HEADER OXIDOREDUCTASE 03-JUL-03 1OJ7
TITLE STRUCTURAL GENOMICS, UNKNOWN FUNCTION CRYSTAL STRUCTURE OF
TITLE 2 E. COLI K-12 YQHD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL OXIDOREDUCTASE YQHD;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PDEST17
KEYWDS OXIDOREDUCTASE, HYPOTHETICAL OXIDOREDUCTASE, STRUCTURAL
KEYWDS 2 GENOMICS, REDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SULZENBACHER,S.PERRIER,V.ROIG-ZAMBONI,F.PAGOT,S.GRISEL,
AUTHOR 2 A.SALAMONI,C.VALENCIA,C.BIGNON,R.VINCENTELLI,M.TEGONI,
AUTHOR 3 C.CAMBILLAU
REVDAT 3 24-FEB-09 1OJ7 1 VERSN
REVDAT 2 02-SEP-04 1OJ7 1 JRNL
REVDAT 1 08-JUL-04 1OJ7 0
JRNL AUTH G.SULZENBACHER,K.ALVAREZ,R.H.H.VAN-DEN-HEUVEL,
JRNL AUTH 2 C.VERSLUIS,S.SPINELLI,V.CAMPANACCI,C.VALENCIA,
JRNL AUTH 3 C.CAMBILLAU,H.EKLUND,M.TEGONI
JRNL TITL CRYSTAL STRUCTURE OF E.COLI ALCOHOL DEHYDROGENASE
JRNL TITL 2 YQHD: EVIDENCE OF A COVALENTLY MODIFIED NADP
JRNL TITL 3 COENZYME
JRNL REF J.MOL.BIOL. V. 342 489 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15327949
JRNL DOI 10.1016/J.JMB.2004.07.034
REMARK 2
REMARK 2 RESOLUTION. 2.0 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 3 NUMBER OF REFLECTIONS : 134578
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) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.164
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4134
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9589
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1820
REMARK 3 BIN FREE R VALUE SET COUNT : 319
REMARK 3 BIN FREE R VALUE : 0.2010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12274
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 162
REMARK 3 SOLVENT ATOMS : 1494
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.69000
REMARK 3 B22 (A**2) : 0.69000
REMARK 3 B33 (A**2) : -1.03000
REMARK 3 B12 (A**2) : 0.34000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.795
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12707 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 11649 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17330 ; 1.115 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27149 ; 0.776 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1570 ; 5.212 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1999 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13928 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2393 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2708 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 13724 ; 0.229 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 6987 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1328 ; 0.158 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.157 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 16 ; 0.147 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 84 ; 0.246 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 57 ; 0.211 ; 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): 7815 ; 0.432 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12642 ; 0.837 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4892 ; 1.391 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4677 ; 2.404 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
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 -2 A 14
REMARK 3 ORIGIN FOR THE GROUP (A): 103.1800 -33.1460 26.3300
REMARK 3 T TENSOR
REMARK 3 T11: 0.2844 T22: 0.2551
REMARK 3 T33: 0.3893 T12: -0.0228
REMARK 3 T13: 0.0145 T23: -0.0614
REMARK 3 L TENSOR
REMARK 3 L11: 2.7377 L22: 3.9750
REMARK 3 L33: 0.7151 L12: 2.4120
REMARK 3 L13: 0.5875 L23: -0.1037
REMARK 3 S TENSOR
REMARK 3 S11: 0.0964 S12: 0.1847 S13: 0.0392
REMARK 3 S21: -0.0669 S22: -0.1194 S23: 0.1011
REMARK 3 S31: 0.0183 S32: 0.0150 S33: 0.0230
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 15 A 183
REMARK 3 ORIGIN FOR THE GROUP (A): 103.5280 -13.5610 16.4840
REMARK 3 T TENSOR
REMARK 3 T11: 0.3084 T22: 0.3129
REMARK 3 T33: 0.3399 T12: -0.0567
REMARK 3 T13: 0.0408 T23: 0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 1.2885 L22: 1.0253
REMARK 3 L33: 1.1012 L12: -0.1961
REMARK 3 L13: 0.3673 L23: -0.0540
REMARK 3 S TENSOR
REMARK 3 S11: 0.0215 S12: 0.2686 S13: 0.0901
REMARK 3 S21: -0.1754 S22: -0.0691 S23: -0.2048
REMARK 3 S31: -0.0220 S32: 0.0640 S33: 0.0476
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 : A 184 A 263
REMARK 3 ORIGIN FOR THE GROUP (A): 96.7260 -23.7640 36.9170
REMARK 3 T TENSOR
REMARK 3 T11: 0.3115 T22: 0.2738
REMARK 3 T33: 0.3869 T12: -0.0425
REMARK 3 T13: -0.0174 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 0.8553 L22: 0.7990
