HEADER PROTEIN BINDING 25-NOV-05 2C7N
TITLE HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAB GUANINE NUCLEOTIDE EXCHANGE FACTOR 1;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 FRAGMENT: TWO UBIQUTIN BINDING DOMAINS, RESIDUES 1-74;
COMPND 5 SYNONYM: RABEX-5, GEF 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: UBIQUITIN;
COMPND 9 CHAIN: B, D, F, H, J, L;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 10 ORGANISM_COMMON: BOVINE;
SOURCE 11 ORGANISM_TAXID: 9913;
SOURCE 12 OTHER_DETAILS: BOSTON BIOCHEM
KEYWDS PROTEIN-BINDING, UBIQUITIN BINDING DOMAIN, ENDOCYTOSIS, NUCLEAR
KEYWDS 2 PROTEIN, POLYPROTEIN, UBIQUITIN COMPLEX, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR L.PENENGO,M.MAPELLI,A.G.MURACHELLI,S.CONFALIONERI,L.MAGRI,
AUTHOR 2 A.MUSACCHIO,P.P.DI FIORE,S.POLO,T.R.SCHNEIDER
REVDAT 7 08-MAY-19 2C7N 1 REMARK
REVDAT 6 13-JUL-11 2C7N 1 VERSN
REVDAT 5 24-FEB-09 2C7N 1 VERSN
REVDAT 4 11-MAY-06 2C7N 1 JRNL
REVDAT 3 29-MAR-06 2C7N 1 JRNL
REVDAT 2 01-MAR-06 2C7N 1 AUTHOR JRNL
REVDAT 1 15-FEB-06 2C7N 0
JRNL AUTH L.PENENGO,M.MAPELLI,A.G.MURACHELLI,S.CONFALONIERI,L.MAGRI,
JRNL AUTH 2 A.MUSACCHIO,P.P.DI FIORE,S.POLO,T.R.SCHNEIDER
JRNL TITL CRYSTAL STRUCTURE OF THE UBIQUITIN BINDING DOMAINS OF
JRNL TITL 2 RABEX-5 REVEALS TWO MODES OF INTERACTION WITH UBIQUITIN.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 124 1183 2006
JRNL REFN ISSN 0092-8674
JRNL PMID 16499958
JRNL DOI 10.1016/J.CELL.2006.02.020
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 53884
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2876
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2391
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 116
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6178
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 253
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) : 44.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.29000
REMARK 3 B22 (A**2) : 0.23000
REMARK 3 B33 (A**2) : -0.58000
REMARK 3 B12 (A**2) : -0.43000
REMARK 3 B13 (A**2) : 0.02000
REMARK 3 B23 (A**2) : -0.10000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.206
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.182
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.127
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6284 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8445 ; 1.768 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 742 ; 6.077 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 322 ;34.686 ;25.093
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1228 ;18.430 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;20.611 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 895 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4735 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2621 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4171 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 257 ; 0.145 ; 0.200
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): 166 ; 0.244 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 67 ; 0.163 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3904 ; 0.994 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6024 ; 1.517 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2782 ; 2.858 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2421 ; 4.268 ; 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 : 18
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 18 A 44
REMARK 3 ORIGIN FOR THE GROUP (A): -18.0468 -51.2292 -15.3409
REMARK 3 T TENSOR
REMARK 3 T11: -0.0920 T22: -0.0063
REMARK 3 T33: -0.2044 T12: 0.0184
REMARK 3 T13: 0.0069 T23: -0.0689
REMARK 3 L TENSOR
REMARK 3 L11: 15.5500 L22: 6.9949
REMARK 3 L33: 14.8104 L12: 7.2259
REMARK 3 L13: 8.8888 L23: 6.4419
REMARK 3 S TENSOR
REMARK 3 S11: 0.0172 S12: 0.4686 S13: -0.4289
REMARK 3 S21: -0.5265 S22: -0.1584 S23: 0.0233
