HEADER METAL BINDING PROTEIN 21-FEB-11 3QSI
TITLE NICKEL BINDING DOMAIN OF NIKR FROM HELICOBACTER PYLORI DISCLOSING
TITLE 2 PARTIAL METAL OCCUPANCY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NIKR NICKEL-RESPONSIVE REGULATOR;
COMPND 3 CHAIN: B, C, D, A, F, G, H, E, J, I;
COMPND 4 FRAGMENT: NICKEL BINDING DOMAIN (UNP RESIDUES 61-148);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;
SOURCE 3 ORGANISM_COMMON: CAMPYLOBACTER PYLORI;
SOURCE 4 ORGANISM_TAXID: 210;
SOURCE 5 GENE: HP_1338;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS NIKR, NICKEL, HELICOBACTER PYLORI, DNA-BINDING, TRANSCRIPTION
KEYWDS 2 REGULATOR, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.GONZALEZ,E.POZHARSKI
REVDAT 4 21-FEB-24 3QSI 1 REMARK LINK
REVDAT 3 08-NOV-17 3QSI 1 REMARK
REVDAT 2 13-JUN-12 3QSI 1 JRNL
REVDAT 1 04-APR-12 3QSI 0
JRNL AUTH A.L.WEST,S.E.EVANS,J.M.GONZALEZ,L.G.CARTER,H.TSURUTA,
JRNL AUTH 2 E.POZHARSKI,S.L.MICHEL
JRNL TITL NI(II) COORDINATION TO MIXED SITES MODULATES DNA BINDING OF
JRNL TITL 2 HPNIKR VIA A LONG-RANGE EFFECT.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 5633 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22451934
JRNL DOI 10.1073/PNAS.1120283109
REMARK 2
REMARK 2 RESOLUTION. 3.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 3.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 103.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 19187
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) : 0.262
REMARK 3 R VALUE (WORKING SET) : 0.257
REMARK 3 FREE R VALUE : 0.304
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2165
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) : 3.08
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1325
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.3710
REMARK 3 BIN FREE R VALUE SET COUNT : 126
REMARK 3 BIN FREE R VALUE : 0.4380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6104
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.88000
REMARK 3 B22 (A**2) : 4.74000
REMARK 3 B33 (A**2) : 0.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.44000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.556
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.467
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 57.211
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.895
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.840
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6236 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3954 ; 0.009 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8389 ; 1.669 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9718 ; 1.269 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 785 ; 7.311 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 274 ;40.430 ;24.416
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1102 ;19.697 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;21.375 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1024 ; 0.167 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6841 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1188 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 3915 ; 0.991 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1630 ; 0.123 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6273 ; 1.842 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2321 ; 1.834 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2116 ; 2.730 ; 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 : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 62 A 142 1
REMARK 3 1 C 62 C 142 1
REMARK 3 1 E 62 E 142 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 952 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 952 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 E (A): 952 ; 0.06 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 952 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 952 ; 0.09 ; 0.50