REMARK 3 L33: 0.3394 L12: -0.2058
REMARK 3 L13: 0.1074 L23: -0.0354
REMARK 3 S TENSOR
REMARK 3 S11: -0.0717 S12: 0.0444 S13: -0.0294
REMARK 3 S21: -0.0032 S22: 0.0449 S23: -0.0443
REMARK 3 S31: -0.0096 S32: -0.0146 S33: 0.0268
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 : A 264 A 387
REMARK 3 ORIGIN FOR THE GROUP (A): 79.8060 -22.3630 33.2700
REMARK 3 T TENSOR
REMARK 3 T11: 0.3011 T22: 0.2872
REMARK 3 T33: 0.3414 T12: -0.0620
REMARK 3 T13: -0.0100 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 1.1670 L22: 1.3803
REMARK 3 L33: 0.8527 L12: -0.4255
REMARK 3 L13: 0.4097 L23: -0.2742
REMARK 3 S TENSOR
REMARK 3 S11: -0.0471 S12: 0.0263 S13: -0.0768
REMARK 3 S21: -0.0512 S22: 0.1057 S23: 0.0809
REMARK 3 S31: -0.0185 S32: -0.1357 S33: -0.0586
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 501 E 501
REMARK 3 ORIGIN FOR THE GROUP (A): 96.2610 -11.6160 26.3920
REMARK 3 T TENSOR
REMARK 3 T11: 0.2281 T22: 0.1909
REMARK 3 T33: 0.2313 T12: -0.0598
REMARK 3 T13: 0.0070 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 3.6331 L22: 4.7155
REMARK 3 L33: 2.1392 L12: 2.0585
REMARK 3 L13: 2.5383 L23: 3.4460
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: 0.0682 S13: -0.1668
REMARK 3 S21: -0.1069 S22: -0.0972 S23: -0.2838
REMARK 3 S31: 0.1612 S32: 0.0993 S33: 0.0627
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 : B -2 B 14
REMARK 3 ORIGIN FOR THE GROUP (A): 78.2980 12.7010 31.3540
REMARK 3 T TENSOR
REMARK 3 T11: 0.4026 T22: 0.3143
REMARK 3 T33: 0.2446 T12: -0.0589
REMARK 3 T13: -0.0270 T23: 0.0215
REMARK 3 L TENSOR
REMARK 3 L11: 0.9881 L22: 5.3472
REMARK 3 L33: 1.3882 L12: 1.5772
REMARK 3 L13: -1.0204 L23: -2.3203
REMARK 3 S TENSOR
REMARK 3 S11: -0.0729 S12: 0.1292 S13: -0.0041
REMARK 3 S21: -0.0929 S22: 0.0841 S23: -0.0480
REMARK 3 S31: -0.0221 S32: -0.0678 S33: -0.0112
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 : B 15 B 183
REMARK 3 ORIGIN FOR THE GROUP (A): 88.8060 17.9230 13.0540
REMARK 3 T TENSOR
REMARK 3 T11: 0.3650 T22: 0.3099
REMARK 3 T33: 0.2756 T12: -0.0963
REMARK 3 T13: 0.0225 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 0.4681 L22: 1.5403
REMARK 3 L33: 1.1360 L12: -0.3218
REMARK 3 L13: -0.1221 L23: 0.5350
REMARK 3 S TENSOR
REMARK 3 S11: 0.0601 S12: 0.0279 S13: 0.0265
REMARK 3 S21: -0.1633 S22: 0.0573 S23: -0.1823
REMARK 3 S31: -0.1892 S32: 0.1254 S33: -0.1174
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 : B 184 B 263
REMARK 3 ORIGIN FOR THE GROUP (A): 66.7490 16.9690 21.7900
REMARK 3 T TENSOR
REMARK 3 T11: 0.4056 T22: 0.3310
REMARK 3 T33: 0.2633 T12: -0.0147
REMARK 3 T13: -0.0230 T23: 0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 0.0943 L22: 0.9663
REMARK 3 L33: 0.5304 L12: -0.0288
REMARK 3 L13: 0.0068 L23: 0.0938
REMARK 3 S TENSOR
REMARK 3 S11: 0.0630 S12: -0.0015 S13: -0.0182
REMARK 3 S21: -0.0850 S22: -0.0259 S23: 0.0581
REMARK 3 S31: -0.0999 S32: -0.0935 S33: -0.0370
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 : B 264 B 387
REMARK 3 ORIGIN FOR THE GROUP (A): 62.2980 3.1140 12.2800
REMARK 3 T TENSOR
REMARK 3 T11: 0.3436 T22: 0.3381
REMARK 3 T33: 0.2615 T12: -0.0525
REMARK 3 T13: -0.0318 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 0.5177 L22: 0.6800
REMARK 3 L33: 1.7539 L12: -0.1636
REMARK 3 L13: -0.2726 L23: 0.0789
REMARK 3 S TENSOR
REMARK 3 S11: -0.0130 S12: 0.0335 S13: -0.0709
REMARK 3 S21: -0.0750 S22: -0.0006 S23: 0.0459
REMARK 3 S31: 0.0626 S32: -0.1791 S33: 0.0136
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 : F 502 F 502
REMARK 3 ORIGIN FOR THE GROUP (A): 76.8920 17.7350 9.2570
REMARK 3 T TENSOR
REMARK 3 T11: 0.3072 T22: 0.2253
REMARK 3 T33: 0.1314 T12: -0.0356
REMARK 3 T13: 0.0117 T23: 0.0776
REMARK 3 L TENSOR
REMARK 3 L11: 4.2766 L22: -0.5503
REMARK 3 L33: 6.7755 L12: 5.6972
REMARK 3 L13: 0.1252 L23: -0.7747
REMARK 3 S TENSOR
REMARK 3 S11: 0.1059 S12: -0.0333 S13: 0.1584
REMARK 3 S21: -0.1536 S22: -0.2143 S23: -0.0186
REMARK 3 S31: -0.0425 S32: -0.0014 S33: 0.1084
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 : C -2 C 14
REMARK 3 ORIGIN FOR THE GROUP (A): 78.6710 21.5940 33.0510
REMARK 3 T TENSOR
REMARK 3 T11: 0.4204 T22: 0.3369
REMARK 3 T33: 0.2627 T12: -0.0458
REMARK 3 T13: 0.0261 T23: 0.0381
REMARK 3 L TENSOR
REMARK 3 L11: -0.0392 L22: 3.8379
REMARK 3 L33: 1.3970 L12: -0.3812
REMARK 3 L13: 0.6114 L23: -1.5773
REMARK 3 S TENSOR
REMARK 3 S11: -0.0086 S12: -0.0086 S13: -0.0318
REMARK 3 S21: 0.2130 S22: 0.0677 S23: 0.1064
REMARK 3 S31: -0.2296 S32: -0.0683 S33: -0.0591
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 : C 15 C 183