REMARK 3 S31: 0.9752 S32: -0.5185 S33: 0.1411
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 : A 45 A 73
REMARK 3 ORIGIN FOR THE GROUP (A): 0.6188 -44.4437 9.3067
REMARK 3 T TENSOR
REMARK 3 T11: -0.3344 T22: -0.2196
REMARK 3 T33: -0.2568 T12: 0.0011
REMARK 3 T13: 0.0565 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 14.6039 L22: 3.7117
REMARK 3 L33: 18.4930 L12: 1.8347
REMARK 3 L13: 13.3957 L23: 1.1485
REMARK 3 S TENSOR
REMARK 3 S11: 0.1754 S12: -0.7411 S13: -0.0286
REMARK 3 S21: 0.5700 S22: -0.2457 S23: -0.0895
REMARK 3 S31: 0.2021 S32: -0.0259 S33: 0.0703
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 : B 1 B 73
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2759 -50.4260 -1.1809
REMARK 3 T TENSOR
REMARK 3 T11: -0.3517 T22: -0.2805
REMARK 3 T33: -0.2370 T12: 0.0263
REMARK 3 T13: 0.0121 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 5.0298 L22: 5.2359
REMARK 3 L33: 3.2402 L12: 2.2735
REMARK 3 L13: -0.4096 L23: 1.2753
REMARK 3 S TENSOR
REMARK 3 S11: -0.0428 S12: 0.0929 S13: -0.4328
REMARK 3 S21: -0.0779 S22: 0.0365 S23: -0.2054
REMARK 3 S31: 0.2182 S32: 0.1527 S33: 0.0063
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 : C 17 C 44
REMARK 3 ORIGIN FOR THE GROUP (A): -40.0776 -98.3394 18.7654
REMARK 3 T TENSOR
REMARK 3 T11: -0.1236 T22: 0.0388
REMARK 3 T33: -0.2027 T12: -0.0010
REMARK 3 T13: -0.0142 T23: -0.0909
REMARK 3 L TENSOR
REMARK 3 L11: 15.7936 L22: 7.3704
REMARK 3 L33: 15.0380 L12: -5.9115
REMARK 3 L13: -10.3939 L23: 6.8735
REMARK 3 S TENSOR
REMARK 3 S11: -0.0097 S12: -0.5257 S13: 0.5520
REMARK 3 S21: 0.3794 S22: -0.1556 S23: 0.1367
REMARK 3 S31: -0.7936 S32: -0.6535 S33: 0.1652
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 : C 45 C 73
REMARK 3 ORIGIN FOR THE GROUP (A): -21.0935-105.4336 -5.9608
REMARK 3 T TENSOR
REMARK 3 T11: -0.3482 T22: -0.2380
REMARK 3 T33: -0.2606 T12: 0.0041
REMARK 3 T13: -0.0522 T23: 0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 17.8515 L22: 3.7495
REMARK 3 L33: 17.2246 L12: -3.6837
REMARK 3 L13: -13.9520 L23: 3.1207
REMARK 3 S TENSOR
REMARK 3 S11: 0.3304 S12: 0.7721 S13: 0.1635
REMARK 3 S21: -0.4927 S22: -0.2630 S23: -0.0440
REMARK 3 S31: -0.2902 S32: -0.0730 S33: -0.0674
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 : D 1 D 73
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4984 -99.3825 4.5009
REMARK 3 T TENSOR
REMARK 3 T11: -0.3519 T22: -0.2742
REMARK 3 T33: -0.2244 T12: -0.0238
REMARK 3 T13: -0.0108 T23: -0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 5.0371 L22: 5.1351
REMARK 3 L33: 2.9623 L12: -2.1453
REMARK 3 L13: 0.2062 L23: 1.3971
REMARK 3 S TENSOR
REMARK 3 S11: -0.0759 S12: -0.1310 S13: 0.4331
REMARK 3 S21: 0.1135 S22: 0.0470 S23: -0.1847
REMARK 3 S31: -0.1895 S32: 0.1160 S33: 0.0289
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 : E 17 E 44
REMARK 3 ORIGIN FOR THE GROUP (A): -42.5476 -70.0227 -4.0087
REMARK 3 T TENSOR
REMARK 3 T11: -0.0369 T22: -0.1305
REMARK 3 T33: 0.0781 T12: -0.0868
REMARK 3 T13: 0.0764 T23: -0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 3.7231 L22: 21.2816
REMARK 3 L33: 7.8313 L12: -5.1512
REMARK 3 L13: -1.8224 L23: 3.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.1976 S12: 0.1151 S13: -0.4923
REMARK 3 S21: -0.4271 S22: 0.1100 S23: 0.0733
REMARK 3 S31: 0.9991 S32: -0.2025 S33: 0.0876
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 : E 45 E 65
REMARK 3 ORIGIN FOR THE GROUP (A): -33.8641 -92.9460 -11.9720
REMARK 3 T TENSOR
REMARK 3 T11: -0.0790 T22: -0.1048
REMARK 3 T33: 0.1132 T12: -0.0380
REMARK 3 T13: 0.0124 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 13.2422 L22: 37.9589
REMARK 3 L33: 17.2086 L12: -13.4181
REMARK 3 L13: -7.6935 L23: 15.4931
REMARK 3 S TENSOR
REMARK 3 S11: -0.1084 S12: 0.5411 S13: -1.2138
REMARK 3 S21: 0.0812 S22: -0.1600 S23: 1.2643
REMARK 3 S31: 0.4730 S32: -0.6644 S33: 0.2684