REMARK 3 TIGHT THERMAL 1 E (A**2): 952 ; 0.09 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D H F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 64 B 144 1
REMARK 3 1 D 64 D 144 1
REMARK 3 1 H 64 H 144 1
REMARK 3 1 F 64 F 144 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 895 ; 0.09 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 D (A): 895 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 H (A): 895 ; 0.07 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 F (A): 895 ; 0.07 ; 0.05
REMARK 3 TIGHT THERMAL 2 B (A**2): 895 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 2 D (A**2): 895 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 2 H (A**2): 895 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 2 F (A**2): 895 ; 0.08 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A I G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 62 A 142 1
REMARK 3 1 I 62 I 142 1
REMARK 3 1 G 62 G 142 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 891 ; 0.08 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 I (A): 891 ; 0.06 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 G (A): 891 ; 0.08 ; 0.05
REMARK 3 TIGHT THERMAL 3 A (A**2): 891 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 3 I (A**2): 891 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 3 G (A**2): 891 ; 0.11 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : B J
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 64 B 142 1
REMARK 3 1 J 64 J 142 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 B (A): 927 ; 0.08 ; 0.05
REMARK 3 TIGHT THERMAL 4 B (A**2): 927 ; 0.09 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 64 I 80
REMARK 3 RESIDUE RANGE : I 81 I 124
REMARK 3 RESIDUE RANGE : I 125 I 142
REMARK 3 ORIGIN FOR THE GROUP (A): 54.7281 21.8077 45.3365
REMARK 3 T TENSOR
REMARK 3 T11: 0.1238 T22: 0.1009
REMARK 3 T33: 0.2439 T12: 0.0071
REMARK 3 T13: -0.0024 T23: -0.0691
REMARK 3 L TENSOR
REMARK 3 L11: 2.4052 L22: 1.7670
REMARK 3 L33: 3.6574 L12: -0.9207
REMARK 3 L13: -0.0389 L23: -2.2576
REMARK 3 S TENSOR
REMARK 3 S11: 0.1437 S12: -0.0689 S13: 0.2309
REMARK 3 S21: 0.0191 S22: -0.1574 S23: -0.0716
REMARK 3 S31: -0.1229 S32: 0.2993 S33: 0.0137
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 64 J 77
REMARK 3 RESIDUE RANGE : J 78 J 107
REMARK 3 RESIDUE RANGE : J 108 J 142
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6098 17.5812 40.1913
REMARK 3 T TENSOR
REMARK 3 T11: 0.1212 T22: 0.1936
REMARK 3 T33: 0.1961 T12: -0.0030
REMARK 3 T13: -0.0518 T23: -0.0508
REMARK 3 L TENSOR
REMARK 3 L11: 0.9942 L22: 0.9625
REMARK 3 L33: 1.6804 L12: 0.7415
REMARK 3 L13: 1.1994 L23: 0.8410
REMARK 3 S TENSOR
REMARK 3 S11: -0.0593 S12: -0.0779 S13: 0.1195
REMARK 3 S21: 0.1559 S22: -0.0734 S23: -0.1009
REMARK 3 S31: -0.1029 S32: -0.1446 S33: 0.1327
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 64 G 85
REMARK 3 RESIDUE RANGE : G 86 G 117
REMARK 3 RESIDUE RANGE : G 118 G 142
REMARK 3 RESIDUE RANGE : G 1 G 1
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5198 -9.5604 -1.4815
REMARK 3 T TENSOR
REMARK 3 T11: 0.1129 T22: 0.1768
REMARK 3 T33: 0.2342 T12: 0.0810
REMARK 3 T13: -0.0897 T23: -0.1313
REMARK 3 L TENSOR
REMARK 3 L11: 2.6950 L22: 0.9537
REMARK 3 L33: 7.4808 L12: 1.5442
REMARK 3 L13: 3.3230 L23: 2.3819
REMARK 3 S TENSOR
REMARK 3 S11: -0.0850 S12: -0.5439 S13: 0.0823
REMARK 3 S21: -0.0727 S22: -0.3656 S23: 0.1102
REMARK 3 S31: -0.2666 S32: -0.8045 S33: 0.4505
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 64 H 82
REMARK 3 RESIDUE RANGE : H 83 H 107
REMARK 3 RESIDUE RANGE : H 108 H 142
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5460 -14.2617 -20.7218
REMARK 3 T TENSOR
REMARK 3 T11: 0.2110 T22: 0.1702
REMARK 3 T33: 0.1225 T12: 0.1199
REMARK 3 T13: -0.1174 T23: -0.1396
REMARK 3 L TENSOR
REMARK 3 L11: 1.4419 L22: 1.0846
REMARK 3 L33: 3.4409 L12: -0.0040
REMARK 3 L13: 2.0006 L23: -0.8474
REMARK 3 S TENSOR
REMARK 3 S11: -0.1722 S12: -0.0236 S13: 0.0334
