HEADER OXIDOREDUCTASE 22-SEP-09 3JZ4
TITLE CRYSTAL STRUCTURE OF E. COLI NADP DEPENDENT ENZYME
CAVEAT 3JZ4 CHIRALITY ERROR AT CA CENTER OF LYS1C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUCCINATE-SEMIALDEHYDE DEHYDROGENASE [NADP+];
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: SSDH, NADP DEPENDENT ENZYME;
COMPND 5 EC: 1.2.1.16;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: MC1061;
SOURCE 5 GENE: B2661, GABD, JW2636, NA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSETC
KEYWDS TETRAMER, NADP BINDING, NADP, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.G.LANGENDORF,T.L.G.KEY,G.FENALTI,W.T.KAN,A.M.BUCKLE,T.CARADOC-
AUTHOR 2 DAVIES,K.L.TUCK,R.H.P.LAW,J.C.WHISSTOCK
REVDAT 3 21-FEB-24 3JZ4 1 REMARK
REVDAT 2 13-JUL-11 3JZ4 1 VERSN
REVDAT 1 16-MAR-10 3JZ4 0
JRNL AUTH C.G.LANGENDORF,T.L.KEY,G.FENALTI,W.T.KAN,A.M.BUCKLE,
JRNL AUTH 2 T.CARADOC-DAVIES,K.L.TUCK,R.H.LAW,J.C.WHISSTOCK
JRNL TITL THE X-RAY CRYSTAL STRUCTURE OF ESCHERICHIA COLI SUCCINIC
JRNL TITL 2 SEMIALDEHYDE DEHYDROGENASE; STRUCTURAL INSIGHTS INTO
JRNL TITL 3 NADP+/ENZYME INTERACTIONS.
JRNL REF PLOS ONE V. 5 E9280 2010
JRNL REFN ESSN 1932-6203
JRNL PMID 20174634
JRNL DOI 10.1371/JOURNAL.PONE.0009280
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.3
REMARK 3 NUMBER OF REFLECTIONS : 74545
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3717
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4599
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.1700
REMARK 3 BIN FREE R VALUE SET COUNT : 246
REMARK 3 BIN FREE R VALUE : 0.2140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 331
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) : 19.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.14000
REMARK 3 B22 (A**2) : -0.14000
REMARK 3 B33 (A**2) : 0.28000
REMARK 3 B12 (A**2) : 0.00000
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): 0.518
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.243
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.158
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.053
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15060 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20475 ; 1.297 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1977 ; 6.056 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 639 ;34.037 ;24.664
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2456 ;14.890 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 87 ;14.936 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2294 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11437 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7251 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10370 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 800 ; 0.136 ; 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): 71 ; 0.264 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.136 ; 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): 9851 ; 1.456 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15300 ; 2.191 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5862 ; 1.845 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5150 ; 2.775 ; 6.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 12
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 9 1
REMARK 3 1 B 2 B 9 1
REMARK 3 1 C 2 C 9 1
REMARK 3 1 D 2 D 9 1
REMARK 3 2 A 10 A 208 1
REMARK 3 2 B 10 B 208 1
REMARK 3 2 C 10 C 208 1
REMARK 3 2 D 10 D 208 1
REMARK 3 3 A 209 A 214 6
REMARK 3 3 B 209 B 214 6
REMARK 3 3 C 209 C 214 6
REMARK 3 3 D 209 D 214 6
REMARK 3 4 A 215 A 312 1
REMARK 3 4 B 215 B 312 1
REMARK 3 4 C 215 C 312 1
REMARK 3 4 D 215 D 312 1
REMARK 3 5 A 313 A 316 6
REMARK 3 5 B 313 B 316 6
REMARK 3 5 C 313 C 316 6
REMARK 3 5 D 313 D 316 6
REMARK 3 6 A 317 A 329 1
REMARK 3 6 B 317 B 329 1
REMARK 3 6 C 317 C 329 1
REMARK 3 6 D 317 D 329 1
REMARK 3 7 A 330 A 359 4
REMARK 3 7 B 330 B 359 4
REMARK 3 7 C 330 C 359 4
REMARK 3 7 D 330 D 359 4
REMARK 3 8 A 360 A 365 3
REMARK 3 8 B 360 B 365 3
REMARK 3 8 C 360 C 365 3
REMARK 3 8 D 360 D 365 3