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 : F 1 F 73
REMARK 3 ORIGIN FOR THE GROUP (A): -23.4036 -85.7545 -18.7282
REMARK 3 T TENSOR
REMARK 3 T11: 0.0346 T22: 0.0311
REMARK 3 T33: -0.1218 T12: -0.0092
REMARK 3 T13: 0.0795 T23: 0.0674
REMARK 3 L TENSOR
REMARK 3 L11: 7.5836 L22: 11.1096
REMARK 3 L33: 6.5274 L12: -1.8209
REMARK 3 L13: -0.7207 L23: -4.0758
REMARK 3 S TENSOR
REMARK 3 S11: 0.3025 S12: 1.2056 S13: 0.2439
REMARK 3 S21: -0.8100 S22: -0.4076 S23: -0.5308
REMARK 3 S31: -0.1513 S32: 0.3970 S33: 0.1051
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 : G 17 G 44
REMARK 3 ORIGIN FOR THE GROUP (A): -64.4481 -79.8209 7.3119
REMARK 3 T TENSOR
REMARK 3 T11: -0.0498 T22: -0.1367
REMARK 3 T33: 0.0169 T12: 0.0933
REMARK 3 T13: -0.0647 T23: -0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 6.8939 L22: 20.4493
REMARK 3 L33: 10.9750 L12: 5.3331
REMARK 3 L13: 4.7908 L23: 4.4316
REMARK 3 S TENSOR
REMARK 3 S11: -0.1678 S12: -0.0773 S13: 0.3932
REMARK 3 S21: 0.2532 S22: 0.0200 S23: 0.2420
REMARK 3 S31: -0.8785 S32: -0.0099 S33: 0.1478
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 : G 45 G 71
REMARK 3 ORIGIN FOR THE GROUP (A): -54.9731 -53.9227 18.0949
REMARK 3 T TENSOR
REMARK 3 T11: 0.0579 T22: 0.0191
REMARK 3 T33: 0.2110 T12: 0.0431
REMARK 3 T13: 0.0448 T23: -0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 10.4676 L22: 44.9093
REMARK 3 L33: 20.3898 L12: 11.4294
REMARK 3 L13: 7.7404 L23: 18.0818
REMARK 3 S TENSOR
REMARK 3 S11: 0.1894 S12: -0.9485 S13: 1.5074
REMARK 3 S21: 0.9181 S22: -0.6230 S23: 0.7128
REMARK 3 S31: -1.1138 S32: -0.5232 S33: 0.4336
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 73
REMARK 3 ORIGIN FOR THE GROUP (A): -45.6520 -64.2170 22.0978
REMARK 3 T TENSOR
REMARK 3 T11: 0.0528 T22: 0.0284
REMARK 3 T33: -0.0804 T12: 0.0072
REMARK 3 T13: -0.0802 T23: 0.0631
REMARK 3 L TENSOR
REMARK 3 L11: 7.1350 L22: 8.7981
REMARK 3 L33: 8.8214 L12: 1.2204
REMARK 3 L13: 0.6664 L23: -4.5310
REMARK 3 S TENSOR
REMARK 3 S11: 0.2647 S12: -1.1828 S13: -0.2610
REMARK 3 S21: 0.8372 S22: -0.3677 S23: -0.6880
REMARK 3 S31: 0.1113 S32: 0.4464 S33: 0.1030
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 17 I 44
REMARK 3 ORIGIN FOR THE GROUP (A): -55.7560 -79.1740 31.8523
REMARK 3 T TENSOR
REMARK 3 T11: 0.5177 T22: 0.3977
REMARK 3 T33: 0.2290 T12: -0.3000
REMARK 3 T13: -0.1398 T23: 0.3219
REMARK 3 L TENSOR
REMARK 3 L11: 4.9021 L22: 18.1721
REMARK 3 L33: 14.3553 L12: -8.6369
REMARK 3 L13: 3.9669 L23: -12.7280
REMARK 3 S TENSOR
REMARK 3 S11: 0.5301 S12: -0.1127 S13: 0.2883
REMARK 3 S21: 0.4316 S22: 0.2967 S23: 0.9003
REMARK 3 S31: 0.9541 S32: -1.2556 S33: -0.8268
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 45 I 74
REMARK 3 ORIGIN FOR THE GROUP (A): -48.6809-106.4560 46.4720
REMARK 3 T TENSOR
REMARK 3 T11: 0.7281 T22: 0.2105
REMARK 3 T33: 0.0509 T12: -0.0660
REMARK 3 T13: 0.1212 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 5.9823 L22: 52.6944
REMARK 3 L33: 12.3307 L12: -10.4971
REMARK 3 L13: 5.4844 L23: -18.6356
REMARK 3 S TENSOR
REMARK 3 S11: 0.1639 S12: 0.1440 S13: -1.2076
REMARK 3 S21: 1.1372 S22: 0.5389 S23: 1.2446
REMARK 3 S31: 0.9571 S32: -0.1883 S33: -0.7027
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 72
REMARK 3 ORIGIN FOR THE GROUP (A): -37.0476-100.4013 38.9220
REMARK 3 T TENSOR
REMARK 3 T11: 0.3650 T22: 0.1997
REMARK 3 T33: -0.1395 T12: 0.0868
REMARK 3 T13: -0.0434 T23: -0.0554
REMARK 3 L TENSOR
REMARK 3 L11: 5.8396 L22: 5.5938
REMARK 3 L33: 13.2738 L12: -0.9024
REMARK 3 L13: 1.0712 L23: -0.1629
REMARK 3 S TENSOR
REMARK 3 S11: 0.0210 S12: -0.1059 S13: -0.3813
REMARK 3 S21: 1.0995 S22: 0.2367 S23: -0.3311
REMARK 3 S31: 0.6118 S32: 0.8079 S33: -0.2576
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 17 K 44
REMARK 3 ORIGIN FOR THE GROUP (A): -55.5358-101.6445 62.5384
REMARK 3 T TENSOR
REMARK 3 T11: 0.4581 T22: 0.4540
REMARK 3 T33: 0.1948 T12: 0.1596