REMARK 3 ORIGIN FOR THE GROUP (A): 91.5070 14.0610 50.6580
REMARK 3 T TENSOR
REMARK 3 T11: 0.3402 T22: 0.2697
REMARK 3 T33: 0.2961 T12: -0.0285
REMARK 3 T13: -0.0212 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 1.2849 L22: 2.3894
REMARK 3 L33: 0.5882 L12: 1.0826
REMARK 3 L13: -0.0326 L23: -0.0333
REMARK 3 S TENSOR
REMARK 3 S11: 0.0814 S12: -0.0336 S13: 0.0189
REMARK 3 S21: 0.1332 S22: -0.0022 S23: -0.1664
REMARK 3 S31: 0.0186 S32: 0.0184 S33: -0.0792
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 : C 184 C 263
REMARK 3 ORIGIN FOR THE GROUP (A): 67.1950 17.7510 42.8250
REMARK 3 T TENSOR
REMARK 3 T11: 0.3770 T22: 0.3211
REMARK 3 T33: 0.2750 T12: -0.0167
REMARK 3 T13: -0.0160 T23: 0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 0.0412 L22: 2.1660
REMARK 3 L33: 0.7489 L12: 0.0014
REMARK 3 L13: -0.2667 L23: -0.7067
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: 0.0351 S13: -0.0180
REMARK 3 S21: 0.0176 S22: 0.0290 S23: -0.0628
REMARK 3 S31: -0.0618 S32: -0.0964 S33: -0.0361
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 : C 264 C 387
REMARK 3 ORIGIN FOR THE GROUP (A): 63.0940 31.7740 52.4450
REMARK 3 T TENSOR
REMARK 3 T11: 0.3309 T22: 0.2839
REMARK 3 T33: 0.2896 T12: 0.0369
REMARK 3 T13: -0.0135 T23: 0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 0.8890 L22: 1.5627
REMARK 3 L33: 1.5359 L12: 0.2913
REMARK 3 L13: 0.3015 L23: 0.5924
REMARK 3 S TENSOR
REMARK 3 S11: 0.0123 S12: 0.0168 S13: 0.1180
REMARK 3 S21: 0.0579 S22: -0.0345 S23: 0.0051
REMARK 3 S31: -0.0311 S32: -0.1771 S33: 0.0223
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 : D -2 D 14
REMARK 3 ORIGIN FOR THE GROUP (A): 110.8400 -30.2990 30.2790
REMARK 3 T TENSOR
REMARK 3 T11: 0.3058 T22: 0.2419
REMARK 3 T33: 0.3769 T12: -0.0364
REMARK 3 T13: -0.0271 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 2.2037 L22: 4.1812
REMARK 3 L33: 1.1893 L12: 1.6728
REMARK 3 L13: 1.0011 L23: 2.1109
REMARK 3 S TENSOR
REMARK 3 S11: -0.0181 S12: 0.1846 S13: -0.0785
REMARK 3 S21: 0.0412 S22: -0.0200 S23: -0.2598
REMARK 3 S31: 0.1163 S32: 0.0716 S33: 0.0381
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 : D 15 D 183
REMARK 3 ORIGIN FOR THE GROUP (A): 119.6590 -48.2880 21.1010
REMARK 3 T TENSOR
REMARK 3 T11: 0.3300 T22: 0.2963
REMARK 3 T33: 0.3965 T12: -0.0083
REMARK 3 T13: 0.1231 T23: -0.1794
REMARK 3 L TENSOR
REMARK 3 L11: 2.2241 L22: 1.1917
REMARK 3 L33: 1.0836 L12: -0.3524
REMARK 3 L13: 0.5091 L23: -0.3354
REMARK 3 S TENSOR
REMARK 3 S11: 0.0277 S12: 0.5303 S13: -0.4187
REMARK 3 S21: -0.3581 S22: -0.0879 S23: -0.2031
REMARK 3 S31: 0.1536 S32: 0.1659 S33: 0.0603
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 : D 184 D 263
REMARK 3 ORIGIN FOR THE GROUP (A): 107.1610 -41.5080 40.3850
REMARK 3 T TENSOR
REMARK 3 T11: 0.3031 T22: 0.2292
REMARK 3 T33: 0.4306 T12: -0.0225
REMARK 3 T13: 0.0044 T23: -0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 1.3674 L22: 1.5221
REMARK 3 L33: 0.0245 L12: 0.1509
REMARK 3 L13: 0.3676 L23: -0.1297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0548 S12: 0.0377 S13: -0.2167
REMARK 3 S21: 0.0199 S22: 0.0042 S23: -0.0585
REMARK 3 S31: -0.0116 S32: 0.0115 S33: 0.0506
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 : D 264 D 387
REMARK 3 ORIGIN FOR THE GROUP (A): 120.5730 -43.5680 51.0660
REMARK 3 T TENSOR
REMARK 3 T11: 0.2825 T22: 0.2191
REMARK 3 T33: 0.4094 T12: 0.0060
REMARK 3 T13: -0.0233 T23: 0.0297
REMARK 3 L TENSOR
REMARK 3 L11: 2.4934 L22: 1.3835
REMARK 3 L33: 0.4268 L12: -0.0806
REMARK 3 L13: 0.0160 L23: -0.0146
REMARK 3 S TENSOR
REMARK 3 S11: -0.0626 S12: -0.1970 S13: -0.2785
REMARK 3 S21: 0.1117 S22: 0.0638 S23: -0.1473
REMARK 3 S31: 0.0137 S32: 0.0386 S33: -0.0012
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 503 H 503
REMARK 3 ORIGIN FOR THE GROUP (A): 116.5890 -52.1180 32.5240
REMARK 3 T TENSOR
REMARK 3 T11: 0.1907 T22: 0.0749
REMARK 3 T33: 0.4324 T12: -0.0842
REMARK 3 T13: 0.0646 T23: -0.1529
REMARK 3 L TENSOR
REMARK 3 L11: -1.0470 L22: -4.8059
REMARK 3 L33: 5.5744 L12: -4.8109
REMARK 3 L13: 3.6626 L23: 2.1736
REMARK 3 S TENSOR
REMARK 3 S11: -0.3470 S12: 0.3438 S13: -0.4524
REMARK 3 S21: -0.5779 S22: 0.5328 S23: -0.5848
REMARK 3 S31: -0.5008 S32: -0.3879 S33: -0.1859
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1OJ7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JUL-03.
REMARK 100 THE PDBE ID CODE IS EBI-12984.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
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 : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80905
