HEADER OXIDOREDUCTASE 26-FEB-04 1UXM
TITLE A4V MUTANT OF HUMAN SOD1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT, METAL- BINDING,
KEYWDS 2 AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.HOUGH,J.G.GROSSMANN,S.V.ANTONYUK,R.W.STRANGE,P.A.DOUCETTE,
AUTHOR 2 J.A.RODRIGUEZ,L.J.WHITSON,P.J.HART,L.J.HAYWARD,J.S.VALENTINE,
AUTHOR 3 S.S.HASNAIN
REVDAT 5 13-DEC-23 1UXM 1 REMARK LINK
REVDAT 4 13-JUL-11 1UXM 1 VERSN
REVDAT 3 24-FEB-09 1UXM 1 VERSN
REVDAT 2 05-JAN-05 1UXM 1 JRNL
REVDAT 1 19-MAR-04 1UXM 0
JRNL AUTH M.A.HOUGH,J.G.GROSSMANN,S.V.ANTONYUK,R.W.STRANGE,
JRNL AUTH 2 P.A.DOUCETTE,J.A.RODRIGUEZ,L.J.WHITSON,P.J.HART,L.J.HAYWARD,
JRNL AUTH 3 J.S.VALENTINE,S.S.HASNAIN
JRNL TITL DIMER DESTABILIZATION IN SUPEROXIDE DISMUTASE MAY RESULT IN
JRNL TITL 2 DISEASE-CAUSING PROPERTIES: STRUCTURES OF MOTOR NEURON
JRNL TITL 3 DISEASE MUTANTS
JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 5976 2004
JRNL REFN ISSN 0027-8424
JRNL PMID 15056757
JRNL DOI 10.1073/PNAS.0305143101
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 225403
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) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11944
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13965
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 734
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13344
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 1096
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) : 18.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.40000
REMARK 3 B22 (A**2) : 3.24000
REMARK 3 B33 (A**2) : -2.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.35000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.132
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.366
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13572 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18312 ; 1.786 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1824 ; 4.792 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2331 ;20.379 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2028 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10344 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7656 ; 0.319 ; 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): 2194 ; 0.242 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 42 ; 0.130 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 129 ; 0.402 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 44 ; 0.355 ; 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): 8940 ; 0.902 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14220 ; 1.556 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4632 ; 2.637 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4092 ; 4.200 ; 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 : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 153
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0420 -29.1190 -1.8830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1352 T22: 0.0571
REMARK 3 T33: 0.1357 T12: 0.0089
REMARK 3 T13: -0.0208 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 2.6422 L22: 0.8793
REMARK 3 L33: 1.2272 L12: -0.1822
REMARK 3 L13: 0.4856 L23: -0.1071
REMARK 3 S TENSOR
REMARK 3 S11: 0.0486 S12: 0.1913 S13: 0.0020
REMARK 3 S21: -0.0367 S22: -0.0173 S23: 0.0139
REMARK 3 S31: -0.0323 S32: -0.0286 S33: -0.0313
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): 23.9950 -29.3360 12.3570
REMARK 3 T TENSOR
REMARK 3 T11: 0.1540 T22: 0.0484
REMARK 3 T33: 0.1429 T12: 0.0006
REMARK 3 T13: -0.0275 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 2.2851 L22: 0.6703
REMARK 3 L33: 1.6410 L12: 0.1182
REMARK 3 L13: 0.9340 L23: -0.0840
REMARK 3 S TENSOR
REMARK 3 S11: -0.0469 S12: 0.1456 S13: 0.0559
REMARK 3 S21: 0.0832 S22: -0.0072 S23: 0.0002
REMARK 3 S31: -0.0972 S32: 0.1248 S33: 0.0541
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): 3.9560 -67.4660 4.1650
REMARK 3 T TENSOR
REMARK 3 T11: 0.1523 T22: 0.0268
REMARK 3 T33: 0.1345 T12: -0.0207
REMARK 3 T13: -0.0187 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.9315 L22: 0.7242
REMARK 3 L33: 1.4761 L12: 0.1384
REMARK 3 L13: 0.8463 L23: 0.0849
REMARK 3 S TENSOR
REMARK 3 S11: -0.0433 S12: 0.0414 S13: -0.0082
REMARK 3 S21: 0.0183 S22: 0.0245 S23: 0.0547
REMARK 3 S31: 0.0119 S32: -0.0101 S33: 0.0188
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): 28.2270 -67.0530 17.8000
REMARK 3 T TENSOR
REMARK 3 T11: 0.1394 T22: 0.0314
REMARK 3 T33: 0.1471 T12: 0.0022
REMARK 3 T13: -0.0134 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 2.6553 L22: 0.6276
REMARK 3 L33: 1.4533 L12: -0.0933
REMARK 3 L13: 0.6461 L23: 0.0209
REMARK 3 S TENSOR
REMARK 3 S11: -0.0354 S12: -0.0810 S13: -0.1196
REMARK 3 S21: -0.0238 S22: 0.0123 S23: -0.0718
REMARK 3 S31: 0.0203 S32: 0.0274 S33: 0.0232
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): 11.9530 4.9340 51.6450
REMARK 3 T TENSOR
REMARK 3 T11: 0.1563 T22: 0.1779
REMARK 3 T33: 0.1118 T12: -0.0096
REMARK 3 T13: -0.0159 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.4518 L22: 0.6762
REMARK 3 L33: 6.4102 L12: -0.1045
REMARK 3 L13: 0.2928 L23: -0.1270
REMARK 3 S TENSOR
REMARK 3 S11: 0.0619 S12: -0.1033 S13: -0.0946
REMARK 3 S21: 0.0118 S22: 0.0238 S23: -0.0477
REMARK 3 S31: -0.0218 S32: -0.1830 S33: -0.0857
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 153
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6280 4.6980 23.7830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1590 T22: 0.1240