REMARK 3 T13: 0.0840 T23: 0.2905
REMARK 3 L TENSOR
REMARK 3 L11: 3.2203 L22: 19.2918
REMARK 3 L33: 9.8969 L12: 7.3690
REMARK 3 L13: -5.6211 L23: -12.4083
REMARK 3 S TENSOR
REMARK 3 S11: 0.4065 S12: 0.0540 S13: -0.4291
REMARK 3 S21: -0.4510 S22: 0.5037 S23: 0.6949
REMARK 3 S31: -0.5647 S32: -0.9782 S33: -0.9102
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : K 45 K 65
REMARK 3 ORIGIN FOR THE GROUP (A): -50.4980 -80.2523 49.6011
REMARK 3 T TENSOR
REMARK 3 T11: 0.5127 T22: 0.2049
REMARK 3 T33: -0.1171 T12: 0.0413
REMARK 3 T13: -0.1913 T23: 0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 7.1938 L22: 59.9669
REMARK 3 L33: 16.5289 L12: 8.7221
REMARK 3 L13: -3.6076 L23: -20.1653
REMARK 3 S TENSOR
REMARK 3 S11: -0.0576 S12: -0.1109 S13: 0.8676
REMARK 3 S21: -1.2157 S22: 0.4524 S23: 1.2356
REMARK 3 S31: -0.8304 S32: -0.2898 S33: -0.3948
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 73
REMARK 3 ORIGIN FOR THE GROUP (A): -37.1870 -79.7658 55.2491
REMARK 3 T TENSOR
REMARK 3 T11: 0.3765 T22: 0.2272
REMARK 3 T33: -0.1225 T12: -0.0624
REMARK 3 T13: 0.0139 T23: -0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 5.8304 L22: 4.7902
REMARK 3 L33: 11.8340 L12: 1.0907
REMARK 3 L13: 0.0144 L23: -0.3747
REMARK 3 S TENSOR
REMARK 3 S11: -0.0871 S12: 0.2033 S13: 0.5267
REMARK 3 S21: -1.0429 S22: 0.1945 S23: -0.1256
REMARK 3 S31: -0.6244 S32: 0.6913 S33: -0.1075
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. RESIDUES 1-17 ARE DISORDERED IN ALL COPIES OF RABEX-5
REMARK 3 1-74. THE C-TERMINUS OF RABEX-5 1-74 IS ORDERED TO A VARIABLE
REMARK 3 DEGREE. RESIDUES 74-76 OF UBIQUTIN ARE DISORDERED IN ALL COPIES
REMARK 4
REMARK 4 2C7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1290026561.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57954
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.03000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.17000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: HKL2MAP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP 300NL PLUS 300NL 0.2M
REMARK 280 AMMONIUM ACETATE 0.1M NACITRATE PH 6.5 25% PEG400, PH 6.50,
REMARK 280 VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 300 REMARK: THE QUATERNARY STRUCTURE FOR THIS ENTRY IS
REMARK 300 NOT RELEVANTSINCE THE COMPLEX IS ONLY MADE UP OF
REMARK 300 FRAGMENTS OF RABEX-5IN COMPLEX WITH UBIQUITIN.
REMARK 300 HOWEVER, THESE REMARKSONLY INDICATE THE COMPLEX AS
REMARK 300 SEEN IN THE PDB FILE, ANDDO NOT HAVE RELEVANCE
REMARK 300 TO THE BIOLOGICAL STATE OF THEMOLECULE.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.9 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.4 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.9 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.2 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.9 KCAL/MOL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 1330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.7 KCAL/MOL
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 INVOLVED IN THE ATP-DEPENDENT SELECTIVE DEGRADATION OF
REMARK 400 CELLULAR PROTEINS, THE MAINTENANCE OF CHROMATIN STRUCTURE,
REMARK 400 THE REGULATION OF GENE EXPRESSION, THE STRESS RESPONSE, AND
REMARK 400 RIBOSOME BIOGENESIS
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 MET A 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
REMARK 465 LYS A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 GLY A 9
REMARK 465 ILE A 10
REMARK 465 HIS A 11
REMARK 465 VAL A 12
REMARK 465 ASP A 13
REMARK 465 GLN A 14
REMARK 465 SER A 15
REMARK 465 ASP A 16
REMARK 465 LEU A 17
REMARK 465 SER A 74
REMARK 465 GLY B 75
REMARK 465 GLY B 76
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LEU C 3
REMARK 465 LYS C 4
REMARK 465 SER C 5
REMARK 465 GLU C 6
REMARK 465 ARG C 7
REMARK 465 ARG C 8
REMARK 465 GLY C 9
REMARK 465 ILE C 10
REMARK 465 HIS C 11
REMARK 465 VAL C 12
REMARK 465 ASP C 13