REMARK 3 S21: 0.2695 S22: 0.0128 S23: -0.1037
REMARK 3 S31: -0.4703 S32: -0.0900 S33: 0.1594
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 62 A 85
REMARK 3 RESIDUE RANGE : A 86 A 124
REMARK 3 RESIDUE RANGE : A 125 A 141
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8325 -14.5238 38.8681
REMARK 3 T TENSOR
REMARK 3 T11: 0.1231 T22: 0.2849
REMARK 3 T33: 0.1431 T12: -0.0902
REMARK 3 T13: -0.0275 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.3307 L22: 2.4025
REMARK 3 L33: 0.4265 L12: 0.4811
REMARK 3 L13: 0.0669 L23: -0.7358
REMARK 3 S TENSOR
REMARK 3 S11: -0.0728 S12: -0.0602 S13: 0.1623
REMARK 3 S21: 0.0397 S22: -0.0784 S23: 0.0324
REMARK 3 S31: -0.1023 S32: 0.0235 S33: 0.1512
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 64 B 82
REMARK 3 RESIDUE RANGE : B 83 B 107
REMARK 3 RESIDUE RANGE : B 108 B 144
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8359 -17.5972 21.0582
REMARK 3 T TENSOR
REMARK 3 T11: 0.1680 T22: 0.2206
REMARK 3 T33: 0.1599 T12: -0.1124
REMARK 3 T13: -0.0497 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 4.4433 L22: 0.8124
REMARK 3 L33: 0.9683 L12: -0.1307
REMARK 3 L13: -1.7339 L23: -0.4319
REMARK 3 S TENSOR
REMARK 3 S11: -0.2220 S12: -0.0275 S13: -0.0484
REMARK 3 S21: -0.2270 S22: 0.1194 S23: -0.1528
REMARK 3 S31: 0.2282 S32: -0.0394 S33: 0.1025
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 63 C 85
REMARK 3 RESIDUE RANGE : C 86 C 124
REMARK 3 RESIDUE RANGE : C 125 C 142
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6106 -4.0398 23.7536
REMARK 3 T TENSOR
REMARK 3 T11: 0.1154 T22: 0.3174
REMARK 3 T33: 0.0718 T12: -0.0588
REMARK 3 T13: -0.0260 T23: -0.1039
REMARK 3 L TENSOR
REMARK 3 L11: 2.9373 L22: 1.4597
REMARK 3 L33: 0.3979 L12: 0.9104
REMARK 3 L13: -0.6268 L23: -0.7518
REMARK 3 S TENSOR
REMARK 3 S11: 0.0051 S12: -0.2026 S13: 0.1154
REMARK 3 S21: -0.1192 S22: 0.0845 S23: 0.1605
REMARK 3 S31: 0.0552 S32: -0.0372 S33: -0.0896
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 64 D 83
REMARK 3 RESIDUE RANGE : D 84 D 107
REMARK 3 RESIDUE RANGE : D 108 D 142
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8631 -8.8337 42.3097
REMARK 3 T TENSOR
REMARK 3 T11: 0.0764 T22: 0.4297
REMARK 3 T33: 0.0560 T12: -0.0615
REMARK 3 T13: -0.0274 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 1.0421 L22: 4.0886
REMARK 3 L33: 0.1182 L12: 0.9024
REMARK 3 L13: -0.1276 L23: 0.4615
REMARK 3 S TENSOR
REMARK 3 S11: -0.0338 S12: -0.2884 S13: -0.0556
REMARK 3 S21: 0.0098 S22: 0.0002 S23: 0.1907
REMARK 3 S31: 0.0216 S32: 0.0885 S33: 0.0336
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 63 E 85
REMARK 3 RESIDUE RANGE : E 86 E 127
REMARK 3 RESIDUE RANGE : E 128 E 142
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7355 -30.7386 -16.8925
REMARK 3 T TENSOR
REMARK 3 T11: 0.1942 T22: 0.1655
REMARK 3 T33: 0.1366 T12: 0.0546
REMARK 3 T13: 0.0191 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.1022 L22: 1.1973
REMARK 3 L33: 0.8805 L12: 0.3296
REMARK 3 L13: -0.0350 L23: 0.0127
REMARK 3 S TENSOR
REMARK 3 S11: -0.0723 S12: -0.0547 S13: -0.0073
REMARK 3 S21: -0.0834 S22: -0.0907 S23: -0.0023
REMARK 3 S31: -0.0678 S32: 0.2370 S33: 0.1630
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 64 F 83
REMARK 3 RESIDUE RANGE : F 84 F 107
REMARK 3 RESIDUE RANGE : F 108 F 141
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4533 -30.1997 0.4864
REMARK 3 T TENSOR
REMARK 3 T11: 0.3004 T22: 0.0850
REMARK 3 T33: 0.1229 T12: 0.0281
REMARK 3 T13: 0.0660 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 2.7217 L22: 2.7790
REMARK 3 L33: 0.0797 L12: -1.8233
REMARK 3 L13: -0.3637 L23: 0.4057
REMARK 3 S TENSOR
REMARK 3 S11: -0.1757 S12: -0.0256 S13: 0.0883
REMARK 3 S21: 0.4096 S22: 0.1175 S23: 0.2265
REMARK 3 S31: 0.1053 S32: 0.0262 S33: 0.0582
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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
REMARK 4