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : 0.06600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.15800
REMARK 200 R SYM FOR SHELL (I) : 0.22300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: SOLVE, MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE STRUCTURE WAS SOLVED BY SAD ON THE PLATINUM EDGE,
REMARK 200 BUT THE MODEL WAS REFINED AGAINST THE NATIVE DATA
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.7
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0,95 M NA-CITRATE,
REMARK 280 0.01 M NA-BORATE PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.49600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.24800
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.49600
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 22.24800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 GENERATING THE BIOMOLECULE
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, 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 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 SER A -19
REMARK 465 TYR A -18
REMARK 465 TYR A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 LEU A -10
REMARK 465 GLU A -9
REMARK 465 SER A -8
REMARK 465 THR A -7
REMARK 465 SER A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 LYS A -3
REMARK 465 MET B -20
REMARK 465 SER B -19
REMARK 465 TYR B -18
REMARK 465 TYR B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 LEU B -10
REMARK 465 GLU B -9
REMARK 465 SER B -8
REMARK 465 THR B -7
REMARK 465 SER B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 LYS B -3
REMARK 465 MET C -20
REMARK 465 SER C -19
REMARK 465 TYR C -18
REMARK 465 TYR C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 LEU C -10
REMARK 465 GLU C -9
REMARK 465 SER C -8
REMARK 465 THR C -7
REMARK 465 SER C -6
REMARK 465 LEU C -5
REMARK 465 TYR C -4
REMARK 465 LYS C -3
REMARK 465 MET D -20
REMARK 465 SER D -19
REMARK 465 TYR D -18
REMARK 465 TYR D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 LEU D -10
REMARK 465 GLU D -9
REMARK 465 SER D -8
REMARK 465 THR D -7
REMARK 465 SER D -6
REMARK 465 LEU D -5
REMARK 465 TYR D -4
REMARK 465 LYS D -3
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 ND1 HIS A 342 - O HOH A 2311 2.19
REMARK 500 OG1 THR A 375 - OD2 ASP A 377 2.15
REMARK 500 ND1 HIS B 372 - O HOH B 2391 2.13
REMARK 500 ND1 HIS C 342 - O HOH C 2360 2.14
REMARK 500 O HOH B 2016 - O HOH C 2040 2.12
REMARK 500 O HOH B 2087 - O HOH B 2093 2.18
REMARK 500 O HOH B 2213 - O HOH B 2272 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 194 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 194 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP C 58 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP C 227 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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 68 74.11 58.56
REMARK 500 ALA A 141 -54.72 -160.70
REMARK 500 THR A 205 -139.86 -145.33
REMARK 500 LEU A 252 45.44 -149.15
REMARK 500 ASP A 263 -81.22 -91.19
REMARK 500 MET A 365 52.70 -97.66
REMARK 500 ASN B 68 71.47 65.39
REMARK 500 ALA B 141 -55.04 -162.45
REMARK 500 SER B 146 38.72 -143.53
REMARK 500 TYR B 203 -46.20 -133.26
REMARK 500 THR B 205 -115.93 -131.44
REMARK 500 LEU B 252 57.72 -152.54
REMARK 500 ASP B 263 -83.63 -91.33
REMARK 500 TYR C 203 -46.56 -133.95
REMARK 500 THR C 205 -123.98 -142.39
REMARK 500 ASP C 263 -81.80 -86.99
REMARK 500 MET C 365 59.14 -91.67
REMARK 500 ASN D 68 73.28 58.98
REMARK 500 ALA D 141 -58.19 -163.73
REMARK 500 TYR D 203 -46.72 -137.11
REMARK 500 THR D 205 -115.07 -132.64
REMARK 500 LEU D 252 39.07 -150.32
REMARK 500 ASP D 263 -80.26 -89.88
REMARK 500 MET D 365 56.36 -95.91
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 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 B1389 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 194 OD1
REMARK 620 2 HIS B 198 NE2 82.6
REMARK 620 3 HIS B 267 NE2 117.5 90.4
REMARK 620 4 HIS B 281 NE2 103.1 164.7 99.2
REMARK 620 5 NZQ B1388 O5N 139.7 69.9 92.4 97.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1388 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 194 OD1
REMARK 620 2 HIS C 198 NE2 90.9
REMARK 620 3 HIS C 281 NE2 85.9 174.6
REMARK 620 4 BO3 C1390 O2 113.4 84.2 93.1
REMARK 620 5 BO3 C1390 O3 161.2 74.1 108.1 54.7
REMARK 620 6 HIS C 267 NE2 112.5 88.0 97.2 133.5 79.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D1389 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 194 OD1
REMARK 620 2 HIS D 198 NE2 81.4
REMARK 620 3 HIS D 267 NE2 119.4 88.0
REMARK 620 4 HIS D 281 NE2 103.1 167.5 99.5