REMARK 465 GLN C 14
REMARK 465 SER C 15
REMARK 465 ASP C 16
REMARK 465 SER C 74
REMARK 465 GLY D 75
REMARK 465 GLY D 76
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 LEU E 3
REMARK 465 LYS E 4
REMARK 465 SER E 5
REMARK 465 GLU E 6
REMARK 465 ARG E 7
REMARK 465 ARG E 8
REMARK 465 GLY E 9
REMARK 465 ILE E 10
REMARK 465 HIS E 11
REMARK 465 VAL E 12
REMARK 465 ASP E 13
REMARK 465 GLN E 14
REMARK 465 SER E 15
REMARK 465 ASP E 16
REMARK 465 GLU E 66
REMARK 465 GLU E 67
REMARK 465 ALA E 68
REMARK 465 PHE E 69
REMARK 465 ALA E 70
REMARK 465 SER E 71
REMARK 465 SER E 72
REMARK 465 GLN E 73
REMARK 465 SER E 74
REMARK 465 GLY F 75
REMARK 465 GLY F 76
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 LEU G 3
REMARK 465 LYS G 4
REMARK 465 SER G 5
REMARK 465 GLU G 6
REMARK 465 ARG G 7
REMARK 465 ARG G 8
REMARK 465 GLY G 9
REMARK 465 ILE G 10
REMARK 465 HIS G 11
REMARK 465 VAL G 12
REMARK 465 ASP G 13
REMARK 465 GLN G 14
REMARK 465 SER G 15
REMARK 465 ASP G 16
REMARK 465 SER G 72
REMARK 465 GLN G 73
REMARK 465 SER G 74
REMARK 465 ARG H 74
REMARK 465 GLY H 75
REMARK 465 GLY H 76
REMARK 465 MET I 1
REMARK 465 SER I 2
REMARK 465 LEU I 3
REMARK 465 LYS I 4
REMARK 465 SER I 5
REMARK 465 GLU I 6
REMARK 465 ARG I 7
REMARK 465 ARG I 8
REMARK 465 GLY I 9
REMARK 465 ILE I 10
REMARK 465 HIS I 11
REMARK 465 VAL I 12
REMARK 465 ASP I 13
REMARK 465 GLN I 14
REMARK 465 SER I 15
REMARK 465 ASP I 16
REMARK 465 LEU J 73
REMARK 465 ARG J 74
REMARK 465 GLY J 75
REMARK 465 GLY J 76
REMARK 465 MET K 1
REMARK 465 SER K 2
REMARK 465 LEU K 3
REMARK 465 LYS K 4
REMARK 465 SER K 5
REMARK 465 GLU K 6
REMARK 465 ARG K 7
REMARK 465 ARG K 8
REMARK 465 GLY K 9
REMARK 465 ILE K 10
REMARK 465 HIS K 11
REMARK 465 VAL K 12
REMARK 465 ASP K 13
REMARK 465 GLN K 14
REMARK 465 SER K 15
REMARK 465 ASP K 16
REMARK 465 GLU K 66
REMARK 465 GLU K 67
REMARK 465 ALA K 68
REMARK 465 PHE K 69
REMARK 465 ALA K 70
REMARK 465 SER K 71
REMARK 465 SER K 72
REMARK 465 GLN K 73
REMARK 465 SER K 74
REMARK 465 GLY L 75
REMARK 465 GLY L 76
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 GLN A 73 CA C O CB CG CD OE1
REMARK 470 GLN A 73 NE2
REMARK 470 ARG B 74 CA C O CB CG CD NE
REMARK 470 ARG B 74 CZ NH1 NH2
REMARK 470 GLN C 73 CA C O CB CG CD OE1
REMARK 470 GLN C 73 NE2
REMARK 470 ARG D 74 CA C O CB CG CD NE
REMARK 470 ARG D 74 CZ NH1 NH2
REMARK 470 GLU E 65 CA C O CB CG CD OE1
REMARK 470 GLU E 65 OE2
REMARK 470 ARG F 74 CA C O CB CG CD NE
REMARK 470 ARG F 74 CZ NH1 NH2
REMARK 470 SER G 71 CA C O CB OG
REMARK 470 LEU H 73 CA C O CB CG CD1 CD2
REMARK 470 ARG J 72 CA C O CB CG CD NE
REMARK 470 ARG J 72 CZ NH1 NH2
REMARK 470 GLU K 65 CA C O CB CG CD OE1
REMARK 470 GLU K 65 OE2
REMARK 470 ARG L 74 CA C O CB CG CD NE
REMARK 470 ARG L 74 CZ NH1 NH2
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 NZ LYS B 48 O HOH B 2027 2.18
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 GLU C 67 CG GLU C 67 CD 0.125
REMARK 500 LYS D 33 CB LYS D 33 CG -0.200
REMARK 500 GLU E 64 CD GLU E 64 OE1 0.352
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 ARG B 54 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 LYS D 6 CD - CE - NZ ANGL. DEV. = -16.7 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 TRP A 31 40.41 -109.83
REMARK 500 SER B 20 0.12 -68.66
REMARK 500 SER C 71 -37.06 142.79
REMARK 500 GLU H 34 -114.32 -120.74
REMARK 500 PRO H 38 -39.00 -39.34
REMARK 500 GLU H 64 16.19 58.52
REMARK 500 GLU J 64 7.11 83.45
REMARK 500 CYS K 23 -58.15 -4.31
REMARK 500 ASP L 39 3.48 -68.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 499 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 19 SG
REMARK 620 2 CYS A 23 SG 113.3
REMARK 620 3 CYS A 35 SG 111.2 105.6
REMARK 620 4 CYS A 38 SG 102.0 120.0 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 499 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 19 SG
REMARK 620 2 CYS C 23 SG 112.2
