 HIS S 48 HIS S 63 HIS S 120
SITE 1 EC3 4 HIS S 63 HIS S 71 HIS S 80 ASP S 83
CRYST1 76.871 172.380 112.450 90.00 93.45 90.00 P 1 21 1 36
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 0.013009 0.000000 0.000784 0.00000
SCALE2 0.000000 0.005801 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008909 0.00000
MTRIX1 1 0.895050 -0.368850 0.250680 3.40235 1
MTRIX2 1 -0.372240 -0.927450 -0.035590 183.62323 1
MTRIX3 1 0.245620 -0.061460 -0.967420 171.62170 1
MTRIX1 2 -0.986350 0.057530 -0.154280 41.97392 1
MTRIX2 2 -0.057730 -0.998330 -0.003230 173.66074 1
MTRIX3 2 -0.154210 0.005720 0.988020 59.29191 1
MTRIX1 3 -0.915130 0.389020 0.105830 4.91064 1
MTRIX2 3 0.392310 0.919760 0.011510 4.10431 1
MTRIX3 3 -0.092860 0.052050 -0.994320 115.60555 1
MTRIX1 4 0.956450 -0.194120 -0.218000 23.65226 1
MTRIX2 4 -0.084730 0.530050 -0.843720 71.57378 1
MTRIX3 4 0.279340 0.825450 0.490520 -10.01044 1
MTRIX1 5 0.957930 -0.190040 0.215050 8.83297 1
MTRIX2 5 -0.280800 -0.465950 0.839070 110.49805 1
MTRIX3 5 -0.059250 -0.864160 -0.499710 183.51767 1
MTRIX1 6 -0.925350 0.224510 -0.305480 46.64627 1
MTRIX2 6 0.146330 -0.531820 -0.834120 204.50653 1
MTRIX3 6 -0.349720 -0.816560 0.459270 120.70108 1
MTRIX1 7 -0.964170 0.227780 0.135960 8.10633 1
MTRIX2 7 0.228470 0.452630 0.861930 -27.88937 1
MTRIX3 7 0.134790 0.862120 -0.488450 56.90441 1
MTRIX1 8 0.911560 -0.356640 -0.204620 53.72966 1
MTRIX2 8 -0.350000 -0.411870 -0.841350 211.35992 1
MTRIX3 8 0.215780 0.838550 -0.500260 -2.85196 1
MTRIX1 9 0.999010 0.029030 -0.033620 -13.08864 1
MTRIX2 9 0.015690 0.477480 0.878500 -33.34248 1
MTRIX3 9 0.041560 -0.878160 0.476560 175.54706 1
MTRIX1 10 0.977310 -0.039520 0.208080 22.31427 1
MTRIX2 10 0.163110 -0.486220 -0.858480 242.66022 1
MTRIX3 10 0.135100 0.872940 -0.468740 31.64304 1
MTRIX1 11 0.862630 0.368500 0.346530 -44.52737 1
MTRIX2 11 -0.487130 0.420620 0.765360 -52.29001 1
MTRIX3 11 0.136280 -0.829030 0.542350 133.84116 1
MTRIX1 12 -0.932870 0.360180 0.005670 1.61367 1
MTRIX2 12 0.191420 0.508970 -0.839230 66.00793 1
MTRIX3 12 -0.305160 -0.781810 -0.543740 231.29517 1
MTRIX1 13 -0.983110 -0.024850 0.181300 43.37927 1
MTRIX2 13 0.163560 -0.563660 0.809650 111.04368 1
MTRIX3 13 0.082070 0.825630 0.558210 -56.49068 1
MTRIX1 14 -0.915630 -0.365090 -0.168290 137.16948 1
MTRIX2 14 0.054550 -0.527580 0.847750 60.40010 1
MTRIX3 14 -0.398290 0.767050 0.502990 -44.98087 1
MTRIX1 15 -0.950280 0.006510 -0.311320 107.06050 1
MTRIX2 15 0.257450 0.578810 -0.773760 86.02035 1
MTRIX3 15 0.175150 -0.815440 -0.551710 243.48880 1
MTRIX1 16 0.539870 0.661280 0.520810 -87.03172 1
MTRIX2 16 -0.544850 -0.197090 0.815040 116.28680 1
MTRIX3 16 0.641620 -0.723780 0.253890 146.14423 1
MTRIX1 17 0.844560 0.480970 0.235360 -70.59261 1
MTRIX2 17 0.284100 -0.029920 -0.958330 101.88297 1
MTRIX3 17 -0.453880 0.876230 -0.161910 1.33548 1
(ATOM LINES ARE NOT SHOWN.)
END