REMARK 3 T33: 0.1123 T12: 0.0235
REMARK 3 T13: -0.0250 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 1.5595 L22: 0.3623
REMARK 3 L33: 10.7670 L12: -0.2433
REMARK 3 L13: 1.3867 L23: -0.2241
REMARK 3 S TENSOR
REMARK 3 S11: 0.1365 S12: 0.0930 S13: -0.0444
REMARK 3 S21: -0.0130 S22: -0.0199 S23: 0.0792
REMARK 3 S31: 0.0595 S32: 0.3076 S33: -0.1166
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): 28.1950 5.0700 -3.8850
REMARK 3 T TENSOR
REMARK 3 T11: 0.1689 T22: 0.2797
REMARK 3 T33: 0.1624 T12: 0.0347
REMARK 3 T13: 0.0197 T23: 0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 4.8687 L22: 0.9088
REMARK 3 L33: 1.8924 L12: 0.3960
REMARK 3 L13: -1.0954 L23: -0.3765
REMARK 3 S TENSOR
REMARK 3 S11: -0.1190 S12: -0.3729 S13: 0.0238
REMARK 3 S21: -0.0051 S22: 0.0136 S23: -0.0836
REMARK 3 S31: 0.1409 S32: 0.3979 S33: 0.1054
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 153
REMARK 3 ORIGIN FOR THE GROUP (A): 52.2150 5.7530 -18.1260
REMARK 3 T TENSOR
REMARK 3 T11: 0.1721 T22: 0.3176
REMARK 3 T33: 0.2275 T12: -0.0194
REMARK 3 T13: 0.0215 T23: 0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 7.0243 L22: -0.2740
REMARK 3 L33: 1.3593 L12: 0.5342
REMARK 3 L13: -0.7296 L23: 0.0810
REMARK 3 S TENSOR
REMARK 3 S11: -0.0699 S12: 0.4753 S13: -0.1156
REMARK 3 S21: 0.0270 S22: 0.0512 S23: -0.0854
REMARK 3 S31: 0.0249 S32: -0.1289 S33: 0.0187
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 153
REMARK 3 ORIGIN FOR THE GROUP (A): 56.3230 44.4450 -12.2030
REMARK 3 T TENSOR
REMARK 3 T11: 0.0910 T22: 0.3930
REMARK 3 T33: 0.1674 T12: -0.0054
REMARK 3 T13: 0.0082 T23: -0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 6.4516 L22: 0.6680
REMARK 3 L33: 2.4921 L12: 0.4821
REMARK 3 L13: -0.9662 L23: -0.1770
REMARK 3 S TENSOR
REMARK 3 S11: -0.1469 S12: 0.8672 S13: 0.0212
REMARK 3 S21: 0.0482 S22: 0.1092 S23: -0.0436
REMARK 3 S31: -0.0167 S32: -0.0035 S33: 0.0377
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 153
REMARK 3 ORIGIN FOR THE GROUP (A): 32.0080 44.2900 1.5150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0953 T22: 0.2355
REMARK 3 T33: 0.1634 T12: 0.0138
REMARK 3 T13: -0.0068 T23: -0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 7.4031 L22: 0.3809
REMARK 3 L33: 2.1133 L12: 0.2749
REMARK 3 L13: -0.3944 L23: -0.0468
REMARK 3 S TENSOR
REMARK 3 S11: -0.0055 S12: -0.2589 S13: 0.2263
REMARK 3 S21: -0.0684 S22: -0.0234 S23: 0.0215
REMARK 3 S31: 0.0397 S32: -0.1138 S33: 0.0289
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 1 K 153
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8990 43.0440 57.4740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1922 T22: 0.4020
REMARK 3 T33: 0.1407 T12: 0.0125
REMARK 3 T13: -0.0264 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 1.0991 L22: 0.5256
REMARK 3 L33: 13.3599 L12: -0.3720
REMARK 3 L13: 1.9363 L23: -1.1642
REMARK 3 S TENSOR
REMARK 3 S11: -0.0522 S12: -0.1596 S13: 0.0204
REMARK 3 S21: 0.0534 S22: 0.1924 S23: 0.0043
REMARK 3 S31: -0.1363 S32: -1.6750 S33: -0.1402
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 153
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3350 43.6770 29.6130
REMARK 3 T TENSOR
REMARK 3 T11: 0.1646 T22: 0.3025
REMARK 3 T33: 0.1354 T12: -0.0295
REMARK 3 T13: -0.0203 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 1.6275 L22: 0.5399
REMARK 3 L33: 6.5942 L12: -0.2185
REMARK 3 L13: 2.6414 L23: -0.6139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0699 S12: -0.0880 S13: -0.0309
REMARK 3 S21: 0.0794 S22: 0.0065 S23: -0.0874
REMARK 3 S31: -0.0135 S32: -0.4014 S33: -0.0765
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. THIS ENTRY CONTAINS SOME ATOMS THAT HAVE BEEN REFINED
REMARK 3 WITH AN OCCUPANCY OF 0.00
REMARK 4
REMARK 4 1UXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1290014650.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
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 : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 246133
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 1HL5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CA ACET, 15% PEG 2000, 0.1 M
REMARK 280 TRIS PH 8.0, PH 6.00
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 72.79100
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
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, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
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: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 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: E, F
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 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: I, 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
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: 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 400
REMARK 400 COMPOUND
REMARK 400 DESTROYS RADICALS WHICH ARE NORMALLY PRODUCED WITHIN THE
REMARK 400 CELLS AND WHICH ARE TOXIC TO BIOLOGICAL SYSTEMS.
REMARK 400
REMARK 400 ENGINEERED MUTATION ALA 4 TO VAL 4 IN CHAINS A TO L
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 LEU K 38
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 ALA A 1 N CA CB
REMARK 480 ASN A 26 ND2
REMARK 480 LYS A 30 CD CE NZ
REMARK 480 LYS A 128 NZ
REMARK 480 LYS B 122 NZ
REMARK 480 LYS C 75 CE NZ
REMARK 480 LYS C 122 CE NZ
REMARK 480 ALA E 1 N CA CB
REMARK 480 LYS E 23 CE NZ
REMARK 480 LYS E 70 CG CD CE NZ
REMARK 480 ALA F 1 CA CB