REMARK 620 3 CYS C 38 SG 106.1 122.9
REMARK 620 4 CYS C 35 SG 110.3 100.7 103.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 499 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 19 SG
REMARK 620 2 CYS E 23 SG 114.5
REMARK 620 3 CYS E 35 SG 111.6 107.2
REMARK 620 4 CYS E 38 SG 109.9 110.9 102.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 499 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 19 SG
REMARK 620 2 CYS G 35 SG 109.1
REMARK 620 3 CYS G 38 SG 106.3 104.2
REMARK 620 4 CYS G 23 SG 116.8 105.1 114.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN I 499 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 23 SG
REMARK 620 2 CYS I 35 SG 95.1
REMARK 620 3 CYS I 38 SG 93.7 95.1
REMARK 620 4 CYS I 19 SG 132.0 118.5 114.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN K 499 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 38 SG
REMARK 620 2 CYS K 19 SG 95.6
REMARK 620 3 CYS K 35 SG 91.2 94.5
REMARK 620 4 CYS K 23 SG 117.4 138.8 107.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 499
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AAR RELATED DB: PDB
REMARK 900 DI-UBIQUITIN
REMARK 900 RELATED ID: 1E0Q RELATED DB: PDB
REMARK 900 MUTANT PEPTIDE FROM THE FIRST N-TERMINAL 17 AMINO-ACID OF UBIQUITIN
REMARK 900 RELATED ID: 1P3Q RELATED DB: PDB
REMARK 900 MECHANISM OF UBIQUITIN RECOGNITION BY THE CUE DOMAIN OF VPS9
REMARK 900 RELATED ID: 1UZX RELATED DB: PDB
REMARK 900 A COMPLEX OF THE VPS23 UEV WITH UBIQUITIN
REMARK 900 RELATED ID: 1V80 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURES OF UBIQUITIN AT 30 BAR AND 3 KBAR
REMARK 900 RELATED ID: 1V81 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURES OF UBIQUITIN AT 30 BAR AND 3 KBAR
REMARK 900 RELATED ID: 1WR6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GGA3 GAT DOMAIN IN COMPLEX WITH UBIQUITIN
REMARK 900 RELATED ID: 1WRD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TOM1 GAT DOMAIN IN COMPLEX WITH UBIQUITIN
REMARK 900 RELATED ID: 1YD8 RELATED DB: PDB
REMARK 900 COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN
REMARK 900 RELATED ID: 2BGF RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF LYS48-LINKED DI-UBIQUITIN USING CHEMICAL SHIFT
REMARK 900 PERTURBATION DATA TOGETHER WITH RDCS AND 15N-RELAXATION DATA
REMARK 900 RELATED ID: 2C7M RELATED DB: PDB
REMARK 900 COMPLEX OF HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT USED IN THE STRUCTURE DETERMINATION
REMARK 999 CONTAINED ONLY RESIDUES 1-74
DBREF 2C7N A 1 74 UNP Q53FG0 Q53FG0_HUMAN 1 74
DBREF 2C7N B 1 76 UNP P62990 UBIQ_BOVIN 1 76
DBREF 2C7N C 1 74 UNP Q53FG0 Q53FG0_HUMAN 1 74
DBREF 2C7N D 1 76 UNP P62990 UBIQ_BOVIN 1 76
DBREF 2C7N E 1 74 UNP Q53FG0 Q53FG0_HUMAN 1 74
DBREF 2C7N F 1 76 UNP P62990 UBIQ_BOVIN 1 76
DBREF 2C7N G 1 74 UNP Q53FG0 Q53FG0_HUMAN 1 74
DBREF 2C7N H 1 76 UNP P62990 UBIQ_BOVIN 1 76
DBREF 2C7N I 1 74 UNP Q53FG0 Q53FG0_HUMAN 1 74
DBREF 2C7N J 1 76 UNP P62990 UBIQ_BOVIN 1 76
DBREF 2C7N K 1 74 UNP Q53FG0 Q53FG0_HUMAN 1 74
DBREF 2C7N L 1 76 UNP P62990 UBIQ_BOVIN 1 76
SEQRES 1 A 74 MET SER LEU LYS SER GLU ARG ARG GLY ILE HIS VAL ASP
SEQRES 2 A 74 GLN SER ASP LEU LEU CYS LYS LYS GLY CYS GLY TYR TYR
SEQRES 3 A 74 GLY ASN PRO ALA TRP GLN GLY PHE CYS SER LYS CYS TRP
SEQRES 4 A 74 ARG GLU GLU TYR HIS LYS ALA ARG GLN LYS GLN ILE GLN
SEQRES 5 A 74 GLU ASP TRP GLU LEU ALA GLU ARG LEU GLN ARG GLU GLU
SEQRES 6 A 74 GLU GLU ALA PHE ALA SER SER GLN SER
SEQRES 1 B 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 B 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 B 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 B 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 B 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 B 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 C 74 MET SER LEU LYS SER GLU ARG ARG GLY ILE HIS VAL ASP
SEQRES 2 C 74 GLN SER ASP LEU LEU CYS LYS LYS GLY CYS GLY TYR TYR