REMARK 4 3QSI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000064047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21352
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.080
REMARK 200 RESOLUTION RANGE LOW (A) : 103.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES SODIUM SALT PH 7.5, 2
REMARK 280 %(V/V) PEG 400, 2.0 M AMMONIUM SULFATE, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 73.68950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 73.68950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.70000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, 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 BIOMT1 2 -1.000000 0.000000 0.000000 81.99811
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 103.50232
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 ASP B 61
REMARK 465 GLU B 62
REMARK 465 SER B 63
REMARK 465 GLU B 145
REMARK 465 TYR B 146
REMARK 465 ASN B 147
REMARK 465 GLU B 148
REMARK 465 ASP C 61
REMARK 465 GLU C 62
REMARK 465 SER C 143
REMARK 465 PHE C 144
REMARK 465 GLU C 145
REMARK 465 TYR C 146
REMARK 465 ASN C 147
REMARK 465 GLU C 148
REMARK 465 ASP D 61
REMARK 465 GLU D 62
REMARK 465 SER D 63
REMARK 465 SER D 143
REMARK 465 PHE D 144
REMARK 465 GLU D 145
REMARK 465 TYR D 146
REMARK 465 ASN D 147
REMARK 465 GLU D 148
REMARK 465 ASP A 61
REMARK 465 SER A 142
REMARK 465 SER A 143
REMARK 465 PHE A 144
REMARK 465 GLU A 145
REMARK 465 TYR A 146
REMARK 465 ASN A 147
REMARK 465 GLU A 148
REMARK 465 ASP F 61
REMARK 465 GLU F 62
REMARK 465 SER F 63
REMARK 465 SER F 142
REMARK 465 SER F 143
REMARK 465 PHE F 144
REMARK 465 GLU F 145
REMARK 465 TYR F 146
REMARK 465 ASN F 147
REMARK 465 GLU F 148
REMARK 465 ASP G 61
REMARK 465 GLU G 62
REMARK 465 SER G 63
REMARK 465 SER G 143
REMARK 465 PHE G 144
REMARK 465 GLU G 145
REMARK 465 TYR G 146
REMARK 465 ASN G 147
REMARK 465 GLU G 148
REMARK 465 ASP H 61
REMARK 465 GLU H 62
REMARK 465 SER H 63
REMARK 465 PHE H 144
REMARK 465 GLU H 145
REMARK 465 TYR H 146
REMARK 465 ASN H 147
REMARK 465 GLU H 148
REMARK 465 ASP E 61
REMARK 465 GLU E 62
REMARK 465 SER E 143
REMARK 465 PHE E 144
REMARK 465 GLU E 145
REMARK 465 TYR E 146
REMARK 465 ASN E 147
REMARK 465 GLU E 148
REMARK 465 ASP J 61
REMARK 465 GLU J 62
REMARK 465 SER J 63
REMARK 465 SER J 143
REMARK 465 PHE J 144
REMARK 465 GLU J 145
REMARK 465 TYR J 146
REMARK 465 ASN J 147
REMARK 465 GLU J 148
REMARK 465 ASP I 61
REMARK 465 GLU I 62
REMARK 465 SER I 63
REMARK 465 SER I 143
REMARK 465 PHE I 144
REMARK 465 GLU I 145
REMARK 465 TYR I 146
REMARK 465 ASN I 147
REMARK 465 GLU I 148
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 B 64 CG CD CE NZ
REMARK 470 GLU B 104 CG CD OE1 OE2
REMARK 470 PHE B 118 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 122 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 125 CG CD1 CD2
REMARK 470 LYS B 137 CG CD CE NZ
REMARK 470 GLU D 104 CG CD OE1 OE2
REMARK 470 PHE D 118 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 122 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 137 CG CD CE NZ
REMARK 470 LYS D 140 CG CD CE NZ
REMARK 470 GLU A 62 CG CD OE1 OE2
REMARK 470 LYS A 64 CG CD CE NZ
REMARK 470 ARG A 77 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 78 CG CD OE1 OE2
REMARK 470 PHE A 118 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 126 CG CD OE1 OE2
REMARK 470 ARG A 131 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 140 CG CD CE NZ
REMARK 470 ASN F 116 CG OD1 ND2
REMARK 470 PHE F 118 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU F 119 CG CD OE1 OE2
REMARK 470 GLN F 121 CG CD OE1 NE2
REMARK 470 LYS F 137 CG CD CE NZ
REMARK 470 GLN G 76 CG CD OE1 NE2
REMARK 470 ARG G 77 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 78 CG CD OE1 OE2
REMARK 470 ARG G 82 CG CD NE CZ NH1 NH2
REMARK 470 HIS G 93 CG ND1 CD2 CE1 NE2
REMARK 470 ASN G 116 CG OD1 ND2
REMARK 470 LYS G 137 CG CD CE NZ
REMARK 470 LYS H 64 CG CD CE NZ
REMARK 470 HIS H 75 CG ND1 CD2 CE1 NE2
REMARK 470 ASN H 80 CG OD1 ND2
REMARK 470 GLU H 104 CG CD OE1 OE2