REMARK 480 LYS F 9 CD CE NZ
REMARK 480 LYS F 23 CE NZ
REMARK 480 LYS F 70 CE NZ
REMARK 480 LYS F 91 CD CE NZ
REMARK 480 GLU F 132 CD OE1 OE2
REMARK 480 GLN G 15 CD OE1 NE2
REMARK 480 LYS G 23 CE NZ
REMARK 480 ASN G 26 CG OD1 ND2
REMARK 480 LYS G 30 CD CE NZ
REMARK 480 LYS G 75 CD CE NZ
REMARK 480 LYS G 91 CD CE NZ
REMARK 480 GLN G 153 CG CD OE1 NE2
REMARK 480 ALA H 1 N CA CB
REMARK 480 LYS H 3 CE NZ
REMARK 480 LYS H 9 CE NZ
REMARK 480 VAL H 14 CG1 CG2
REMARK 480 GLN H 22 CB CG CD OE1 NE2
REMARK 480 LYS H 23 O CE NZ
REMARK 480 GLU H 24 CD OE1 OE2
REMARK 480 SER H 25 O
REMARK 480 LYS H 30 CG CD CE NZ
REMARK 480 LYS H 36 CG CD CE NZ
REMARK 480 LYS H 70 CG CD CE NZ
REMARK 480 LYS H 75 CD CE NZ
REMARK 480 GLU H 77 CB CG CD OE1 OE2
REMARK 480 LYS H 91 CB CG CD CE NZ
REMARK 480 VAL H 94 CG2
REMARK 480 GLU H 100 CG CD OE1 OE2
REMARK 480 SER H 107 CB OG
REMARK 480 HIS H 110 CB CG ND1 CD2 CE1 NE2
REMARK 480 THR H 135 CG2
REMARK 480 ALA I 1 N CA CB
REMARK 480 LYS I 3 CE NZ
REMARK 480 LYS I 23 CE NZ
REMARK 480 GLU I 24 CG CD OE1 OE2
REMARK 480 SER I 25 O
REMARK 480 ASN I 26 OD1 ND2
REMARK 480 LYS I 70 CD CE NZ
REMARK 480 LYS I 75 CD CE NZ
REMARK 480 LYS I 91 CE NZ
REMARK 480 LYS I 122 CE NZ
REMARK 480 GLU I 132 CB CG CD OE1 OE2
REMARK 480 ALA J 1 N CA CB
REMARK 480 LYS J 3 CG CD CE NZ
REMARK 480 LYS J 23 CD CE NZ
REMARK 480 ASN J 26 OD1 ND2
REMARK 480 LYS J 36 CD CE NZ
REMARK 480 LYS J 70 CD CE NZ
REMARK 480 LYS J 91 CG CD CE NZ
REMARK 480 ALA K 1 N CA CB
REMARK 480 THR K 2 CB OG1 CG2
REMARK 480 LYS K 3 CE NZ
REMARK 480 LYS K 9 CG CD CE NZ
REMARK 480 GLN K 15 CG CD OE1 NE2
REMARK 480 GLU K 24 CG CD OE1 OE2
REMARK 480 SER K 25 O
REMARK 480 ASN K 26 CG OD1 ND2
REMARK 480 LYS K 30 CD CE NZ
REMARK 480 LYS K 36 CB CG CD CE NZ
REMARK 480 THR K 39 N
REMARK 480 GLU K 40 CG CD OE1 OE2
REMARK 480 LYS K 75 CE NZ
REMARK 480 GLU K 77 CG CD OE1 OE2
REMARK 480 LYS K 91 CB CG CD CE NZ
REMARK 480 ASP K 92 O CG OD1 OD2
REMARK 480 VAL K 94 CG1 CG2
REMARK 480 SER K 98 CB OG
REMARK 480 SER K 102 OG
REMARK 480 LYS K 122 CE NZ
REMARK 480 ALA L 1 N CA CB
REMARK 480 LYS L 3 CD CE NZ
REMARK 480 ASP L 11 OD1 OD2
REMARK 480 LYS L 23 CD CE NZ
REMARK 480 SER L 25 OG
REMARK 480 LYS L 91 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 O HOH J 2014 O HOH J 2036 1.77
REMARK 500 OD1 ASP B 96 O HOH B 2089 2.01
REMARK 500 O HOH B 2023 O HOH F 2048 2.04
REMARK 500 O GLU I 132 CG2 THR I 135 2.06
REMARK 500 O SER H 25 N GLY H 27 2.06
REMARK 500 OD1 ASP K 90 N ASP K 92 2.07
REMARK 500 SG CYS G 6 O HOH G 2076 2.10
REMARK 500 OE1 GLN G 153 O HOH G 2078 2.11
REMARK 500 NE2 HIS I 120 O HOH I 2031 2.11
REMARK 500 NE ARG K 69 O HOH K 2026 2.11
REMARK 500 O ASN G 86 O HOH G 2039 2.13
REMARK 500 O CYS G 111 O HOH G 2054 2.14
REMARK 500 O HOH I 2020 O HOH I 2021 2.15
REMARK 500 O HOH A 2064 O HOH A 2072 2.15
REMARK 500 N GLN K 153 O HOH K 2072 2.15
REMARK 500 OG SER G 105 O SER G 107 2.15
REMARK 500 OD1 ASP A 96 O HOH A 2083 2.16
REMARK 500 O HOH G 2015 O HOH G 2035 2.17
REMARK 500 O HOH K 2063 O HOH K 2064 2.19
REMARK 500 O GLU F 132 OG1 THR F 135 2.19
REMARK 500 O GLN A 153 O HOH A 2135 2.19
REMARK 500 N ASP J 11 O HOH J 2003 2.19
REMARK 500 O GLU L 100 O HOH L 2038 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 ND2 ASN D 26 NH2 ARG J 69 1545 1.95
REMARK 500 CG ASN D 26 NE ARG J 69 1545 2.03
REMARK 500 OE2 GLU A 77 N ASP C 109 2555 2.04
REMARK 500 OE1 GLU H 40 NZ LYS K 91 1554 2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASN J 53 CB ASN J 53 CG 0.141
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 THR A 2 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 GLY A 27 C - N - CA ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG A 79 CD - NE - CZ ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP A 101 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 11 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG B 79 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 79 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP B 101 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG C 79 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG C 79 NE - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP D 96 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG D 143 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG E 79 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG E 79 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG F 79 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG F 79 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP G 101 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 VAL H 87 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 ASP I 101 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP I 124 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP J 83 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP K 90 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP L 11 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP L 101 CB - CG - OD2 ANGL. DEV. = 5.5 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 THR A 2 -51.97 -127.00
REMARK 500 ASN A 26 -102.80 -3.48
REMARK 500 ASN A 65 63.95 -150.79
REMARK 500 THR B 2 -53.78 -125.57
REMARK 500 ASN B 26 -46.23 177.05
REMARK 500 ASN C 26 19.01 50.96
REMARK 500 ASN D 26 -23.03 82.24
REMARK 500 ARG D 115 -167.07 -103.04
REMARK 500 SER E 25 90.63 -65.68
REMARK 500 ASN E 26 -34.74 135.11
REMARK 500 THR F 2 -53.66 -137.95
REMARK 500 ASN F 26 -1.35 69.38
REMARK 500 ALA F 55 51.08 -117.45