SEQRES 3 C 74 GLY ASN PRO ALA TRP GLN GLY PHE CYS SER LYS CYS TRP
SEQRES 4 C 74 ARG GLU GLU TYR HIS LYS ALA ARG GLN LYS GLN ILE GLN
SEQRES 5 C 74 GLU ASP TRP GLU LEU ALA GLU ARG LEU GLN ARG GLU GLU
SEQRES 6 C 74 GLU GLU ALA PHE ALA SER SER GLN SER
SEQRES 1 D 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 D 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 D 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 D 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 D 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 D 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 E 74 MET SER LEU LYS SER GLU ARG ARG GLY ILE HIS VAL ASP
SEQRES 2 E 74 GLN SER ASP LEU LEU CYS LYS LYS GLY CYS GLY TYR TYR
SEQRES 3 E 74 GLY ASN PRO ALA TRP GLN GLY PHE CYS SER LYS CYS TRP
SEQRES 4 E 74 ARG GLU GLU TYR HIS LYS ALA ARG GLN LYS GLN ILE GLN
SEQRES 5 E 74 GLU ASP TRP GLU LEU ALA GLU ARG LEU GLN ARG GLU GLU
SEQRES 6 E 74 GLU GLU ALA PHE ALA SER SER GLN SER
SEQRES 1 F 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 F 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 F 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 F 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 F 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 F 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 G 74 MET SER LEU LYS SER GLU ARG ARG GLY ILE HIS VAL ASP
SEQRES 2 G 74 GLN SER ASP LEU LEU CYS LYS LYS GLY CYS GLY TYR TYR
SEQRES 3 G 74 GLY ASN PRO ALA TRP GLN GLY PHE CYS SER LYS CYS TRP
SEQRES 4 G 74 ARG GLU GLU TYR HIS LYS ALA ARG GLN LYS GLN ILE GLN
SEQRES 5 G 74 GLU ASP TRP GLU LEU ALA GLU ARG LEU GLN ARG GLU GLU
SEQRES 6 G 74 GLU GLU ALA PHE ALA SER SER GLN SER
SEQRES 1 H 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 H 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 H 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 H 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 H 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 H 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 I 74 MET SER LEU LYS SER GLU ARG ARG GLY ILE HIS VAL ASP
SEQRES 2 I 74 GLN SER ASP LEU LEU CYS LYS LYS GLY CYS GLY TYR TYR
SEQRES 3 I 74 GLY ASN PRO ALA TRP GLN GLY PHE CYS SER LYS CYS TRP
SEQRES 4 I 74 ARG GLU GLU TYR HIS LYS ALA ARG GLN LYS GLN ILE GLN
SEQRES 5 I 74 GLU ASP TRP GLU LEU ALA GLU ARG LEU GLN ARG GLU GLU
SEQRES 6 I 74 GLU GLU ALA PHE ALA SER SER GLN SER
SEQRES 1 J 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 J 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 J 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 J 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 J 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 J 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 K 74 MET SER LEU LYS SER GLU ARG ARG GLY ILE HIS VAL ASP
SEQRES 2 K 74 GLN SER ASP LEU LEU CYS LYS LYS GLY CYS GLY TYR TYR
SEQRES 3 K 74 GLY ASN PRO ALA TRP GLN GLY PHE CYS SER LYS CYS TRP
SEQRES 4 K 74 ARG GLU GLU TYR HIS LYS ALA ARG GLN LYS GLN ILE GLN
SEQRES 5 K 74 GLU ASP TRP GLU LEU ALA GLU ARG LEU GLN ARG GLU GLU
SEQRES 6 K 74 GLU GLU ALA PHE ALA SER SER GLN SER
SEQRES 1 L 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 L 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 L 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 L 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 L 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 L 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
HET ZN A 499 1
HET ZN C 499 1
HET ZN E 499 1
HET ZN G 499 1
HET ZN I 499 1
HET ZN K 499 1
HETNAM ZN ZINC ION
FORMUL 13 ZN 6(ZN 2+)
FORMUL 19 HOH *253(H2 O)
HELIX 1 1 ASN A 28 GLN A 32 5 5
HELIX 2 2 CYS A 35 SER A 71 1 37
HELIX 3 3 THR B 22 GLY B 35 1 14
HELIX 4 4 PRO B 37 ASP B 39 5 3
HELIX 5 5 LEU B 56 ASN B 60 5 5
HELIX 6 6 ASN C 28 GLN C 32 5 5
HELIX 7 7 CYS C 35 ALA C 70 1 36
HELIX 8 8 THR D 22 GLY D 35 1 14