REMARK 470 HIS H 105 CG ND1 CD2 CE1 NE2
REMARK 470 ARG H 131 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 134 CG CD CE NZ
REMARK 470 LYS H 140 CG CD CE NZ
REMARK 470 SER H 143 OG
REMARK 470 SER E 63 OG
REMARK 470 HIS E 93 CG ND1 CD2 CE1 NE2
REMARK 470 GLU E 104 CG CD OE1 OE2
REMARK 470 LYS E 140 CG CD CE NZ
REMARK 470 SER E 142 OG
REMARK 470 HIS J 75 CG ND1 CD2 CE1 NE2
REMARK 470 GLU J 78 CG CD OE1 OE2
REMARK 470 ARG J 82 CG CD NE CZ NH1 NH2
REMARK 470 GLU J 104 CG CD OE1 OE2
REMARK 470 HIS J 105 CG ND1 CD2 CE1 NE2
REMARK 470 ARG J 131 CG CD NE CZ NH1 NH2
REMARK 470 LYS J 137 CG CD CE NZ
REMARK 470 LYS I 64 CG CD CE NZ
REMARK 470 GLN I 76 CG CD OE1 NE2
REMARK 470 GLU I 104 CG CD OE1 OE2
REMARK 470 SER I 117 OG
REMARK 470 GLN I 121 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O LEU A 125 NH1 ARG I 82 3445 2.00
REMARK 500 NH2 ARG F 77 NH1 ARG G 122 4545 2.08
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 CYS B 107 CB CYS B 107 SG -0.101
REMARK 500 GLU C 78 CG GLU C 78 CD 0.096
REMARK 500 CYS I 107 CB CYS I 107 SG -0.100
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 VAL B 69 CG1 - CB - CG2 ANGL. DEV. = 12.7 DEGREES
REMARK 500 LEU B 108 CB - CG - CD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 HIS A 93 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP B 73 -78.64 -65.26
REMARK 500 HIS B 74 -49.47 119.74
REMARK 500 GLU B 78 17.97 55.58
REMARK 500 ASP B 103 -156.58 -147.86
REMARK 500 PHE B 135 125.96 -175.30
REMARK 500 SER B 142 -65.88 -107.68
REMARK 500 GLN C 76 92.17 -66.93
REMARK 500 GLU C 78 -39.24 85.92
REMARK 500 SER C 90 -46.66 -26.51
REMARK 500 GLN C 121 -39.58 -36.89
REMARK 500 ASP D 73 -79.29 -65.26
REMARK 500 HIS D 74 -47.87 120.56
REMARK 500 GLU D 78 19.17 54.89
REMARK 500 ASP D 103 -152.84 -148.92
REMARK 500 PHE D 135 127.82 -172.42
REMARK 500 GLN A 76 88.28 -68.80
REMARK 500 GLU A 78 -40.35 84.67
REMARK 500 SER A 90 -46.60 -27.91
REMARK 500 ALA A 136 99.47 -161.15
REMARK 500 ASP F 73 -79.08 -64.24
REMARK 500 HIS F 74 -45.94 120.42
REMARK 500 GLU F 78 14.90 56.81
REMARK 500 ASP F 103 -157.26 -149.65
REMARK 500 PHE F 135 128.46 -176.14
REMARK 500 GLN G 76 89.52 -66.30
REMARK 500 GLU G 78 -39.64 86.46
REMARK 500 SER G 90 -44.47 -27.06
REMARK 500 ALA G 136 92.43 -162.17
REMARK 500 ASP H 73 -79.82 -65.14
REMARK 500 HIS H 74 -49.70 118.94
REMARK 500 GLU H 78 17.95 56.03
REMARK 500 ASP H 103 -158.65 -149.44
REMARK 500 PHE H 135 127.56 -174.03
REMARK 500 GLU E 78 -40.97 88.63
REMARK 500 GLN E 121 -38.72 -36.97
REMARK 500 ALA E 136 104.90 -163.98
REMARK 500 ASP J 73 -81.07 -71.28
REMARK 500 HIS J 74 -53.04 120.42
REMARK 500 GLU J 78 15.19 59.43
REMARK 500 PHE J 135 125.84 -178.68
REMARK 500 GLN I 76 87.91 -67.69
REMARK 500 GLU I 78 -33.82 78.96
REMARK 500 SER I 90 -49.53 -26.98
REMARK 500 ALA I 136 92.91 -161.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 143 PHE B 144 128.12
REMARK 500 GLY G 91 THR G 92 147.43
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 NI B 5 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 74 NE2
REMARK 620 2 HIS B 101 NE2 88.2
REMARK 620 3 HIS A 88 NE2 90.4 153.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 3 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 88 NE2
REMARK 620 2 HIS A 99 NE2 174.6
REMARK 620 3 HIS A 101 ND1 88.3 94.8
REMARK 620 4 CYS A 107 SG 86.2 89.1 154.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 4 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 99 NE2
REMARK 620 2 HIS C 101 ND1 94.1
REMARK 620 3 CYS C 107 SG 85.6 177.5
REMARK 620 4 HIS D 88 NE2 166.9 87.4 92.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI D 7 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 88 NE2
REMARK 620 2 HIS D 74 NE2 86.7
REMARK 620 3 HIS D 101 NE2 162.3 92.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI F 6 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 74 NE2
REMARK 620 2 HIS F 101 NE2 95.2