REMARK 500 SER F 68 72.10 46.02
REMARK 500 ASP F 90 -176.14 -68.22
REMARK 500 ARG F 115 -168.74 -102.61
REMARK 500 PRO G 13 -71.51 -42.14
REMARK 500 SER G 68 76.77 43.63
REMARK 500 GLU G 77 -70.22 -60.90
REMARK 500 GLU G 78 89.09 -67.66
REMARK 500 SER G 98 114.71 -164.85
REMARK 500 ARG G 115 -161.49 -106.75
REMARK 500 THR H 2 -67.77 -107.34
REMARK 500 LYS H 23 -23.56 -32.80
REMARK 500 SER H 25 177.34 -51.89
REMARK 500 ASN H 26 -22.20 44.34
REMARK 500 ASP H 90 -166.27 -79.83
REMARK 500 CYS H 111 131.74 -36.71
REMARK 500 ASN I 26 43.22 -86.11
REMARK 500 SER I 98 106.99 -160.33
REMARK 500 LEU I 126 19.67 54.33
REMARK 500 THR J 2 -48.46 -142.09
REMARK 500 SER J 98 104.46 -162.62
REMARK 500 ASN K 26 41.06 -104.69
REMARK 500 PHE K 64 108.63 -59.73
REMARK 500 ASP L 11 11.03 -68.93
REMARK 500 SER L 98 106.41 -164.45
REMARK 500 HIS L 110 33.30 -94.98
REMARK 500 ARG L 115 -161.06 -101.72
REMARK 500 SER L 142 151.83 -41.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH L2019 DISTANCE = 6.13 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A 154 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 46 ND1
REMARK 620 2 HIS A 48 NE2 129.1
REMARK 620 3 HIS A 63 NE2 81.6 99.7
REMARK 620 4 HIS A 120 NE2 95.5 106.8 147.4
REMARK 620 5 HOH A2060 O 117.7 107.6 63.7 90.0
REMARK 620 N 1 2 3 4
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 HIS A 71 ND1 106.7
REMARK 620 3 HIS A 80 ND1 114.8 121.9
REMARK 620 4 ASP A 83 OD1 103.9 99.6 107.4
REMARK 620 N 1 2 3
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 48 NE2 131.4
REMARK 620 3 HIS B 63 NE2 80.6 98.7
REMARK 620 4 HIS B 120 NE2 95.7 106.6 148.6
REMARK 620 5 HOH B2062 O 122.6 104.0 76.7 79.4
REMARK 620 N 1 2 3 4
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 63 ND1
REMARK 620 2 HIS B 71 ND1 109.5
REMARK 620 3 HIS B 80 ND1 113.5 124.2
REMARK 620 4 ASP B 83 OD1 106.0 89.9 109.8
REMARK 620 N 1 2 3
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 132.7
REMARK 620 3 HIS C 63 NE2 83.4 96.5
REMARK 620 4 HIS C 120 NE2 95.9 105.5 150.0
REMARK 620 5 HOH C2063 O 129.6 94.7 73.6 84.3
REMARK 620 N 1 2 3 4
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 63 ND1
REMARK 620 2 HIS C 71 ND1 109.1
REMARK 620 3 HIS C 80 ND1 111.9 121.9
REMARK 620 4 ASP C 83 OD1 104.1 95.7 111.7
REMARK 620 N 1 2 3
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 46 ND1
REMARK 620 2 HIS D 48 NE2 130.5
REMARK 620 3 HIS D 63 NE2 80.4 97.8
REMARK 620 4 HIS D 120 NE2 94.0 107.6 150.2
REMARK 620 5 HOH D2063 O 124.6 102.1 75.8 83.8
REMARK 620 N 1 2 3 4
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 63 ND1
REMARK 620 2 HIS D 71 ND1 108.9
REMARK 620 3 HIS D 80 ND1 113.4 121.7
REMARK 620 4 ASP D 83 OD1 102.0 98.0 110.2
REMARK 620 N 1 2 3
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 HIS E 46 ND1
REMARK 620 2 HIS E 48 NE2 132.7
REMARK 620 3 HIS E 63 NE2 81.4 99.1
REMARK 620 4 HIS E 120 NE2 90.8 104.3 154.0
REMARK 620 5 HOH E2032 O 126.8 98.0 74.9 90.6
REMARK 620 N 1 2 3 4
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 63 ND1
REMARK 620 2 HIS E 71 ND1 103.9
REMARK 620 3 HIS E 80 ND1 113.1 124.3
REMARK 620 4 ASP E 83 OD1 104.7 100.5 108.2
REMARK 620 N 1 2 3
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 HIS F 46 ND1
REMARK 620 2 HIS F 48 NE2 127.4
REMARK 620 3 HIS F 63 NE2 82.0 94.7
REMARK 620 4 HIS F 120 NE2 89.9 112.3 150.7
REMARK 620 5 HOH F2018 O 126.6 101.4 72.8 90.2
REMARK 620 N 1 2 3 4
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 107.7
REMARK 620 3 HIS F 80 ND1 109.1 127.0
REMARK 620 4 ASP F 83 OD1 115.5 92.5 104.4
REMARK 620 N 1 2 3
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 46 ND1
REMARK 620 2 HIS G 48 NE2 131.1
REMARK 620 3 HIS G 63 NE2 81.3 100.0
REMARK 620 4 HIS G 120 NE2 92.5 104.7 151.8
REMARK 620 5 HOH G2030 O 126.6 99.8 73.9 88.5
REMARK 620 N 1 2 3 4
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 71 ND1 109.8
REMARK 620 3 HIS G 80 ND1 111.0 124.0
REMARK 620 4 ASP G 83 OD1 98.8 96.8 112.8
REMARK 620 N 1 2 3
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 48 NE2 130.4
REMARK 620 3 HIS H 63 NE2 85.4 93.3
REMARK 620 4 HIS H 120 NE2 100.5 101.5 154.0
REMARK 620 5 HOH H2065 O 137.2 90.5 79.1 79.6
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 71 ND1 105.7
REMARK 620 3 HIS H 80 ND1 118.4 117.6
REMARK 620 4 ASP H 83 OD1 114.0 96.8 102.3
REMARK 620 N 1 2 3
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 134.4
REMARK 620 3 HIS I 63 NE2 100.4 102.7
REMARK 620 4 HIS I 120 NE2 88.4 100.4 137.0
REMARK 620 5 HOH I2031 O 127.4 93.1 86.1 56.7
REMARK 620 N 1 2 3 4
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 63 ND1
REMARK 620 2 HIS I 71 ND1 98.6
REMARK 620 3 HIS I 80 ND1 115.1 125.0
REMARK 620 4 ASP I 83 OD1 115.7 107.9 95.4
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 46 ND1
REMARK 620 2 HIS J 48 NE2 129.6
REMARK 620 3 HIS J 63 NE2 81.5 96.1
REMARK 620 4 HIS J 120 NE2 96.4 108.1 149.4
REMARK 620 5 HOH J2030 O 128.8 98.5 76.4 81.6
REMARK 620 N 1 2 3 4
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 102.6
REMARK 620 3 HIS J 80 ND1 118.4 130.8
REMARK 620 4 ASP J 83 OD2 152.1 72.2 81.9
REMARK 620 5 ASP J 83 OD1 111.2 108.7 81.9 49.3
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 46 ND1
REMARK 620 2 HIS K 48 NE2 131.3
REMARK 620 3 HIS K 63 NE2 80.3 99.3
REMARK 620 4 HIS K 120 NE2 92.1 104.6 153.6
REMARK 620 5 HOH K2021 O 125.5 102.0 80.4 83.7
REMARK 620 N 1 2 3 4
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 109.1