REMARK 620 5 NZQ D1388 O5N 139.7 72.0 89.9 97.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1389
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C1388
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1389
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D1389
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NZQ A1388
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO3 A1389
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NZQ B1388
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BO3 C1390
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NZQ D1388
DBREF 1OJ7 A -20 1 PDB 1OJ7 1OJ7 -20 1
DBREF 1OJ7 A 2 387 UNP Q46856 YQHD_ECOLI 2 387
DBREF 1OJ7 B -20 1 PDB 1OJ7 1OJ7 -20 1
DBREF 1OJ7 B 2 387 UNP Q46856 YQHD_ECOLI 2 387
DBREF 1OJ7 C -20 1 PDB 1OJ7 1OJ7 -20 1
DBREF 1OJ7 C 2 387 UNP Q46856 YQHD_ECOLI 2 387
DBREF 1OJ7 D -20 1 PDB 1OJ7 1OJ7 -20 1
DBREF 1OJ7 D 2 387 UNP Q46856 YQHD_ECOLI 2 387
SEQADV 1OJ7 HIS A 213 UNP Q46856 GLN 213 CONFLICT
SEQADV 1OJ7 HIS B 213 UNP Q46856 GLN 213 CONFLICT
SEQADV 1OJ7 HIS C 213 UNP Q46856 GLN 213 CONFLICT
SEQADV 1OJ7 HIS D 213 UNP Q46856 GLN 213 CONFLICT
SEQRES 1 A 408 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 A 408 THR SER LEU TYR LYS LYS ALA GLY LEU ASN ASN PHE ASN
SEQRES 3 A 408 LEU HIS THR PRO THR ARG ILE LEU PHE GLY LYS GLY ALA
SEQRES 4 A 408 ILE ALA GLY LEU ARG GLU GLN ILE PRO HIS ASP ALA ARG
SEQRES 5 A 408 VAL LEU ILE THR TYR GLY GLY GLY SER VAL LYS LYS THR
SEQRES 6 A 408 GLY VAL LEU ASP GLN VAL LEU ASP ALA LEU LYS GLY MET
SEQRES 7 A 408 ASP VAL LEU GLU PHE GLY GLY ILE GLU PRO ASN PRO ALA
SEQRES 8 A 408 TYR GLU THR LEU MET ASN ALA VAL LYS LEU VAL ARG GLU
SEQRES 9 A 408 GLN LYS VAL THR PHE LEU LEU ALA VAL GLY GLY GLY SER
SEQRES 10 A 408 VAL LEU ASP GLY THR LYS PHE ILE ALA ALA ALA ALA ASN
SEQRES 11 A 408 TYR PRO GLU ASN ILE ASP PRO TRP HIS ILE LEU GLN THR
SEQRES 12 A 408 GLY GLY LYS GLU ILE LYS SER ALA ILE PRO MET GLY CYS
SEQRES 13 A 408 VAL LEU THR LEU PRO ALA THR GLY SER GLU SER ASN ALA
SEQRES 14 A 408 GLY ALA VAL ILE SER ARG LYS THR THR GLY ASP LYS GLN
SEQRES 15 A 408 ALA PHE HIS SER ALA HIS VAL GLN PRO VAL PHE ALA VAL
SEQRES 16 A 408 LEU ASP PRO VAL TYR THR TYR THR LEU PRO PRO ARG GLN
SEQRES 17 A 408 VAL ALA ASN GLY VAL VAL ASP ALA PHE VAL HIS THR VAL
SEQRES 18 A 408 GLU GLN TYR VAL THR LYS PRO VAL ASP ALA LYS ILE HIS
SEQRES 19 A 408 ASP ARG PHE ALA GLU GLY ILE LEU LEU THR LEU ILE GLU
SEQRES 20 A 408 ASP GLY PRO LYS ALA LEU LYS GLU PRO GLU ASN TYR ASP
SEQRES 21 A 408 VAL ARG ALA ASN VAL MET TRP ALA ALA THR GLN ALA LEU
SEQRES 22 A 408 ASN GLY LEU ILE GLY ALA GLY VAL PRO GLN ASP TRP ALA
SEQRES 23 A 408 THR HIS MET LEU GLY HIS GLU LEU THR ALA MET HIS GLY
SEQRES 24 A 408 LEU ASP HIS ALA GLN THR LEU ALA ILE VAL LEU PRO ALA
SEQRES 25 A 408 LEU TRP ASN GLU LYS ARG ASP THR LYS ARG ALA LYS LEU
SEQRES 26 A 408 LEU GLN TYR ALA GLU ARG VAL TRP ASN ILE THR GLU GLY
SEQRES 27 A 408 SER ASP ASP GLU ARG ILE ASP ALA ALA ILE ALA ALA THR
SEQRES 28 A 408 ARG ASN PHE PHE GLU GLN LEU GLY VAL PRO THR HIS LEU
SEQRES 29 A 408 SER ASP TYR GLY LEU ASP GLY SER SER ILE PRO ALA LEU
SEQRES 30 A 408 LEU LYS LYS LEU GLU GLU HIS GLY MET THR GLN LEU GLY
SEQRES 31 A 408 GLU ASN HIS ASP ILE THR LEU ASP VAL SER ARG ARG ILE
SEQRES 32 A 408 TYR GLU ALA ALA ARG
SEQRES 1 B 408 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 B 408 THR SER LEU TYR LYS LYS ALA GLY LEU ASN ASN PHE ASN
SEQRES 3 B 408 LEU HIS THR PRO THR ARG ILE LEU PHE GLY LYS GLY ALA
SEQRES 4 B 408 ILE ALA GLY LEU ARG GLU GLN ILE PRO HIS ASP ALA ARG
SEQRES 5 B 408 VAL LEU ILE THR TYR GLY GLY GLY SER VAL LYS LYS THR
SEQRES 6 B 408 GLY VAL LEU ASP GLN VAL LEU ASP ALA LEU LYS GLY MET
SEQRES 7 B 408 ASP VAL LEU GLU PHE GLY GLY ILE GLU PRO ASN PRO ALA
SEQRES 8 B 408 TYR GLU THR LEU MET ASN ALA VAL LYS LEU VAL ARG GLU
SEQRES 9 B 408 GLN LYS VAL THR PHE LEU LEU ALA VAL GLY GLY GLY SER
SEQRES 10 B 408 VAL LEU ASP GLY THR LYS PHE ILE ALA ALA ALA ALA ASN
SEQRES 11 B 408 TYR PRO GLU ASN ILE ASP PRO TRP HIS ILE LEU GLN THR
SEQRES 12 B 408 GLY GLY LYS GLU ILE LYS SER ALA ILE PRO MET GLY CYS
SEQRES 13 B 408 VAL LEU THR LEU PRO ALA THR GLY SER GLU SER ASN ALA
SEQRES 14 B 408 GLY ALA VAL ILE SER ARG LYS THR THR GLY ASP LYS GLN
SEQRES 15 B 408 ALA PHE HIS SER ALA HIS VAL GLN PRO VAL PHE ALA VAL
SEQRES 16 B 408 LEU ASP PRO VAL TYR THR TYR THR LEU PRO PRO ARG GLN
SEQRES 17 B 408 VAL ALA ASN GLY VAL VAL ASP ALA PHE VAL HIS THR VAL
SEQRES 18 B 408 GLU GLN TYR VAL THR LYS PRO VAL ASP ALA LYS ILE HIS
SEQRES 19 B 408 ASP ARG PHE ALA GLU GLY ILE LEU LEU THR LEU ILE GLU
SEQRES 20 B 408 ASP GLY PRO LYS ALA LEU LYS GLU PRO GLU ASN TYR ASP