REMARK 620 3 HIS E 88 NE2 86.8 178.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI E 8 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 88 NE2
REMARK 620 2 HIS E 99 NE2 166.6
REMARK 620 3 HIS E 101 ND1 82.1 96.3
REMARK 620 4 CYS E 107 SG 88.7 92.5 170.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI H 9 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SO4 G 1 O4
REMARK 620 2 HIS G 88 NE2 105.4
REMARK 620 3 HIS H 74 NE2 144.3 82.2
REMARK 620 4 HIS H 101 NE2 82.2 170.2 95.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI G 2 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 99 NE2
REMARK 620 2 HIS G 101 ND1 91.5
REMARK 620 3 CYS G 107 SG 89.7 177.7
REMARK 620 4 HIS H 88 NE2 168.1 83.6 95.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI I 1 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 99 NE2
REMARK 620 2 HIS I 101 ND1 87.7
REMARK 620 3 CYS I 107 SG 93.5 164.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI I 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI G 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI F 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI D 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI E 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI H 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 5
DBREF 3QSI B 61 148 UNP O25896 NIKR_HELPY 61 148
DBREF 3QSI C 61 148 UNP O25896 NIKR_HELPY 61 148
DBREF 3QSI D 61 148 UNP O25896 NIKR_HELPY 61 148
DBREF 3QSI A 61 148 UNP O25896 NIKR_HELPY 61 148
DBREF 3QSI F 61 148 UNP O25896 NIKR_HELPY 61 148
DBREF 3QSI G 61 148 UNP O25896 NIKR_HELPY 61 148
DBREF 3QSI H 61 148 UNP O25896 NIKR_HELPY 61 148
DBREF 3QSI E 61 148 UNP O25896 NIKR_HELPY 61 148
DBREF 3QSI J 61 148 UNP O25896 NIKR_HELPY 61 148
DBREF 3QSI I 61 148 UNP O25896 NIKR_HELPY 61 148
SEQRES 1 B 88 ASP GLU SER LYS ILE ALA VAL LEU VAL VAL ILE TYR ASP
SEQRES 2 B 88 HIS HIS GLN ARG GLU LEU ASN GLN ARG MET ILE ASP ILE
SEQRES 3 B 88 GLN HIS ALA SER GLY THR HIS VAL LEU CYS THR THR HIS
SEQRES 4 B 88 ILE HIS MET ASP GLU HIS ASN CYS LEU GLU THR ILE ILE
SEQRES 5 B 88 LEU GLN GLY ASN SER PHE GLU ILE GLN ARG LEU GLN LEU
SEQRES 6 B 88 GLU ILE GLY GLY LEU ARG GLY VAL LYS PHE ALA LYS LEU
SEQRES 7 B 88 THR LYS ALA SER SER PHE GLU TYR ASN GLU
SEQRES 1 C 88 ASP GLU SER LYS ILE ALA VAL LEU VAL VAL ILE TYR ASP
SEQRES 2 C 88 HIS HIS GLN ARG GLU LEU ASN GLN ARG MET ILE ASP ILE
SEQRES 3 C 88 GLN HIS ALA SER GLY THR HIS VAL LEU CYS THR THR HIS
SEQRES 4 C 88 ILE HIS MET ASP GLU HIS ASN CYS LEU GLU THR ILE ILE
SEQRES 5 C 88 LEU GLN GLY ASN SER PHE GLU ILE GLN ARG LEU GLN LEU
SEQRES 6 C 88 GLU ILE GLY GLY LEU ARG GLY VAL LYS PHE ALA LYS LEU
SEQRES 7 C 88 THR LYS ALA SER SER PHE GLU TYR ASN GLU
SEQRES 1 D 88 ASP GLU SER LYS ILE ALA VAL LEU VAL VAL ILE TYR ASP
SEQRES 2 D 88 HIS HIS GLN ARG GLU LEU ASN GLN ARG MET ILE ASP ILE
SEQRES 3 D 88 GLN HIS ALA SER GLY THR HIS VAL LEU CYS THR THR HIS
SEQRES 4 D 88 ILE HIS MET ASP GLU HIS ASN CYS LEU GLU THR ILE ILE
SEQRES 5 D 88 LEU GLN GLY ASN SER PHE GLU ILE GLN ARG LEU GLN LEU
SEQRES 6 D 88 GLU ILE GLY GLY LEU ARG GLY VAL LYS PHE ALA LYS LEU
SEQRES 7 D 88 THR LYS ALA SER SER PHE GLU TYR ASN GLU
SEQRES 1 A 88 ASP GLU SER LYS ILE ALA VAL LEU VAL VAL ILE TYR ASP
SEQRES 2 A 88 HIS HIS GLN ARG GLU LEU ASN GLN ARG MET ILE ASP ILE
SEQRES 3 A 88 GLN HIS ALA SER GLY THR HIS VAL LEU CYS THR THR HIS
SEQRES 4 A 88 ILE HIS MET ASP GLU HIS ASN CYS LEU GLU THR ILE ILE
SEQRES 5 A 88 LEU GLN GLY ASN SER PHE GLU ILE GLN ARG LEU GLN LEU
SEQRES 6 A 88 GLU ILE GLY GLY LEU ARG GLY VAL LYS PHE ALA LYS LEU
SEQRES 7 A 88 THR LYS ALA SER SER PHE GLU TYR ASN GLU
SEQRES 1 F 88 ASP GLU SER LYS ILE ALA VAL LEU VAL VAL ILE TYR ASP
SEQRES 2 F 88 HIS HIS GLN ARG GLU LEU ASN GLN ARG MET ILE ASP ILE
SEQRES 3 F 88 GLN HIS ALA SER GLY THR HIS VAL LEU CYS THR THR HIS
SEQRES 4 F 88 ILE HIS MET ASP GLU HIS ASN CYS LEU GLU THR ILE ILE
SEQRES 5 F 88 LEU GLN GLY ASN SER PHE GLU ILE GLN ARG LEU GLN LEU