REMARK 620 3 HIS K 80 ND1 112.8 121.8
REMARK 620 4 ASP K 83 OD1 109.2 94.0 108.0
REMARK 620 N 1 2 3
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 46 ND1
REMARK 620 2 HIS L 48 NE2 137.3
REMARK 620 3 HIS L 63 NE2 87.7 101.7
REMARK 620 4 HIS L 120 NE2 91.8 102.2 145.0
REMARK 620 5 HOH L2023 O 126.2 94.9 65.0 87.8
REMARK 620 N 1 2 3 4
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 105.3
REMARK 620 3 HIS L 80 ND1 126.0 109.1
REMARK 620 4 ASP L 83 OD1 106.2 95.4 110.5
REMARK 620 N 1 2 3
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA DA GA HA KA LA" IN EACH CHAIN ON
REMARK 700 SHEET RECORDS BELOW IS ACTUALLY AN 9-STRANDED BARREL
REMARK 700 THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE
REMARK 700 FIRST AND LAST STRANDS 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 CU D 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU H 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU I 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU J 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU K 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU L 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 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 SUPEROXIDE DISMUTASE,
REMARK 900 NMR, 36 STRUCTURES
REMARK 900 RELATED ID: 1DSW RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER,
REMARK 900 ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE
REMARK 900 PROTEIN
REMARK 900 RELATED ID: 1FUN RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6
REMARK 900 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)
REMARK 900 RELATED ID: 1HL4 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1HL5 RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1KMG RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF MONOMERIC COPPER- FREE SUPEROXIDEDISMUTASE
REMARK 900 RELATED ID: 1L3N RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE
REMARK 900 STRUCTURAL EFFECTS OF DIMERIZATION
REMARK 900 RELATED ID: 1MFM RELATED DB: PDB
REMARK 900 MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 1N18 RELATED DB: PDB
REMARK 900 THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,C111S
REMARK 900 RELATED ID: 1N19 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE HSOD A4V MUTANT
REMARK 900 RELATED ID: 1OEZ RELATED DB: PDB
REMARK 900 ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1OZT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,ZN
REMARK 900 SUPEROXIDE DISMUTASE (CUZNSOD) TO 2.5A RESOLUTION
REMARK 900 RELATED ID: 1OZU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF HUMAN CU,ZN
REMARK 900 SUPEROXIDE DISMUTASE (CUZNSOD) TO 1.3A RESOLUTION
REMARK 900 RELATED ID: 1P1V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER-ZINCSUPEROXIDE
REMARK 900 DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A
REMARK 900 RELATED ID: 1PTZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE DISMUTASE,FAMILIAL
REMARK 900 AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R
REMARK 900 RELATED ID: 1PU0 RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1RK7 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL
REMARK 900 IONS IN PROTEIN FOLDING
REMARK 900 RELATED ID: 1SOS RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111
REMARK 900 REPLACED BY SER (C6A, C111S)
REMARK 900 RELATED ID: 1SPD RELATED DB: PDB
REMARK 900 SUPEROXIDE DISMUTASE
REMARK 900 RELATED ID: 1UXL RELATED DB: PDB
REMARK 900 I113T MUTANT OF HUMAN SOD1
REMARK 900 RELATED ID: 4SOD RELATED DB: PDB
REMARK 900 CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND
REMARK 900 CYS 111 REPLACED BY SER (C6A,C111S) WITH AN 18-RESIDUE HEPARIN-
REMARK 900 BINDING PEPTIDE FUSED TO THE C- TERMINUS (THEORETICAL MODEL)
DBREF 1UXM A 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM B 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM C 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM D 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM E 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM F 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM G 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM H 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM I 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM J 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM K 1 153 UNP P00441 SODC_HUMAN 1 153
DBREF 1UXM L 1 153 UNP P00441 SODC_HUMAN 1 153
SEQADV 1UXM VAL A 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL B 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL C 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL D 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL E 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL F 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL G 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL H 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL I 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL J 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL K 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQADV 1UXM VAL L 4 UNP P00441 ALA 4 ENGINEERED MUTATION
SEQRES 1 A 153 ALA THR LYS VAL 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 VAL 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 VAL 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 VAL 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 VAL 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 VAL 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 VAL 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 VAL 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 VAL 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 VAL 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 VAL 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 VAL 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