SEQRES 21 B 408 VAL ARG ALA ASN VAL MET TRP ALA ALA THR GLN ALA LEU
SEQRES 22 B 408 ASN GLY LEU ILE GLY ALA GLY VAL PRO GLN ASP TRP ALA
SEQRES 23 B 408 THR HIS MET LEU GLY HIS GLU LEU THR ALA MET HIS GLY
SEQRES 24 B 408 LEU ASP HIS ALA GLN THR LEU ALA ILE VAL LEU PRO ALA
SEQRES 25 B 408 LEU TRP ASN GLU LYS ARG ASP THR LYS ARG ALA LYS LEU
SEQRES 26 B 408 LEU GLN TYR ALA GLU ARG VAL TRP ASN ILE THR GLU GLY
SEQRES 27 B 408 SER ASP ASP GLU ARG ILE ASP ALA ALA ILE ALA ALA THR
SEQRES 28 B 408 ARG ASN PHE PHE GLU GLN LEU GLY VAL PRO THR HIS LEU
SEQRES 29 B 408 SER ASP TYR GLY LEU ASP GLY SER SER ILE PRO ALA LEU
SEQRES 30 B 408 LEU LYS LYS LEU GLU GLU HIS GLY MET THR GLN LEU GLY
SEQRES 31 B 408 GLU ASN HIS ASP ILE THR LEU ASP VAL SER ARG ARG ILE
SEQRES 32 B 408 TYR GLU ALA ALA ARG
SEQRES 1 C 408 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 C 408 THR SER LEU TYR LYS LYS ALA GLY LEU ASN ASN PHE ASN
SEQRES 3 C 408 LEU HIS THR PRO THR ARG ILE LEU PHE GLY LYS GLY ALA
SEQRES 4 C 408 ILE ALA GLY LEU ARG GLU GLN ILE PRO HIS ASP ALA ARG
SEQRES 5 C 408 VAL LEU ILE THR TYR GLY GLY GLY SER VAL LYS LYS THR
SEQRES 6 C 408 GLY VAL LEU ASP GLN VAL LEU ASP ALA LEU LYS GLY MET
SEQRES 7 C 408 ASP VAL LEU GLU PHE GLY GLY ILE GLU PRO ASN PRO ALA
SEQRES 8 C 408 TYR GLU THR LEU MET ASN ALA VAL LYS LEU VAL ARG GLU
SEQRES 9 C 408 GLN LYS VAL THR PHE LEU LEU ALA VAL GLY GLY GLY SER
SEQRES 10 C 408 VAL LEU ASP GLY THR LYS PHE ILE ALA ALA ALA ALA ASN
SEQRES 11 C 408 TYR PRO GLU ASN ILE ASP PRO TRP HIS ILE LEU GLN THR
SEQRES 12 C 408 GLY GLY LYS GLU ILE LYS SER ALA ILE PRO MET GLY CYS
SEQRES 13 C 408 VAL LEU THR LEU PRO ALA THR GLY SER GLU SER ASN ALA
SEQRES 14 C 408 GLY ALA VAL ILE SER ARG LYS THR THR GLY ASP LYS GLN
SEQRES 15 C 408 ALA PHE HIS SER ALA HIS VAL GLN PRO VAL PHE ALA VAL
SEQRES 16 C 408 LEU ASP PRO VAL TYR THR TYR THR LEU PRO PRO ARG GLN
SEQRES 17 C 408 VAL ALA ASN GLY VAL VAL ASP ALA PHE VAL HIS THR VAL
SEQRES 18 C 408 GLU GLN TYR VAL THR LYS PRO VAL ASP ALA LYS ILE HIS
SEQRES 19 C 408 ASP ARG PHE ALA GLU GLY ILE LEU LEU THR LEU ILE GLU
SEQRES 20 C 408 ASP GLY PRO LYS ALA LEU LYS GLU PRO GLU ASN TYR ASP
SEQRES 21 C 408 VAL ARG ALA ASN VAL MET TRP ALA ALA THR GLN ALA LEU
SEQRES 22 C 408 ASN GLY LEU ILE GLY ALA GLY VAL PRO GLN ASP TRP ALA
SEQRES 23 C 408 THR HIS MET LEU GLY HIS GLU LEU THR ALA MET HIS GLY
SEQRES 24 C 408 LEU ASP HIS ALA GLN THR LEU ALA ILE VAL LEU PRO ALA
SEQRES 25 C 408 LEU TRP ASN GLU LYS ARG ASP THR LYS ARG ALA LYS LEU
SEQRES 26 C 408 LEU GLN TYR ALA GLU ARG VAL TRP ASN ILE THR GLU GLY
SEQRES 27 C 408 SER ASP ASP GLU ARG ILE ASP ALA ALA ILE ALA ALA THR
SEQRES 28 C 408 ARG ASN PHE PHE GLU GLN LEU GLY VAL PRO THR HIS LEU
SEQRES 29 C 408 SER ASP TYR GLY LEU ASP GLY SER SER ILE PRO ALA LEU
SEQRES 30 C 408 LEU LYS LYS LEU GLU GLU HIS GLY MET THR GLN LEU GLY
SEQRES 31 C 408 GLU ASN HIS ASP ILE THR LEU ASP VAL SER ARG ARG ILE
SEQRES 32 C 408 TYR GLU ALA ALA ARG
SEQRES 1 D 408 MET SER TYR TYR HIS HIS HIS HIS HIS HIS LEU GLU SER
SEQRES 2 D 408 THR SER LEU TYR LYS LYS ALA GLY LEU ASN ASN PHE ASN
SEQRES 3 D 408 LEU HIS THR PRO THR ARG ILE LEU PHE GLY LYS GLY ALA
SEQRES 4 D 408 ILE ALA GLY LEU ARG GLU GLN ILE PRO HIS ASP ALA ARG
SEQRES 5 D 408 VAL LEU ILE THR TYR GLY GLY GLY SER VAL LYS LYS THR
SEQRES 6 D 408 GLY VAL LEU ASP GLN VAL LEU ASP ALA LEU LYS GLY MET
SEQRES 7 D 408 ASP VAL LEU GLU PHE GLY GLY ILE GLU PRO ASN PRO ALA
SEQRES 8 D 408 TYR GLU THR LEU MET ASN ALA VAL LYS LEU VAL ARG GLU
SEQRES 9 D 408 GLN LYS VAL THR PHE LEU LEU ALA VAL GLY GLY GLY SER
SEQRES 10 D 408 VAL LEU ASP GLY THR LYS PHE ILE ALA ALA ALA ALA ASN
SEQRES 11 D 408 TYR PRO GLU ASN ILE ASP PRO TRP HIS ILE LEU GLN THR
SEQRES 12 D 408 GLY GLY LYS GLU ILE LYS SER ALA ILE PRO MET GLY CYS
SEQRES 13 D 408 VAL LEU THR LEU PRO ALA THR GLY SER GLU SER ASN ALA
SEQRES 14 D 408 GLY ALA VAL ILE SER ARG LYS THR THR GLY ASP LYS GLN
SEQRES 15 D 408 ALA PHE HIS SER ALA HIS VAL GLN PRO VAL PHE ALA VAL
SEQRES 16 D 408 LEU ASP PRO VAL TYR THR TYR THR LEU PRO PRO ARG GLN
SEQRES 17 D 408 VAL ALA ASN GLY VAL VAL ASP ALA PHE VAL HIS THR VAL
SEQRES 18 D 408 GLU GLN TYR VAL THR LYS PRO VAL ASP ALA LYS ILE HIS
SEQRES 19 D 408 ASP ARG PHE ALA GLU GLY ILE LEU LEU THR LEU ILE GLU
SEQRES 20 D 408 ASP GLY PRO LYS ALA LEU LYS GLU PRO GLU ASN TYR ASP
SEQRES 21 D 408 VAL ARG ALA ASN VAL MET TRP ALA ALA THR GLN ALA LEU
SEQRES 22 D 408 ASN GLY LEU ILE GLY ALA GLY VAL PRO GLN ASP TRP ALA
SEQRES 23 D 408 THR HIS MET LEU GLY HIS GLU LEU THR ALA MET HIS GLY
SEQRES 24 D 408 LEU ASP HIS ALA GLN THR LEU ALA ILE VAL LEU PRO ALA