REMARK 3 9 A 366 A 400 4
REMARK 3 9 B 366 B 400 4
REMARK 3 9 C 366 C 400 4
REMARK 3 9 D 366 D 400 4
REMARK 3 10 A 401 A 462 1
REMARK 3 10 B 401 B 462 1
REMARK 3 10 C 401 C 462 1
REMARK 3 10 D 401 D 462 1
REMARK 3 11 A 463 A 466 6
REMARK 3 11 B 463 B 466 6
REMARK 3 11 C 463 C 466 6
REMARK 3 11 D 463 D 466 6
REMARK 3 12 A 467 A 481 1
REMARK 3 12 B 467 B 481 1
REMARK 3 12 C 467 C 481 1
REMARK 3 12 D 467 D 481 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2939 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 2939 ; 0.060 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 C (A): 2939 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 D (A): 2939 ; 0.040 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 467 ; 0.600 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 467 ; 0.660 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 467 ; 0.390 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 467 ; 0.360 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 107 ; 0.390 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 107 ; 0.620 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 C (A): 107 ; 0.290 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 D (A): 107 ; 0.580 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 2939 ; 0.110 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 2939 ; 0.100 ; 0.500
REMARK 3 TIGHT THERMAL 1 C (A**2): 2939 ; 0.090 ; 0.500
REMARK 3 TIGHT THERMAL 1 D (A**2): 2939 ; 0.090 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 467 ; 0.740 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 467 ; 0.680 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 467 ; 0.660 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 467 ; 0.610 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 107 ; 5.270 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 107 ; 2.600 ;10.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 107 ; 2.910 ;10.000
REMARK 3 LOOSE THERMAL 1 D (A**2): 107 ; 2.240 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 60
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6630 42.5695 9.8909
REMARK 3 T TENSOR
REMARK 3 T11: 0.0244 T22: 0.1192
REMARK 3 T33: 0.0769 T12: -0.0024
REMARK 3 T13: 0.0470 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.0855 L22: 1.3283
REMARK 3 L33: 1.3322 L12: -0.5949
REMARK 3 L13: 0.1826 L23: -0.7105
REMARK 3 S TENSOR
REMARK 3 S11: 0.0628 S12: 0.1446 S13: 0.0794
REMARK 3 S21: -0.1138 S22: -0.0783 S23: -0.1429
REMARK 3 S31: -0.0358 S32: 0.1623 S33: 0.0155
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 61 A 264
REMARK 3 ORIGIN FOR THE GROUP (A): -18.8533 38.6646 22.3396
REMARK 3 T TENSOR
REMARK 3 T11: 0.0567 T22: 0.0788
REMARK 3 T33: 0.0674 T12: 0.0094
REMARK 3 T13: 0.0009 T23: -0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.3491 L22: 0.2799
REMARK 3 L33: 0.2499 L12: -0.0223
REMARK 3 L13: -0.1254 L23: 0.0717
REMARK 3 S TENSOR
REMARK 3 S11: 0.0194 S12: -0.0011 S13: 0.0186
REMARK 3 S21: -0.0213 S22: -0.0026 S23: -0.0170
REMARK 3 S31: 0.0173 S32: 0.0115 S33: -0.0168
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 265 A 394
REMARK 3 ORIGIN FOR THE GROUP (A): -37.7593 60.4983 11.5624
REMARK 3 T TENSOR
REMARK 3 T11: 0.0436 T22: 0.0345
REMARK 3 T33: 0.0473 T12: 0.0277
REMARK 3 T13: -0.0047 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 3.8948 L22: 0.9834
REMARK 3 L33: 1.9213 L12: -0.1409
REMARK 3 L13: -1.1066 L23: -0.2592
REMARK 3 S TENSOR
REMARK 3 S11: 0.1395 S12: 0.3585 S13: 0.1655
REMARK 3 S21: -0.1257 S22: -0.0385 S23: 0.0371
REMARK 3 S31: -0.0567 S32: -0.1456 S33: -0.1010
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 395 A 481
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7237 42.0862 26.0531
REMARK 3 T TENSOR
REMARK 3 T11: 0.0550 T22: 0.0723
REMARK 3 T33: 0.0563 T12: -0.0216
REMARK 3 T13: 0.0197 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.3850 L22: 1.6560
REMARK 3 L33: 0.5432 L12: -1.0486
REMARK 3 L13: 0.2867 L23: -0.2946
REMARK 3 S TENSOR
REMARK 3 S11: -0.0647 S12: 0.0367 S13: 0.0805