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 CU D 154 1
HET ZN D 155 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
HETNAM CU COPPER (II) ION
HETNAM ZN ZINC ION
FORMUL 13 CU 12(CU 2+)
FORMUL 14 ZN 12(ZN 2+)
FORMUL 37 HOH *1096(H2 O)
HELIX 1 1 CYS A 57 GLY A 61 5 5
HELIX 2 2 GLU A 133 GLY A 138 1 6
HELIX 3 3 CYS B 57 GLY B 61 5 5
HELIX 4 4 SER B 107 HIS B 110 5 4
HELIX 5 5 GLU B 133 GLY B 138 1 6
HELIX 6 6 ALA C 55 GLY C 61 5 7
HELIX 7 7 GLU C 133 GLY C 138 1 6
HELIX 8 8 CYS D 57 GLY D 61 5 5
HELIX 9 9 SER D 107 HIS D 110 5 4
HELIX 10 10 GLU D 133 GLY D 138 1 6
HELIX 11 11 ALA E 55 GLY E 61 5 7
HELIX 12 12 SER E 107 HIS E 110 5 4
HELIX 13 13 GLU E 133 GLY E 138 1 6
HELIX 14 14 ALA F 55 GLY F 61 5 7
HELIX 15 15 SER F 107 HIS F 110 5 4
HELIX 16 16 GLU F 133 GLY F 138 1 6
HELIX 17 17 ALA G 55 GLY G 61 5 7
HELIX 18 18 GLU G 133 GLY G 138 1 6
HELIX 19 19 CYS H 57 GLY H 61 5 5
HELIX 20 20 GLU H 133 GLY H 138 1 6
HELIX 21 21 ALA I 55 GLY I 61 5 7
HELIX 22 22 SER I 107 HIS I 110 5 4
HELIX 23 23 ALA J 55 GLY J 61 5 7
HELIX 24 24 ALA K 55 GLY K 61 5 7
HELIX 25 25 SER K 107 HIS K 110 5 4
HELIX 26 26 ASN K 131 GLY K 138 1 8
HELIX 27 27 CYS L 57 GLY L 61 5 5
HELIX 28 28 SER L 107 HIS L 110 5 4
HELIX 29 29 GLU L 133 GLY L 138 1 6
SHEET 1 AA10 LYS A 3 LEU A 8 0
SHEET 2 AA10 GLN A 15 GLN A 22 -1 O GLY A 16 N LEU A 8
SHEET 3 AA10 VAL A 29 LYS A 36 -1 O LYS A 30 N GLU A 21
SHEET 4 AA10 ALA A 95 ASP A 101 -1 O ALA A 95 N ILE A 35
SHEET 5 AA10 ASP A 83 ALA A 89 -1 O THR A 88 N ASP A 96
SHEET 6 AA10 GLY A 41 HIS A 48 -1 O GLY A 41 N ALA A 89
SHEET 7 AA10 THR A 116 HIS A 120 -1 O THR A 116 N HIS A 48
SHEET 8 AA10 ARG A 143 ILE A 151 -1 N LEU A 144 O VAL A 119
SHEET 9 AA10 LYS A 3 LEU A 8 -1 O VAL A 5 N GLY A 150
SHEET 10 AA10 LYS A 3 LEU A 8 0
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 GLU B 21 -1 O GLN B 15 N LYS B 36
SHEET 4 BA 5 LYS B 3 LEU B 8 -1 O VAL B 4 N PHE B 20
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 LYS C 3 LEU C 8 -1 O VAL C 4 N PHE C 20
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 9 LYS D 3 LYS D 9 0
SHEET 2 DA 9 GLN D 15 GLN D 22 -1 O GLY D 16 N LEU D 8
SHEET 3 DA 9 VAL D 29 LYS D 36 -1 O LYS D 30 N GLU D 21
SHEET 4 DA 9 ALA D 95 ASP D 101 -1 O ALA D 95 N ILE D 35
SHEET 5 DA 9 ASP D 83 ALA D 89 -1 O THR D 88 N ASP D 96
SHEET 6 DA 9 GLY D 41 HIS D 48 -1 O GLY D 41 N ALA D 89
SHEET 7 DA 9 THR D 116 HIS D 120 -1 O THR D 116 N HIS D 48
SHEET 8 DA 9 ARG D 143 ILE D 151 -1 N LEU D 144 O VAL D 119
SHEET 9 DA 9 LYS D 3 LYS D 9 -1 O VAL D 5 N GLY D 150
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 GLU E 21 -1 O GLN E 15 N LYS E 36
SHEET 4 EA 5 LYS E 3 LEU E 8 -1 O VAL E 4 N PHE E 20
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 5 ALA F 95 ASP F 101 0
SHEET 2 FA 5 VAL F 29 LYS F 36 -1 O VAL F 29 N ASP F 101
SHEET 3 FA 5 GLN F 15 GLN F 22 -1 O GLN F 15 N LYS F 36
SHEET 4 FA 5 LYS F 3 LEU F 8 -1 O VAL F 4 N PHE F 20
SHEET 5 FA 5 GLY F 150 ILE F 151 -1 O GLY F 150 N VAL F 5
SHEET 1 FB 4 ASP F 83 ALA F 89 0
SHEET 2 FB 4 GLY F 41 HIS F 48 -1 O GLY F 41 N ALA F 89
SHEET 3 FB 4 THR F 116 HIS F 120 -1 O THR F 116 N HIS F 48
SHEET 4 FB 4 ARG F 143 VAL F 148 -1 N LEU F 144 O VAL F 119
SHEET 1 GA24 LYS G 3 LEU G 8 0
SHEET 2 GA24 GLN G 15 GLU G 21 -1 O GLY G 16 N LEU G 8
SHEET 3 GA24 VAL G 29 LYS G 36 -1 O LYS G 30 N GLU G 21
SHEET 4 GA24 VAL G 94 ALA G 95 -1 O ALA G 95 N ILE G 35
SHEET 5 GA24 ASP G 83 ALA G 89 0
SHEET 6 GA24 GLY G 41 HIS G 48 -1 O GLY G 41 N ALA G 89
SHEET 7 GA24 THR G 116 HIS G 120 -1 O THR G 116 N HIS G 48
SHEET 8 GA24 ARG G 143 ILE G 151 -1 N LEU G 144 O VAL G 119
SHEET 9 GA24 GLN G 15 GLU G 21 0
SHEET 10 GA24 LYS G 3 LEU G 8 -1 O VAL G 4 N PHE G 20
SHEET 11 GA24 VAL G 29 LYS G 36 0
SHEET 12 GA24 GLN G 15 GLU G 21 -1 O GLN G 15 N LYS G 36
SHEET 13 GA24 GLY G 41 HIS G 48 0
SHEET 14 GA24 ASP G 83 ALA G 89 -1 O GLY G 85 N PHE G 45
SHEET 15 GA24 ASP G 83 ALA G 89 0
SHEET 16 GA24 GLY G 41 HIS G 48 -1 O GLY G 41 N ALA G 89
SHEET 17 GA24 VAL G 94 ALA G 95 0
SHEET 18 GA24 VAL G 29 LYS G 36 -1 O ILE G 35 N ALA G 95
SHEET 19 GA24 SER G 98 ASP G 101 -1 O ILE G 99 N VAL G 31
SHEET 20 GA24 VAL G 29 LYS G 36 1 O VAL G 29 N ASP G 101
SHEET 21 GA24 THR G 116 HIS G 120 0
SHEET 22 GA24 GLY G 41 HIS G 48 -1 O GLY G 44 N HIS G 120
SHEET 23 GA24 ARG G 143 ILE G 151 0
SHEET 24 GA24 LYS G 3 LEU G 8 -1 O VAL G 5 N GLY G 150
SHEET 1 HA16 LYS H 3 LYS H 9 0
SHEET 2 HA16 GLN H 15 GLU H 21 -1 O GLY H 16 N LEU H 8
SHEET 3 HA16 GLN H 15 GLU H 21 0
SHEET 4 HA16 LYS H 3 LYS H 9 -1 O VAL H 4 N PHE H 20
SHEET 5 HA16 VAL H 29 LYS H 36 0
SHEET 6 HA16 GLN H 15 GLU H 21 -1 O GLN H 15 N LYS H 36
SHEET 7 HA16 GLY H 41 HIS H 48 0
SHEET 8 HA16 ASP H 83 ALA H 89 -1 O GLY H 85 N PHE H 45
SHEET 9 HA16 ASP H 83 ALA H 89 0
SHEET 10 HA16 GLY H 41 HIS H 48 -1 O GLY H 41 N ALA H 89
SHEET 11 HA16 VAL H 94 ASP H 101 0
SHEET 12 HA16 VAL H 29 LYS H 36 -1 O VAL H 29 N ASP H 101
SHEET 13 HA16 THR H 116 HIS H 120 0
SHEET 14 HA16 GLY H 41 HIS H 48 -1 O GLY H 44 N HIS H 120
SHEET 15 HA16 ARG H 143 GLY H 150 0
SHEET 16 HA16 LYS H 3 LYS H 9 -1 O VAL H 5 N GLY H 150
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 LYS I 3 LEU I 8 -1 O VAL I 4 N PHE I 20