SEQRES 25 D 408 LEU TRP ASN GLU LYS ARG ASP THR LYS ARG ALA LYS LEU
SEQRES 26 D 408 LEU GLN TYR ALA GLU ARG VAL TRP ASN ILE THR GLU GLY
SEQRES 27 D 408 SER ASP ASP GLU ARG ILE ASP ALA ALA ILE ALA ALA THR
SEQRES 28 D 408 ARG ASN PHE PHE GLU GLN LEU GLY VAL PRO THR HIS LEU
SEQRES 29 D 408 SER ASP TYR GLY LEU ASP GLY SER SER ILE PRO ALA LEU
SEQRES 30 D 408 LEU LYS LYS LEU GLU GLU HIS GLY MET THR GLN LEU GLY
SEQRES 31 D 408 GLU ASN HIS ASP ILE THR LEU ASP VAL SER ARG ARG ILE
SEQRES 32 D 408 TYR GLU ALA ALA ARG
HET ZN B1389 1
HET ZN C1388 1
HET CL C1389 1
HET ZN D1389 1
HET NZQ A1388 50
HET BO3 A1389 4
HET NZQ B1388 50
HET BO3 C1390 4
HET NZQ D1388 50
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM NZQ 5,6-DIHYDROXY-NADP
HETNAM BO3 BORIC ACID
FORMUL 5 ZN 3(ZN 2+)
FORMUL 7 CL CL 1-
FORMUL 9 NZQ 3(C21 H32 N7 O19 P3)
FORMUL 10 BO3 2(B H3 O3)
FORMUL 14 HOH *1494(H2 O1)
HELIX 1 1 GLY A 17 ALA A 20 5 4
HELIX 2 2 GLY A 21 ILE A 26 1 6
HELIX 3 3 GLY A 39 GLY A 45 1 7
HELIX 4 4 GLY A 45 LEU A 54 1 10
HELIX 5 5 ALA A 70 LYS A 85 1 16
HELIX 6 6 GLY A 94 ALA A 108 1 15
HELIX 7 7 TRP A 117 THR A 122 1 6
HELIX 8 8 GLY A 143 ASN A 147 5 5
HELIX 9 9 ALA A 166 GLN A 169 5 4
HELIX 10 10 PRO A 177 TYR A 181 5 5
HELIX 11 11 PRO A 184 VAL A 204 1 21
HELIX 12 12 ALA A 210 GLU A 234 1 25
HELIX 13 13 ASN A 237 LEU A 252 1 16
HELIX 14 14 TRP A 264 GLY A 278 1 15
HELIX 15 15 ASP A 280 LYS A 296 1 17
HELIX 16 16 LYS A 300 ASN A 313 1 14
HELIX 17 17 SER A 318 LEU A 337 1 20
HELIX 18 18 HIS A 342 GLY A 347 5 6
HELIX 19 19 SER A 352 HIS A 363 1 12
HELIX 20 20 THR A 375 ALA A 386 1 12
HELIX 21 21 GLY B 17 ALA B 20 5 4
HELIX 22 22 GLY B 21 ILE B 26 1 6
HELIX 23 23 GLY B 39 THR B 44 1 6
HELIX 24 24 GLY B 45 LEU B 54 1 10
HELIX 25 25 ALA B 70 LYS B 85 1 16
HELIX 26 26 GLY B 94 ASN B 109 1 16
HELIX 27 27 TRP B 117 THR B 122 1 6
HELIX 28 28 GLY B 143 ASN B 147 5 5
HELIX 29 29 ALA B 166 GLN B 169 5 4
HELIX 30 30 ASP B 176 TYR B 181 5 6
HELIX 31 31 PRO B 184 GLN B 202 1 19
HELIX 32 32 ALA B 210 GLU B 234 1 25
HELIX 33 33 ASN B 237 LEU B 252 1 16
HELIX 34 34 TRP B 264 GLY B 278 1 15
HELIX 35 35 ASP B 280 LYS B 296 1 17
HELIX 36 36 LYS B 300 ASN B 313 1 14
HELIX 37 37 SER B 318 GLY B 338 1 21
HELIX 38 38 HIS B 342 GLY B 347 5 6
HELIX 39 39 SER B 352 HIS B 363 1 12
HELIX 40 40 THR B 375 ALA B 386 1 12
HELIX 41 41 GLY C 17 GLN C 25 5 9
HELIX 42 42 GLY C 39 THR C 44 1 6
HELIX 43 43 GLY C 45 LEU C 54 1 10
HELIX 44 44 ALA C 70 LYS C 85 1 16
HELIX 45 45 GLY C 94 TYR C 110 1 17
HELIX 46 46 TRP C 117 THR C 122 1 6
HELIX 47 47 GLY C 143 ASN C 147 5 5
HELIX 48 48 ALA C 166 GLN C 169 5 4
HELIX 49 49 ASP C 176 TYR C 181 5 6
HELIX 50 50 PRO C 184 GLU C 201 1 18
HELIX 51 51 ALA C 210 GLU C 234 1 25
HELIX 52 52 ASN C 237 LEU C 252 1 16
HELIX 53 53 TRP C 264 GLY C 278 1 15
HELIX 54 54 ASP C 280 LYS C 296 1 17
HELIX 55 55 LYS C 300 ASN C 313 1 14
HELIX 56 56 SER C 318 LEU C 337 1 20
HELIX 57 57 HIS C 342 GLY C 347 5 6
HELIX 58 58 SER C 352 HIS C 363 1 12
HELIX 59 59 THR C 375 ALA C 386 1 12
HELIX 60 60 GLY D 17 ALA D 20 5 4
HELIX 61 61 GLY D 21 ILE D 26 1 6
HELIX 62 62 GLY D 39 GLY D 45 1 7
HELIX 63 63 GLY D 45 LEU D 54 1 10
HELIX 64 64 ALA D 70 GLN D 84 1 15
HELIX 65 65 GLY D 94 ALA D 108 1 15
HELIX 66 66 TRP D 117 THR D 122 1 6
HELIX 67 67 GLY D 143 ASN D 147 5 5
HELIX 68 68 ALA D 166 GLN D 169 5 4
HELIX 69 69 PRO D 177 TYR D 181 5 5
HELIX 70 70 PRO D 184 GLN D 202 1 19
HELIX 71 71 ALA D 210 GLU D 234 1 25
HELIX 72 72 ASN D 237 LEU D 252 1 16
HELIX 73 73 TRP D 264 GLY D 278 1 15
HELIX 74 74 ASP D 280 LYS D 296 1 17
HELIX 75 75 LYS D 300 ASN D 313 1 14
HELIX 76 76 SER D 318 LEU D 337 1 20
HELIX 77 77 HIS D 342 GLY D 347 5 6
HELIX 78 78 SER D 352 HIS D 363 1 12
HELIX 79 79 THR D 375 ALA D 386 1 12
SHEET 1 AA12 ASP A 58 PHE A 62 0
SHEET 2 AA12 ARG A 31 TYR A 36 1 O VAL A 32 N LEU A 60
SHEET 3 AA12 PHE A 88 GLY A 93 1 O PHE A 88 N LEU A 33
SHEET 4 AA12 MET A 133 LEU A 137 1 O GLY A 134 N ALA A 91
SHEET 5 AA12 PHE A 172 LEU A 175 1 O PHE A 172 N CYS A 135
SHEET 6 AA12 PHE A 4 PHE A 14 1 O ARG A 11 N ALA A 173
SHEET 7 AA12 PHE D 4 PHE D 14 -1 O PHE D 4 N PHE A 14
SHEET 8 AA12 PHE D 172 LEU D 175 1 O ALA D 173 N LEU D 13
SHEET 9 AA12 MET D 133 LEU D 137 1 O CYS D 135 N VAL D 174
SHEET 10 AA12 PHE D 88 GLY D 93 1 O LEU D 89 N GLY D 134
SHEET 11 AA12 ARG D 31 THR D 35 1 O ARG D 31 N PHE D 88
SHEET 12 AA12 ASP D 58 PHE D 62 1 O ASP D 58 N VAL D 32
SHEET 1 AB 2 GLY A 149 ARG A 154 0
SHEET 2 AB 2 ASP A 159 HIS A 164 -1 O ASP A 159 N ARG A 154
SHEET 1 BA12 ASP B 58 PHE B 62 0
SHEET 2 BA12 ARG B 31 THR B 35 1 O VAL B 32 N LEU B 60