HELIX 9 9 PRO D 37 ASP D 39 5 3
HELIX 10 10 LEU D 56 ASN D 60 5 5
HELIX 11 11 ASN E 28 GLN E 32 5 5
HELIX 12 12 CYS E 35 GLU E 64 1 30
HELIX 13 13 THR F 22 GLY F 35 1 14
HELIX 14 14 PRO F 37 ASP F 39 5 3
HELIX 15 15 LEU F 56 ASN F 60 5 5
HELIX 16 16 ASN G 28 GLN G 32 5 5
HELIX 17 17 CYS G 35 ALA G 70 1 36
HELIX 18 18 THR H 22 GLU H 34 1 13
HELIX 19 19 PRO H 37 ASP H 39 5 3
HELIX 20 20 LEU H 56 ASN H 60 5 5
HELIX 21 21 ASN I 28 GLN I 32 5 5
HELIX 22 22 CYS I 35 SER I 74 1 40
HELIX 23 23 THR J 22 GLY J 35 1 14
HELIX 24 24 PRO J 37 GLN J 41 5 5
HELIX 25 25 LEU J 56 ASN J 60 5 5
HELIX 26 26 CYS K 35 GLU K 64 1 30
HELIX 27 27 THR L 22 GLY L 35 1 14
HELIX 28 28 PRO L 37 ASP L 39 5 3
HELIX 29 29 LEU L 56 ASN L 60 5 5
SHEET 1 BA 5 THR B 12 GLU B 16 0
SHEET 2 BA 5 GLN B 2 THR B 7 -1 O ILE B 3 N LEU B 15
SHEET 3 BA 5 THR B 66 LEU B 71 1 O LEU B 67 N LYS B 6
SHEET 4 BA 5 GLN B 41 PHE B 45 -1 O ARG B 42 N VAL B 70
SHEET 5 BA 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45
SHEET 1 DA 5 THR D 12 GLU D 16 0
SHEET 2 DA 5 GLN D 2 THR D 7 -1 O ILE D 3 N LEU D 15
SHEET 3 DA 5 THR D 66 LEU D 71 1 O LEU D 67 N LYS D 6
SHEET 4 DA 5 GLN D 41 PHE D 45 -1 O ARG D 42 N VAL D 70
SHEET 5 DA 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45
SHEET 1 FA 5 THR F 12 GLU F 16 0
SHEET 2 FA 5 GLN F 2 THR F 7 -1 O ILE F 3 N LEU F 15
SHEET 3 FA 5 THR F 66 LEU F 71 1 O LEU F 67 N LYS F 6
SHEET 4 FA 5 GLN F 41 PHE F 45 -1 O ARG F 42 N VAL F 70
SHEET 5 FA 5 LYS F 48 GLN F 49 -1 O LYS F 48 N PHE F 45
SHEET 1 HA 5 THR H 12 GLU H 16 0
SHEET 2 HA 5 GLN H 2 LYS H 6 -1 O ILE H 3 N LEU H 15
SHEET 3 HA 5 THR H 66 LEU H 71 1 O LEU H 67 N LYS H 6
SHEET 4 HA 5 GLN H 41 PHE H 45 -1 O ARG H 42 N VAL H 70
SHEET 5 HA 5 LYS H 48 GLN H 49 -1 O LYS H 48 N PHE H 45
SHEET 1 JA 5 THR J 12 GLU J 16 0
SHEET 2 JA 5 GLN J 2 LYS J 6 -1 O ILE J 3 N LEU J 15
SHEET 3 JA 5 THR J 66 VAL J 70 1 O LEU J 67 N LYS J 6
SHEET 4 JA 5 ARG J 42 PHE J 45 -1 O ARG J 42 N VAL J 70
SHEET 5 JA 5 LYS J 48 GLN J 49 -1 O LYS J 48 N PHE J 45
SHEET 1 LA 5 THR L 12 GLU L 16 0
SHEET 2 LA 5 GLN L 2 LYS L 6 -1 O ILE L 3 N LEU L 15
SHEET 3 LA 5 THR L 66 LEU L 71 1 O LEU L 67 N LYS L 6
SHEET 4 LA 5 GLN L 41 PHE L 45 -1 O ARG L 42 N VAL L 70
SHEET 5 LA 5 LYS L 48 GLN L 49 -1 O LYS L 48 N PHE L 45
LINK ZN ZN A 499 SG CYS A 19 1555 1555 2.08
LINK ZN ZN A 499 SG CYS A 23 1555 1555 2.36
LINK ZN ZN A 499 SG CYS A 35 1555 1555 2.28
LINK ZN ZN A 499 SG CYS A 38 1555 1555 2.42
LINK ZN ZN C 499 SG CYS C 19 1555 1555 2.05
LINK ZN ZN C 499 SG CYS C 23 1555 1555 2.41
LINK ZN ZN C 499 SG CYS C 38 1555 1555 2.38
LINK ZN ZN C 499 SG CYS C 35 1555 1555 2.34
LINK ZN ZN E 499 SG CYS E 19 1555 1555 2.35
LINK ZN ZN E 499 SG CYS E 23 1555 1555 2.33
LINK ZN ZN E 499 SG CYS E 35 1555 1555 2.37
LINK ZN ZN E 499 SG CYS E 38 1555 1555 2.34
LINK ZN ZN G 499 SG CYS G 19 1555 1555 2.36
LINK ZN ZN G 499 SG CYS G 35 1555 1555 2.46
LINK ZN ZN G 499 SG CYS G 38 1555 1555 2.37
LINK ZN ZN G 499 SG CYS G 23 1555 1555 2.34
LINK ZN ZN I 499 SG CYS I 23 1555 1555 2.70
LINK ZN ZN I 499 SG CYS I 35 1555 1555 2.51
LINK ZN ZN I 499 SG CYS I 38 1555 1555 2.71
LINK ZN ZN I 499 SG CYS I 19 1555 1555 2.24
LINK ZN ZN K 499 SG CYS K 38 1555 1555 2.70
LINK ZN ZN K 499 SG CYS K 19 1555 1555 2.39
LINK ZN ZN K 499 SG CYS K 35 1555 1555 2.72
LINK ZN ZN K 499 SG CYS K 23 1555 1555 2.54
SITE 1 AC1 4 CYS A 19 CYS A 23 CYS A 35 CYS A 38
SITE 1 AC2 4 CYS C 19 CYS C 23 CYS C 35 CYS C 38
SITE 1 AC3 4 CYS E 19 CYS E 23 CYS E 35 CYS E 38
SITE 1 AC4 4 CYS G 19 CYS G 23 CYS G 35 CYS G 38
SITE 1 AC5 4 CYS I 19 CYS I 23 CYS I 35 CYS I 38
SITE 1 AC6 4 CYS K 19 CYS K 23 CYS K 35 CYS K 38
CRYST1 44.300 68.900 98.500 108.20 102.70 90.40 P 1 6
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 0.022573 0.000158 0.005426 0.00000
SCALE2 0.000000 0.014514 0.004932 0.00000
SCALE3 0.000000 0.000000 0.010991 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