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 8 ASP J 83 ALA J 89 0
SHEET 2 JA 8 GLY J 41 HIS J 48 -1 O GLY J 41 N ALA J 89
SHEET 3 JA 8 THR J 116 HIS J 120 -1 O THR J 116 N HIS J 48
SHEET 4 JA 8 ARG J 143 ILE J 151 -1 N LEU J 144 O VAL J 119
SHEET 5 JA 8 LYS J 3 GLY J 10 -1 O VAL J 5 N GLY J 150
SHEET 6 JA 8 GLN J 15 GLN J 22 -1 O GLY J 16 N LEU J 8
SHEET 7 JA 8 VAL J 29 LYS J 36 -1 O LYS J 30 N GLU J 21
SHEET 8 JA 8 ALA J 95 ASP J 101 -1 O ALA J 95 N ILE J 35
SHEET 1 KA16 LYS K 3 LEU K 8 0
SHEET 2 KA16 GLN K 15 GLN K 22 -1 O GLY K 16 N LEU K 8
SHEET 3 KA16 GLN K 15 GLN K 22 0
SHEET 4 KA16 LYS K 3 LEU K 8 -1 O VAL K 4 N PHE K 20
SHEET 5 KA16 VAL K 29 LYS K 36 0
SHEET 6 KA16 GLN K 15 GLN K 22 -1 O GLN K 15 N LYS K 36
SHEET 7 KA16 GLY K 41 HIS K 48 0
SHEET 8 KA16 ASP K 83 ALA K 89 -1 O GLY K 85 N PHE K 45
SHEET 9 KA16 ASP K 83 ALA K 89 0
SHEET 10 KA16 GLY K 41 HIS K 48 -1 O GLY K 41 N ALA K 89
SHEET 11 KA16 VAL K 94 ASP K 101 0
SHEET 12 KA16 VAL K 29 LYS K 36 -1 O VAL K 29 N ASP K 101
SHEET 13 KA16 THR K 116 HIS K 120 0
SHEET 14 KA16 GLY K 41 HIS K 48 -1 O GLY K 44 N HIS K 120
SHEET 15 KA16 ARG K 143 ILE K 151 0
SHEET 16 KA16 LYS K 3 LEU K 8 -1 O VAL K 5 N GLY K 150
SHEET 1 LA16 LYS L 3 LEU L 8 0
SHEET 2 LA16 GLN L 15 GLU L 21 -1 O GLY L 16 N LEU L 8
SHEET 3 LA16 GLN L 15 GLU L 21 0
SHEET 4 LA16 LYS L 3 LEU L 8 -1 O VAL L 4 N PHE L 20
SHEET 5 LA16 VAL L 29 LYS L 36 0
SHEET 6 LA16 GLN L 15 GLU L 21 -1 O GLN L 15 N LYS L 36
SHEET 7 LA16 GLY L 41 HIS L 48 0
SHEET 8 LA16 ASP L 83 ALA L 89 -1 O GLY L 85 N PHE L 45
SHEET 9 LA16 ASP L 83 ALA L 89 0
SHEET 10 LA16 GLY L 41 HIS L 48 -1 O GLY L 41 N ALA L 89
SHEET 11 LA16 ALA L 95 ASP L 101 0
SHEET 12 LA16 VAL L 29 LYS L 36 -1 O VAL L 29 N ASP L 101
SHEET 13 LA16 THR L 116 HIS L 120 0
SHEET 14 LA16 GLY L 41 HIS L 48 -1 O GLY L 44 N HIS L 120
SHEET 15 LA16 ARG L 143 ILE L 151 0
SHEET 16 LA16 LYS L 3 LEU L 8 -1 O VAL L 5 N GLY L 150
SSBOND 1 CYS A 57 CYS A 146 1555 1555 2.16
SSBOND 2 CYS B 57 CYS B 146 1555 1555 2.17
SSBOND 3 CYS C 57 CYS C 146 1555 1555 2.16
SSBOND 4 CYS D 57 CYS D 146 1555 1555 2.18
SSBOND 5 CYS E 57 CYS E 146 1555 1555 2.10
SSBOND 6 CYS F 57 CYS F 146 1555 1555 2.10
SSBOND 7 CYS G 57 CYS G 146 1555 1555 2.05
SSBOND 8 CYS H 57 CYS H 146 1555 1555 2.09
SSBOND 9 CYS I 57 CYS I 146 1555 1555 2.10
SSBOND 10 CYS J 57 CYS J 146 1555 1555 2.10
SSBOND 11 CYS K 57 CYS K 146 1555 1555 2.08
SSBOND 12 CYS L 57 CYS L 146 1555 1555 2.04
LINK ND1 HIS A 46 CU CU A 154 1555 1555 2.18
LINK NE2 HIS A 48 CU CU A 154 1555 1555 2.13
LINK NE2 HIS A 63 CU CU A 154 1555 1555 2.36
LINK ND1 HIS A 63 ZN ZN A 155 1555 1555 2.01
LINK ND1 HIS A 71 ZN ZN A 155 1555 1555 2.08
LINK ND1 HIS A 80 ZN ZN A 155 1555 1555 1.91
LINK OD1 ASP A 83 ZN ZN A 155 1555 1555 1.91
LINK NE2 HIS A 120 CU CU A 154 1555 1555 2.08
LINK CU CU A 154 O HOH A2060 1555 1555 1.86
LINK ND1 HIS B 46 CU CU B 154 1555 1555 2.12
LINK NE2 HIS B 48 CU CU B 154 1555 1555 2.15
LINK NE2 HIS B 63 CU CU B 154 1555 1555 2.22
LINK ND1 HIS B 63 ZN ZN B 155 1555 1555 2.05
LINK ND1 HIS B 71 ZN ZN B 155 1555 1555 2.02
LINK ND1 HIS B 80 ZN ZN B 155 1555 1555 1.97
LINK OD1 ASP B 83 ZN ZN B 155 1555 1555 1.95
LINK NE2 HIS B 120 CU CU B 154 1555 1555 2.19
LINK CU CU B 154 O HOH B2062 1555 1555 2.21
LINK ND1 HIS C 46 CU CU C 154 1555 1555 2.22
LINK NE2 HIS C 48 CU CU C 154 1555 1555 2.09
LINK NE2 HIS C 63 CU CU C 154 1555 1555 2.29
LINK ND1 HIS C 63 ZN ZN C 155 1555 1555 2.02
LINK ND1 HIS C 71 ZN ZN C 155 1555 1555 2.04
LINK ND1 HIS C 80 ZN ZN C 155 1555 1555 1.96
LINK OD1 ASP C 83 ZN ZN C 155 1555 1555 1.98
LINK NE2 HIS C 120 CU CU C 154 1555 1555 2.09
LINK CU CU C 154 O HOH C2063 1555 1555 2.44
LINK ND1 HIS D 46 CU CU D 154 1555 1555 2.09
LINK NE2 HIS D 48 CU CU D 154 1555 1555 2.12
LINK NE2 HIS D 63 CU CU D 154 1555 1555 2.36
LINK ND1 HIS D 63 ZN ZN D 155 1555 1555 1.95
LINK ND1 HIS D 71 ZN ZN D 155 1555 1555 2.02
LINK ND1 HIS D 80 ZN ZN D 155 1555 1555 1.94
LINK OD1 ASP D 83 ZN ZN D 155 1555 1555 1.90
LINK NE2 HIS D 120 CU CU D 154 1555 1555 2.05
LINK CU CU D 154 O HOH D2063 1555 1555 2.14
LINK ND1 HIS E 46 CU CU E 154 1555 1555 2.08
LINK NE2 HIS E 48 CU CU E 154 1555 1555 2.21
LINK NE2 HIS E 63 CU CU E 154 1555 1555 2.20
LINK ND1 HIS E 63 ZN ZN E 155 1555 1555 2.03
LINK ND1 HIS E 71 ZN ZN E 155 1555 1555 2.12
LINK ND1 HIS E 80 ZN ZN E 155 1555 1555 1.90
LINK OD1 ASP E 83 ZN ZN E 155 1555 1555 1.99
LINK NE2 HIS E 120 CU CU E 154 1555 1555 2.02
LINK CU CU E 154 O HOH E2032 1555 1555 2.35
LINK ND1 HIS F 46 CU CU F 154 1555 1555 2.17
LINK NE2 HIS F 48 CU CU F 154 1555 1555 2.14
LINK NE2 HIS F 63 CU CU F 154 1555 1555 2.43
LINK ND1 HIS F 63 ZN ZN F 155 1555 1555 1.94
LINK ND1 HIS F 71 ZN ZN F 155 1555 1555 1.95
LINK ND1 HIS F 80 ZN ZN F 155 1555 1555 2.13
LINK OD1 ASP F 83 ZN ZN F 155 1555 1555 1.91
LINK NE2 HIS F 120 CU CU F 154 1555 1555 1.99
LINK CU CU F 154 O HOH F2018 1555 1555 2.03
LINK ND1 HIS G 46 CU CU G 154 1555 1555 2.07
LINK NE2 HIS G 48 CU CU G 154 1555 1555 2.18
LINK NE2 HIS G 63 CU CU G 154 1555 1555 2.36
LINK ND1 HIS G 63 ZN ZN G 155 1555 1555 1.92
LINK ND1 HIS G 71 ZN ZN G 155 1555 1555 2.03
LINK ND1 HIS G 80 ZN ZN G 155 1555 1555 1.91
LINK OD1 ASP G 83 ZN ZN G 155 1555 1555 1.93
LINK NE2 HIS G 120 CU CU G 154 1555 1555 2.15
LINK CU CU G 154 O HOH G2030 1555 1555 2.43
LINK ND1 HIS H 46 CU CU H 154 1555 1555 2.05
LINK NE2 HIS H 48 CU CU H 154 1555 1555 2.26
LINK NE2 HIS H 63 CU CU H 154 1555 1555 2.22