SHEET 3 BA12 PHE B 88 GLY B 93 1 O PHE B 88 N LEU B 33
SHEET 4 BA12 MET B 133 LEU B 137 1 O GLY B 134 N ALA B 91
SHEET 5 BA12 PHE B 172 LEU B 175 1 O PHE B 172 N CYS B 135
SHEET 6 BA12 PHE B 4 PHE B 14 1 O ARG B 11 N ALA B 173
SHEET 7 BA12 PHE C 4 PHE C 14 -1 O PHE C 4 N PHE B 14
SHEET 8 BA12 PHE C 172 LEU C 175 1 O ALA C 173 N LEU C 13
SHEET 9 BA12 MET C 133 LEU C 137 1 O CYS C 135 N VAL C 174
SHEET 10 BA12 PHE C 88 GLY C 93 1 O LEU C 89 N GLY C 134
SHEET 11 BA12 ARG C 31 TYR C 36 1 O LEU C 33 N LEU C 90
SHEET 12 BA12 ASP C 58 PHE C 62 1 O ASP C 58 N VAL C 32
SHEET 1 BB 2 GLY B 149 ARG B 154 0
SHEET 2 BB 2 ASP B 159 HIS B 164 -1 O ASP B 159 N ARG B 154
SHEET 1 CA 2 GLY C 149 ARG C 154 0
SHEET 2 CA 2 ASP C 159 HIS C 164 -1 O ASP C 159 N ARG C 154
SHEET 1 DA 2 GLY D 149 ARG D 154 0
SHEET 2 DA 2 ASP D 159 HIS D 164 -1 O ASP D 159 N ARG D 154
LINK O5N NZQ B1388 ZN ZN B1389 1555 1555 1.75
LINK ZN ZN B1389 NE2 HIS B 198 1555 1555 2.55
LINK ZN ZN B1389 NE2 HIS B 267 1555 1555 2.11
LINK ZN ZN B1389 NE2 HIS B 281 1555 1555 2.12
LINK ZN ZN B1389 OD1 ASP B 194 1555 1555 2.04
LINK ZN ZN C1388 NE2 HIS C 198 1555 1555 2.32
LINK ZN ZN C1388 NE2 HIS C 281 1555 1555 2.18
LINK ZN ZN C1388 O2 BO3 C1390 1555 1555 2.44
LINK ZN ZN C1388 O3 BO3 C1390 1555 1555 2.52
LINK ZN ZN C1388 NE2 HIS C 267 1555 1555 2.13
LINK ZN ZN C1388 OD1 ASP C 194 1555 1555 2.16
LINK O5N NZQ D1388 ZN ZN D1389 1555 1555 1.90
LINK ZN ZN D1389 NE2 HIS D 281 1555 1555 2.09
LINK ZN ZN D1389 NE2 HIS D 267 1555 1555 2.11
LINK ZN ZN D1389 NE2 HIS D 198 1555 1555 2.57
LINK ZN ZN D1389 OD1 ASP D 194 1555 1555 1.98
SITE 1 AC1 5 ASP B 194 HIS B 198 HIS B 267 HIS B 281
SITE 2 AC1 5 NZQ B1388
SITE 1 AC2 5 ASP C 194 HIS C 198 HIS C 267 HIS C 281
SITE 2 AC2 5 BO3 C1390
SITE 1 AC3 5 GLY C 38 GLY C 39 SER C 40 HOH C2031
SITE 2 AC3 5 HOH C2064
SITE 1 AC4 6 ASP D 194 HIS D 198 HIS D 267 HIS D 281
SITE 2 AC4 6 LEU D 285 NZQ D1388
SITE 1 AC5 44 GLY A 38 GLY A 39 SER A 40 PRO A 67
SITE 2 AC5 44 ASN A 68 GLY A 94 GLY A 95 SER A 96
SITE 3 AC5 44 ASP A 99 THR A 138 LEU A 139 ALA A 141
SITE 4 AC5 44 THR A 142 SER A 144 ASN A 147 GLY A 149
SITE 5 AC5 44 VAL A 151 LYS A 160 TYR A 179 THR A 182
SITE 6 AC5 44 LEU A 183 GLN A 187 ASP A 194 HIS A 198
SITE 7 AC5 44 HIS A 267 HIS A 271 HIS A 281 HOH A2069
SITE 8 AC5 44 HOH A2134 HOH A2170 HOH A2352 HOH A2353
SITE 9 AC5 44 HOH A2354 HOH A2355 HOH A2356 HOH A2357
SITE 10 AC5 44 HOH A2358 HOH A2359 HOH A2360 HOH A2361
SITE 11 AC5 44 HOH A2362 HOH A2363 HOH A2364 HOH A2365
SITE 1 AC6 6 ARG A 186 ASN A 190 ASP A 280 GLN A 283
SITE 2 AC6 6 GLY A 338 VAL A 339
SITE 1 AC7 46 GLY B 38 GLY B 39 SER B 40 PRO B 67
SITE 2 AC7 46 ASN B 68 GLY B 94 GLY B 95 SER B 96
SITE 3 AC7 46 ASP B 99 THR B 138 LEU B 139 ALA B 141
SITE 4 AC7 46 THR B 142 SER B 144 ASN B 147 GLY B 149
SITE 5 AC7 46 VAL B 151 LYS B 160 TYR B 179 THR B 182
SITE 6 AC7 46 LEU B 183 PRO B 184 GLN B 187 ASP B 194
SITE 7 AC7 46 HIS B 198 LEU B 252 HIS B 267 HIS B 271
SITE 8 AC7 46 HIS B 281 ZN B1389 HOH B2083 HOH B2161
SITE 9 AC7 46 HOH B2171 HOH B2210 HOH B2417 HOH B2418
SITE 10 AC7 46 HOH B2419 HOH B2420 HOH B2421 HOH B2422
SITE 11 AC7 46 HOH B2423 HOH B2424 HOH B2425 HOH B2426
SITE 12 AC7 46 HOH B2427 HOH B2428
SITE 1 AC8 5 ASP C 194 HIS C 198 HIS C 267 HIS C 281
SITE 2 AC8 5 ZN C1388
SITE 1 AC9 43 GLY D 38 GLY D 39 SER D 40 PRO D 67
SITE 2 AC9 43 ASN D 68 GLY D 94 GLY D 95 SER D 96
SITE 3 AC9 43 ASP D 99 THR D 138 LEU D 139 ALA D 141
SITE 4 AC9 43 THR D 142 SER D 144 ASN D 147 GLY D 149
SITE 5 AC9 43 VAL D 151 LYS D 160 TYR D 179 THR D 182
SITE 6 AC9 43 LEU D 183 GLN D 187 ASP D 194 HIS D 198
SITE 7 AC9 43 HIS D 267 HIS D 271 HIS D 281 ZN D1389
SITE 8 AC9 43 HOH D2090 HOH D2282 HOH D2283 HOH D2284
SITE 9 AC9 43 HOH D2285 HOH D2286 HOH D2287 HOH D2288
SITE 10 AC9 43 HOH D2289 HOH D2290 HOH D2292 HOH D2293
SITE 11 AC9 43 HOH D2294 HOH D2295 HOH D2296
CRYST1 237.925 237.925 66.744 90.00 90.00 120.00 P 62 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 0.004203 0.002427 0.000000 0.00000
SCALE2 0.000000 0.004853 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014983 0.00000
MTRIX1 1 0.460470 0.091240 -0.882970 56.95176 1
MTRIX2 1 0.760680 0.472140 0.445480 -61.81264 1
MTRIX3 1 0.457530 -0.876790 0.148010 -48.72829 1
MTRIX1 2 0.375690 0.082390 -0.923080 67.36762 1
MTRIX2 2 -0.787740 -0.496290 -0.364910 95.38748 1
MTRIX3 2 -0.488180 0.864240 -0.121550 114.93341 1
MTRIX1 3 -0.620270 0.067680 -0.781460 197.64517 1
MTRIX2 3 0.070610 -0.987410 -0.141560 -66.61557 1
MTRIX3 3 -0.781200 -0.142980 0.607680 90.04625 1
(ATOM LINES ARE NOT SHOWN.)
END