SEQRES 6 F 88 GLU ILE GLY GLY LEU ARG GLY VAL LYS PHE ALA LYS LEU
SEQRES 7 F 88 THR LYS ALA SER SER PHE GLU TYR ASN GLU
SEQRES 1 G 88 ASP GLU SER LYS ILE ALA VAL LEU VAL VAL ILE TYR ASP
SEQRES 2 G 88 HIS HIS GLN ARG GLU LEU ASN GLN ARG MET ILE ASP ILE
SEQRES 3 G 88 GLN HIS ALA SER GLY THR HIS VAL LEU CYS THR THR HIS
SEQRES 4 G 88 ILE HIS MET ASP GLU HIS ASN CYS LEU GLU THR ILE ILE
SEQRES 5 G 88 LEU GLN GLY ASN SER PHE GLU ILE GLN ARG LEU GLN LEU
SEQRES 6 G 88 GLU ILE GLY GLY LEU ARG GLY VAL LYS PHE ALA LYS LEU
SEQRES 7 G 88 THR LYS ALA SER SER PHE GLU TYR ASN GLU
SEQRES 1 H 88 ASP GLU SER LYS ILE ALA VAL LEU VAL VAL ILE TYR ASP
SEQRES 2 H 88 HIS HIS GLN ARG GLU LEU ASN GLN ARG MET ILE ASP ILE
SEQRES 3 H 88 GLN HIS ALA SER GLY THR HIS VAL LEU CYS THR THR HIS
SEQRES 4 H 88 ILE HIS MET ASP GLU HIS ASN CYS LEU GLU THR ILE ILE
SEQRES 5 H 88 LEU GLN GLY ASN SER PHE GLU ILE GLN ARG LEU GLN LEU
SEQRES 6 H 88 GLU ILE GLY GLY LEU ARG GLY VAL LYS PHE ALA LYS LEU
SEQRES 7 H 88 THR LYS ALA SER SER PHE GLU TYR ASN GLU
SEQRES 1 E 88 ASP GLU SER LYS ILE ALA VAL LEU VAL VAL ILE TYR ASP
SEQRES 2 E 88 HIS HIS GLN ARG GLU LEU ASN GLN ARG MET ILE ASP ILE
SEQRES 3 E 88 GLN HIS ALA SER GLY THR HIS VAL LEU CYS THR THR HIS
SEQRES 4 E 88 ILE HIS MET ASP GLU HIS ASN CYS LEU GLU THR ILE ILE
SEQRES 5 E 88 LEU GLN GLY ASN SER PHE GLU ILE GLN ARG LEU GLN LEU
SEQRES 6 E 88 GLU ILE GLY GLY LEU ARG GLY VAL LYS PHE ALA LYS LEU
SEQRES 7 E 88 THR LYS ALA SER SER PHE GLU TYR ASN GLU
SEQRES 1 J 88 ASP GLU SER LYS ILE ALA VAL LEU VAL VAL ILE TYR ASP
SEQRES 2 J 88 HIS HIS GLN ARG GLU LEU ASN GLN ARG MET ILE ASP ILE
SEQRES 3 J 88 GLN HIS ALA SER GLY THR HIS VAL LEU CYS THR THR HIS
SEQRES 4 J 88 ILE HIS MET ASP GLU HIS ASN CYS LEU GLU THR ILE ILE
SEQRES 5 J 88 LEU GLN GLY ASN SER PHE GLU ILE GLN ARG LEU GLN LEU
SEQRES 6 J 88 GLU ILE GLY GLY LEU ARG GLY VAL LYS PHE ALA LYS LEU
SEQRES 7 J 88 THR LYS ALA SER SER PHE GLU TYR ASN GLU
SEQRES 1 I 88 ASP GLU SER LYS ILE ALA VAL LEU VAL VAL ILE TYR ASP
SEQRES 2 I 88 HIS HIS GLN ARG GLU LEU ASN GLN ARG MET ILE ASP ILE
SEQRES 3 I 88 GLN HIS ALA SER GLY THR HIS VAL LEU CYS THR THR HIS
SEQRES 4 I 88 ILE HIS MET ASP GLU HIS ASN CYS LEU GLU THR ILE ILE
SEQRES 5 I 88 LEU GLN GLY ASN SER PHE GLU ILE GLN ARG LEU GLN LEU
SEQRES 6 I 88 GLU ILE GLY GLY LEU ARG GLY VAL LYS PHE ALA LYS LEU
SEQRES 7 I 88 THR LYS ALA SER SER PHE GLU TYR ASN GLU
HET NI B 5 1
HET SO4 B 4 5
HET NI C 4 1
HET SO4 C 5 5
HET NI D 7 1
HET NI A 3 1
HET NI F 6 1
HET SO4 F 2 5
HET NI G 2 1
HET SO4 G 1 5
HET NI H 9 1
HET NI E 8 1
HET SO4 E 3 5
HET NI I 1 1
HETNAM NI NICKEL (II) ION
HETNAM SO4 SULFATE ION
FORMUL 11 NI 9(NI 2+)
FORMUL 12 SO4 5(O4 S 2-)
HELIX 1 1 GLU B 78 SER B 90 1 13
HELIX 2 2 ASN B 116 LEU B 130 1 15
HELIX 3 3 GLU C 78 GLY C 91 1 14
HELIX 4 4 ASN C 116 GLY C 129 1 14
HELIX 5 5 GLU D 78 SER D 90 1 13
HELIX 6 6 ASN D 116 LEU D 130 1 15
HELIX 7 7 GLU A 78 GLY A 91 1 14
HELIX 8 8 ASN A 116 GLY A 129 1 14
HELIX 9 9 GLU F 78 SER F 90 1 13
HELIX 10 10 ASN F 116 LEU F 130 1 15
HELIX 11 11 GLU G 78 GLY G 91 1 14
HELIX 12 12 ASN G 116 GLY G 129 1 14
HELIX 13 13 GLU H 78 SER H 90 1 13
HELIX 14 14 ASN H 116 LEU H 130 1 15
HELIX 15 15 GLU E 78 GLY E 91 1 14
HELIX 16 16 ASN E 116 GLY E 129 1 14
HELIX 17 17 GLU J 78 SER J 90 1 13
HELIX 18 18 ASN J 116 LEU J 130 1 15
HELIX 19 19 GLU I 78 GLY I 91 1 14
HELIX 20 20 ASN I 116 GLY I 129 1 14
SHEET 1 A 8 VAL B 133 LYS B 140 0
SHEET 2 A 8 ALA B 66 TYR B 72 -1 N VAL B 67 O THR B 139
SHEET 3 A 8 CYS B 107 GLN B 114 -1 O GLU B 109 N VAL B 70
SHEET 4 A 8 HIS B 93 HIS B 101 -1 N HIS B 93 O GLN B 114
SHEET 5 A 8 HIS A 93 ASP A 103 -1 O HIS A 99 N THR B 97
SHEET 6 A 8 ASN A 106 GLY A 115 -1 O THR A 110 N THR A 98
SHEET 7 A 8 LYS A 64 TYR A 72 -1 N ALA A 66 O LEU A 113
SHEET 8 A 8 VAL A 133 ALA A 141 -1 O LYS A 134 N ILE A 71
SHEET 1 B 8 VAL C 133 ALA C 141 0
SHEET 2 B 8 LYS C 64 TYR C 72 -1 N VAL C 69 O LYS C 137
SHEET 3 B 8 ASN C 106 GLY C 115 -1 O LEU C 113 N ALA C 66
SHEET 4 B 8 HIS C 93 ASP C 103 -1 N THR C 98 O THR C 110