LINK ND1 HIS H 63 ZN ZN H 155 1555 1555 2.02
LINK ND1 HIS H 71 ZN ZN H 155 1555 1555 2.17
LINK ND1 HIS H 80 ZN ZN H 155 1555 1555 1.82
LINK OD1 ASP H 83 ZN ZN H 155 1555 1555 2.07
LINK NE2 HIS H 120 CU CU H 154 1555 1555 2.05
LINK CU CU H 154 O HOH H2065 1555 1555 2.62
LINK ND1 HIS I 46 CU CU I 154 1555 1555 2.34
LINK NE2 HIS I 48 CU CU I 154 1555 1555 2.28
LINK NE2 HIS I 63 CU CU I 154 1555 1555 1.97
LINK ND1 HIS I 63 ZN ZN I 155 1555 1555 2.29
LINK ND1 HIS I 71 ZN ZN I 155 1555 1555 2.07
LINK ND1 HIS I 80 ZN ZN I 155 1555 1555 1.74
LINK OD1 ASP I 83 ZN ZN I 155 1555 1555 2.12
LINK NE2 HIS I 120 CU CU I 154 1555 1555 2.17
LINK CU CU I 154 O HOH I2031 1555 1555 2.28
LINK ND1 HIS J 46 CU CU J 154 1555 1555 2.01
LINK NE2 HIS J 48 CU CU J 154 1555 1555 2.24
LINK NE2 HIS J 63 CU CU J 154 1555 1555 2.15
LINK ND1 HIS J 63 ZN ZN J 155 1555 1555 2.06
LINK ND1 HIS J 71 ZN ZN J 155 1555 1555 1.98
LINK ND1 HIS J 80 ZN ZN J 155 1555 1555 1.85
LINK OD2 ASP J 83 ZN ZN J 155 1555 1555 2.77
LINK OD1 ASP J 83 ZN ZN J 155 1555 1555 1.84
LINK NE2 HIS J 120 CU CU J 154 1555 1555 2.04
LINK CU CU J 154 O HOH J2030 1555 1555 2.28
LINK ND1 HIS K 46 CU CU K 154 1555 1555 2.08
LINK NE2 HIS K 48 CU CU K 154 1555 1555 2.18
LINK NE2 HIS K 63 CU CU K 154 1555 1555 2.26
LINK ND1 HIS K 63 ZN ZN K 155 1555 1555 1.93
LINK ND1 HIS K 71 ZN ZN K 155 1555 1555 2.11
LINK ND1 HIS K 80 ZN ZN K 155 1555 1555 2.03
LINK OD1 ASP K 83 ZN ZN K 155 1555 1555 1.95
LINK NE2 HIS K 120 CU CU K 154 1555 1555 2.13
LINK CU CU K 154 O HOH K2021 1555 1555 2.35
LINK ND1 HIS L 46 CU CU L 154 1555 1555 2.11
LINK NE2 HIS L 48 CU CU L 154 1555 1555 2.16
LINK NE2 HIS L 63 CU CU L 154 1555 1555 1.96
LINK ND1 HIS L 63 ZN ZN L 155 1555 1555 2.28
LINK ND1 HIS L 71 ZN ZN L 155 1555 1555 2.14
LINK ND1 HIS L 80 ZN ZN L 155 1555 1555 1.63
LINK OD1 ASP L 83 ZN ZN L 155 1555 1555 1.99
LINK NE2 HIS L 120 CU CU L 154 1555 1555 2.23
LINK CU CU L 154 O HOH L2023 1555 1555 2.47
CISPEP 1 ASN A 26 GLY A 27 0 -0.81
SITE 1 AC1 5 HIS A 46 HIS A 48 HIS A 63 HIS A 120
SITE 2 AC1 5 HOH A2060
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 B2062
SITE 1 AC4 5 HIS B 63 HIS B 71 HIS B 80 ASP B 83
SITE 2 AC4 5 LYS B 136
SITE 1 AC5 5 HIS C 46 HIS C 48 HIS C 63 HIS C 120
SITE 2 AC5 5 HOH C2063
SITE 1 AC6 5 HIS C 63 HIS C 71 HIS C 80 ASP C 83
SITE 2 AC6 5 LYS C 136
SITE 1 AC7 5 HIS D 46 HIS D 48 HIS D 63 HIS D 120
SITE 2 AC7 5 HOH D2063
SITE 1 AC8 5 HIS D 63 HIS D 71 HIS D 80 ASP D 83
SITE 2 AC8 5 LYS D 136
SITE 1 AC9 5 HIS E 46 HIS E 48 HIS E 63 HIS E 120
SITE 2 AC9 5 HOH E2032
SITE 1 BC1 5 HIS E 63 HIS E 71 HIS E 80 ASP E 83
SITE 2 BC1 5 LYS E 136
SITE 1 BC2 5 HIS F 46 HIS F 48 HIS F 63 HIS F 120
SITE 2 BC2 5 HOH F2018
SITE 1 BC3 4 HIS F 63 HIS F 71 HIS F 80 ASP F 83
SITE 1 BC4 5 HIS G 46 HIS G 48 HIS G 63 HIS G 120
SITE 2 BC4 5 HOH G2030
SITE 1 BC5 5 HIS G 63 HIS G 71 HIS G 80 ASP G 83
SITE 2 BC5 5 LYS G 136
SITE 1 BC6 5 HIS H 46 HIS H 48 HIS H 63 HIS H 120
SITE 2 BC6 5 HOH H2065
SITE 1 BC7 5 HIS H 63 HIS H 71 HIS H 80 ASP H 83
SITE 2 BC7 5 LYS H 136
SITE 1 BC8 5 HIS I 46 HIS I 48 HIS I 63 HIS I 120
SITE 2 BC8 5 HOH I2031
SITE 1 BC9 5 HIS I 63 HIS I 71 HIS I 80 ASP I 83
SITE 2 BC9 5 LYS I 136
SITE 1 CC1 5 HIS J 46 HIS J 48 HIS J 63 HIS J 120
SITE 2 CC1 5 HOH J2030
SITE 1 CC2 4 HIS J 63 HIS J 71 HIS J 80 ASP J 83
SITE 1 CC3 5 HIS K 46 HIS K 48 HIS K 63 HIS K 120
SITE 2 CC3 5 HOH K2021
SITE 1 CC4 5 HIS K 63 HIS K 71 HIS K 80 ASP K 83
SITE 2 CC4 5 LYS K 136
SITE 1 CC5 5 HIS L 46 HIS L 48 HIS L 63 HIS L 120
SITE 2 CC5 5 HOH L2023
SITE 1 CC6 5 HIS L 63 HIS L 71 HIS L 80 ASP L 83
SITE 2 CC6 5 LYS L 136
CRYST1 112.374 145.582 112.497 90.00 120.05 90.00 P 1 21 1 24
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 0.008899 0.000000 0.005148 0.00000
SCALE2 0.000000 0.006869 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010269 0.00000
MTRIX1 1 -0.998090 -0.061730 -0.001080 22.19083 1
MTRIX2 1 -0.061340 0.989390 0.131680 -0.27397 1
MTRIX3 1 -0.007060 0.131500 -0.991290 14.30155 1
MTRIX1 2 0.500080 -0.001140 0.865980 5.53139 1
MTRIX2 2 0.008610 -0.999940 -0.006290 -96.49535 1
MTRIX3 2 0.865940 0.010600 -0.500040 3.50316 1
MTRIX1 3 0.500080 -0.001140 0.865980 5.53139 1
MTRIX2 3 0.008610 -0.999940 -0.006290 -96.49535 1
MTRIX3 3 0.865940 0.010600 -0.500040 3.50316 1
MTRIX1 4 0.497670 0.043040 -0.866300 11.47130 1
MTRIX2 4 -0.011810 -0.998340 -0.056390 -24.22828 1
MTRIX3 4 -0.867290 0.038300 -0.496330 51.82755 1
MTRIX1 5 -0.496760 -0.103430 0.861700 10.20352 1
MTRIX2 5 0.037170 -0.994500 -0.097940 -24.47743 1
MTRIX3 5 0.867090 -0.016620 0.497870 24.20590 1
MTRIX1 6 0.999310 0.037140 -0.000220 29.20916 1
MTRIX2 6 0.037050 -0.997330 -0.062990 -24.06009 1
MTRIX3 6 -0.002560 0.062930 -0.998010 -3.92607 1
MTRIX1 7 -0.999750 0.022480 0.001970 52.84855 1
MTRIX2 7 -0.022540 -0.998820 -0.043060 -23.35865 1
MTRIX3 7 0.001000 -0.043100 0.999070 -17.47200 1
MTRIX1 8 -0.505140 0.036020 -0.862290 55.65426 1
MTRIX2 8 0.029500 0.999270 0.024460 73.59691 1
MTRIX3 8 0.862540 -0.013080 -0.505830 -13.55712 1
MTRIX1 9 0.505200 -0.100660 0.857110 30.64955 1
MTRIX2 9 -0.022250 0.991320 0.129540 73.32990 1
MTRIX3 9 -0.862710 -0.084510 0.498580 0.01541 1
MTRIX1 10 -0.489450 -0.071680 0.869080 15.39836 1
MTRIX2 10 0.001270 0.996560 0.082900 72.11509 1
MTRIX3 10 -0.872030 0.041680 -0.487670 57.78385 1
MTRIX1 11 0.494860 0.066130 -0.866450 16.56118 1
MTRIX2 11 -0.033700 0.997810 0.056910 72.75935 1
MTRIX3 11 0.868320 0.001040 0.496000 30.56594 1
(ATOM LINES ARE NOT SHOWN.)
END