REMARK 3 S21: 0.0762 S22: 0.0346 S23: 0.0265
REMARK 3 S31: -0.0008 S32: -0.0565 S33: 0.0301
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 : B 1 B 58
REMARK 3 ORIGIN FOR THE GROUP (A): -55.6011 9.5843 15.0519
REMARK 3 T TENSOR
REMARK 3 T11: 0.1118 T22: 0.0552
REMARK 3 T33: 0.0561 T12: -0.0205
REMARK 3 T13: -0.0327 T23: -0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.2593 L22: 1.9520
REMARK 3 L33: 1.1484 L12: -0.2880
REMARK 3 L13: 0.1905 L23: -0.0676
REMARK 3 S TENSOR
REMARK 3 S11: 0.0452 S12: 0.0049 S13: -0.1307
REMARK 3 S21: -0.2420 S22: -0.0234 S23: 0.3557
REMARK 3 S31: 0.0952 S32: -0.0684 S33: -0.0219
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 59 B 264
REMARK 3 ORIGIN FOR THE GROUP (A): -43.6447 18.4856 25.6486
REMARK 3 T TENSOR
REMARK 3 T11: 0.1031 T22: 0.0648
REMARK 3 T33: 0.0595 T12: -0.0027
REMARK 3 T13: -0.0018 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.3851 L22: 0.2942
REMARK 3 L33: 0.2940 L12: 0.0613
REMARK 3 L13: 0.1253 L23: 0.0599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: -0.0197 S13: -0.0405
REMARK 3 S21: -0.0304 S22: -0.0045 S23: -0.0265
REMARK 3 S31: 0.0407 S32: -0.0177 S33: 0.0010
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 265 B 394
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1530 -5.2586 23.1118
REMARK 3 T TENSOR
REMARK 3 T11: 0.1390 T22: 0.0351
REMARK 3 T33: 0.1316 T12: 0.0299
REMARK 3 T13: 0.0112 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 1.7426 L22: 0.9777
REMARK 3 L33: 0.3645 L12: 0.6777
REMARK 3 L13: 0.3455 L23: 0.5461
REMARK 3 S TENSOR
REMARK 3 S11: 0.0206 S12: 0.1816 S13: -0.3015
REMARK 3 S21: -0.0791 S22: 0.0983 S23: -0.1739
REMARK 3 S31: 0.0564 S32: 0.1003 S33: -0.1189
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 395 B 481
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8980 16.9305 30.7837
REMARK 3 T TENSOR
REMARK 3 T11: 0.0820 T22: 0.0663
REMARK 3 T33: 0.0832 T12: -0.0151
REMARK 3 T13: -0.0139 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.4950 L22: 1.8839
REMARK 3 L33: 0.4586 L12: -1.2100
REMARK 3 L13: 0.1019 L23: 0.0071
REMARK 3 S TENSOR
REMARK 3 S11: -0.0251 S12: -0.0132 S13: -0.0840
REMARK 3 S21: 0.0456 S22: 0.0935 S23: -0.1219
REMARK 3 S31: 0.0931 S32: 0.0352 S33: -0.0684
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 : C 1 C 113
REMARK 3 ORIGIN FOR THE GROUP (A): -54.0411 18.5587 64.7875
REMARK 3 T TENSOR
REMARK 3 T11: 0.2186 T22: 0.0972
REMARK 3 T33: 0.0754 T12: -0.0398
REMARK 3 T13: 0.0525 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.5277 L22: 0.8875
REMARK 3 L33: 1.6996 L12: -0.2171
REMARK 3 L13: -0.7849 L23: 0.0150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0883 S12: 0.0027 S13: -0.0405
REMARK 3 S21: 0.2803 S22: 0.0218 S23: 0.1942
REMARK 3 S31: 0.2185 S32: -0.1143 S33: 0.0665
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 : C 114 C 264
REMARK 3 ORIGIN FOR THE GROUP (A): -41.0866 26.8112 61.6239
REMARK 3 T TENSOR
REMARK 3 T11: 0.2058 T22: 0.1494
REMARK 3 T33: 0.0459 T12: 0.0187
REMARK 3 T13: -0.0004 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.2626 L22: 0.4780
REMARK 3 L33: 0.1848 L12: 0.0432
REMARK 3 L13: 0.0138 L23: 0.0398
REMARK 3 S TENSOR
REMARK 3 S11: -0.0389 S12: -0.0813 S13: 0.0118
REMARK 3 S21: 0.1896 S22: 0.0147 S23: 0.0262
REMARK 3 S31: 0.0946 S32: -0.0063 S33: 0.0242
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 265 C 394
REMARK 3 ORIGIN FOR THE GROUP (A): -63.1539 49.5899 62.3528
REMARK 3 T TENSOR
REMARK 3 T11: 0.1366 T22: 0.1429
REMARK 3 T33: 0.1327 T12: 0.0264
REMARK 3 T13: 0.0598 T23: 0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 0.4743 L22: 3.4833
REMARK 3 L33: 1.6625 L12: 0.6774
REMARK 3 L13: -0.8859 L23: -1.4053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0674 S12: 0.0780 S13: 0.0221
REMARK 3 S21: 0.4945 S22: 0.0712 S23: 0.3743
REMARK 3 S31: -0.1676 S32: -0.1545 S33: -0.1386
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 395 C 481
REMARK 3 ORIGIN FOR THE GROUP (A): -42.7138 44.0675 52.1067
REMARK 3 T TENSOR