SHEET 5 B 8 HIS D 93 HIS D 101 -1 O THR D 97 N HIS C 99
SHEET 6 B 8 CYS D 107 GLN D 114 -1 O GLN D 114 N HIS D 93
SHEET 7 B 8 ILE D 65 TYR D 72 -1 N VAL D 70 O GLU D 109
SHEET 8 B 8 VAL D 133 LYS D 140 -1 O THR D 139 N VAL D 67
SHEET 1 C 8 VAL F 133 LYS F 140 0
SHEET 2 C 8 ILE F 65 TYR F 72 -1 N VAL F 67 O THR F 139
SHEET 3 C 8 CYS F 107 GLN F 114 -1 O GLU F 109 N VAL F 70
SHEET 4 C 8 HIS F 93 HIS F 101 -1 N THR F 98 O THR F 110
SHEET 5 C 8 HIS E 93 ASP E 103 -1 O HIS E 99 N THR F 97
SHEET 6 C 8 ASN E 106 GLY E 115 -1 O THR E 110 N THR E 98
SHEET 7 C 8 LYS E 64 TYR E 72 -1 N TYR E 72 O CYS E 107
SHEET 8 C 8 VAL E 133 LYS E 140 -1 O THR E 139 N VAL E 67
SHEET 1 D 8 VAL G 133 ALA G 141 0
SHEET 2 D 8 ILE G 65 TYR G 72 -1 N VAL G 69 O LYS G 137
SHEET 3 D 8 ASN G 106 GLN G 114 -1 O LEU G 113 N ALA G 66
SHEET 4 D 8 HIS G 93 ASP G 103 -1 N ILE G 100 O LEU G 108
SHEET 5 D 8 HIS H 93 HIS H 101 -1 O THR H 97 N HIS G 99
SHEET 6 D 8 CYS H 107 GLN H 114 -1 O GLN H 114 N HIS H 93
SHEET 7 D 8 ILE H 65 TYR H 72 -1 N VAL H 70 O GLU H 109
SHEET 8 D 8 VAL H 133 LYS H 140 -1 O THR H 139 N VAL H 67
SHEET 1 E 4 HIS J 93 HIS J 101 0
SHEET 2 E 4 CYS J 107 GLN J 114 -1 O ILE J 112 N CYS J 96
SHEET 3 E 4 ALA J 66 TYR J 72 -1 N VAL J 70 O GLU J 109
SHEET 4 E 4 PHE J 135 LYS J 140 -1 O THR J 139 N VAL J 67
SHEET 1 F 4 HIS I 93 ASP I 103 0
SHEET 2 F 4 ASN I 106 GLN I 114 -1 O THR I 110 N THR I 98
SHEET 3 F 4 ILE I 65 TYR I 72 -1 N ALA I 66 O LEU I 113
SHEET 4 F 4 VAL I 133 LYS I 140 -1 O LYS I 134 N ILE I 71
LINK NI NI B 5 NE2 HIS B 74 1555 1555 2.04
LINK NI NI B 5 NE2 HIS B 101 1555 1555 2.12
LINK NI NI B 5 NE2 HIS A 88 1555 1555 2.12
LINK NE2 HIS B 88 NI NI A 3 1555 1555 2.03
LINK NI NI C 4 NE2 HIS C 99 1555 1555 2.00
LINK NI NI C 4 ND1 HIS C 101 1555 1555 2.11
LINK NI NI C 4 SG CYS C 107 1555 1555 2.29
LINK NI NI C 4 NE2 HIS D 88 1555 1555 2.03
LINK NE2 HIS C 88 NI NI D 7 1555 1555 2.06
LINK NI NI D 7 NE2 HIS D 74 1555 1555 2.08
LINK NI NI D 7 NE2 HIS D 101 1555 1555 2.04
LINK NI NI A 3 NE2 HIS A 99 1555 1555 2.01
LINK NI NI A 3 ND1 HIS A 101 1555 1555 2.07
LINK NI NI A 3 SG CYS A 107 1555 1555 2.31
LINK NI NI F 6 NE2 HIS F 74 1555 1555 2.07
LINK NI NI F 6 NE2 HIS F 101 1555 1555 1.99
LINK NI NI F 6 NE2 HIS E 88 1555 1555 2.02
LINK NE2 HIS F 88 NI NI E 8 1555 1555 2.06
LINK O4 SO4 G 1 NI NI H 9 1555 1555 2.59
LINK NI NI G 2 NE2 HIS G 99 1555 1555 2.01
LINK NI NI G 2 ND1 HIS G 101 1555 1555 2.12
LINK NI NI G 2 SG CYS G 107 1555 1555 2.31
LINK NI NI G 2 NE2 HIS H 88 1555 1555 2.04
LINK NE2 HIS G 88 NI NI H 9 1555 1555 2.02
LINK NI NI H 9 NE2 HIS H 74 1555 1555 2.06
LINK NI NI H 9 NE2 HIS H 101 1555 1555 2.01
LINK NI NI E 8 NE2 HIS E 99 1555 1555 1.99
LINK NI NI E 8 ND1 HIS E 101 1555 1555 2.07
LINK NI NI E 8 SG CYS E 107 1555 1555 2.33
LINK NI NI I 1 NE2 HIS I 99 1555 1555 2.01
LINK NI NI I 1 ND1 HIS I 101 1555 1555 2.16
LINK NI NI I 1 SG CYS I 107 1555 1555 2.24
SITE 1 AC1 5 HIS I 99 HIS I 101 CYS I 107 ILE J 84
SITE 2 AC1 5 HIS J 88
SITE 1 AC2 5 HIS G 99 HIS G 101 CYS G 107 ILE H 84
SITE 2 AC2 5 HIS H 88
SITE 1 AC3 5 HIS A 99 HIS A 101 CYS A 107 ILE B 84
SITE 2 AC3 5 HIS B 88
SITE 1 AC4 5 HIS C 99 HIS C 101 CYS C 107 ILE D 84
SITE 2 AC4 5 HIS D 88
SITE 1 AC5 3 HIS A 88 HIS B 74 HIS B 101
SITE 1 AC6 3 HIS E 88 HIS F 74 HIS F 101
SITE 1 AC7 3 HIS C 88 HIS D 74 HIS D 101
SITE 1 AC8 5 HIS E 99 HIS E 101 CYS E 107 ILE F 84
SITE 2 AC8 5 HIS F 88
SITE 1 AC9 4 SO4 G 1 HIS G 88 HIS H 74 HIS H 101
SITE 1 BC1 8 ARG F 131 GLN G 87 HIS G 88 THR G 92
SITE 2 BC1 8 HIS G 93 VAL G 94 NI H 9 HIS H 101
SITE 1 BC2 1 ARG F 122
SITE 1 BC3 1 ARG E 77
SITE 1 BC4 4 LYS C 137 LEU C 138 THR C 139 LYS C 140
CRYST1 147.379 79.400 122.423 90.00 122.28 90.00 C 1 2 1 40
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 0.006785 0.000000 0.004286 0.00000
SCALE2 0.000000 0.012594 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009662 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