REMARK 3 T11: 0.0947 T22: 0.1032
REMARK 3 T33: 0.0571 T12: -0.0126
REMARK 3 T13: 0.0078 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 1.0730 L22: 1.4131
REMARK 3 L33: 0.7445 L12: -0.7520
REMARK 3 L13: 0.2869 L23: -0.1384
REMARK 3 S TENSOR
REMARK 3 S11: -0.0153 S12: -0.1300 S13: 0.0026
REMARK 3 S21: 0.0903 S22: 0.0145 S23: 0.1286
REMARK 3 S31: -0.1009 S32: -0.0940 S33: 0.0008
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 : D 1 D 58
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6225 56.4406 67.4512
REMARK 3 T TENSOR
REMARK 3 T11: 0.1123 T22: 0.2113
REMARK 3 T33: 0.1907 T12: -0.0055
REMARK 3 T13: -0.0665 T23: -0.1372
REMARK 3 L TENSOR
REMARK 3 L11: 4.2339 L22: 1.1823
REMARK 3 L33: 1.6091 L12: -1.1665
REMARK 3 L13: 0.5369 L23: 0.4448
REMARK 3 S TENSOR
REMARK 3 S11: -0.1460 S12: -0.1730 S13: 0.4234
REMARK 3 S21: 0.1435 S22: 0.2569 S23: -0.3337
REMARK 3 S31: -0.2213 S32: 0.2995 S33: -0.1109
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 : D 59 D 264
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0509 44.2967 57.0826
REMARK 3 T TENSOR
REMARK 3 T11: 0.1088 T22: 0.1772
REMARK 3 T33: 0.0842 T12: 0.0254
REMARK 3 T13: -0.0304 T23: -0.0501
REMARK 3 L TENSOR
REMARK 3 L11: 0.3196 L22: 0.4378
REMARK 3 L33: 0.6704 L12: -0.0387
REMARK 3 L13: 0.0250 L23: 0.3872
REMARK 3 S TENSOR
REMARK 3 S11: -0.0376 S12: -0.1562 S13: 0.0324
REMARK 3 S21: 0.0826 S22: 0.1231 S23: -0.1069
REMARK 3 S31: 0.0141 S32: 0.1095 S33: -0.0855
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 265 D 394
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8135 21.8185 68.0400
REMARK 3 T TENSOR
REMARK 3 T11: 0.1914 T22: 0.3615
REMARK 3 T33: 0.0261 T12: 0.1433
REMARK 3 T13: -0.0835 T23: -0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 2.1814 L22: 4.2596
REMARK 3 L33: 1.1932 L12: 0.4329
REMARK 3 L13: 0.4292 L23: 0.6555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0313 S12: -0.6982 S13: 0.0178
REMARK 3 S21: 0.4626 S22: 0.1466 S23: -0.0700
REMARK 3 S31: 0.2537 S32: 0.1558 S33: -0.1153
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 395 D 481
REMARK 3 ORIGIN FOR THE GROUP (A): -20.7966 23.6108 56.2609
REMARK 3 T TENSOR
REMARK 3 T11: 0.1490 T22: 0.1278
REMARK 3 T33: 0.0701 T12: 0.0222
REMARK 3 T13: -0.0269 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 1.3702 L22: 1.2840
REMARK 3 L33: 0.8372 L12: -0.6830
REMARK 3 L13: 0.0354 L23: 0.0059
REMARK 3 S TENSOR
REMARK 3 S11: -0.0525 S12: -0.2283 S13: -0.0634
REMARK 3 S21: 0.2161 S22: 0.0911 S23: -0.1288
REMARK 3 S31: 0.1851 S32: 0.1550 S33: -0.0385
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 : 1.20
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
REMARK 4
REMARK 4 3JZ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055341.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95364
REMARK 200 MONOCHROMATOR : NA
REMARK 200 OPTICS : NA
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74567
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 37.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.18800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.18800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM TARTRATE, 30 % PEG
REMARK 280 3350, 10 MM 2-MERCAPTOETHANOL, 0.1 M TRIS, PH 7.5, TEMPERATURE
REMARK 280 298K, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 75.94250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 75.94250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 75.94250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 75.94250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 75.94250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.94250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 75.94250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.94250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: FOUR MONOMERS RELATED BY NON-CRYSTALLOGRAPHIC 222 SYMETRY
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 ASN A 3 OD1 ND2
REMARK 470 ARG A 50 CZ NH1 NH2
REMARK 470 GLU A 274 CG CD OE1 OE2
REMARK 470 GLU A 341 CD OE1 OE2
REMARK 470 LYS A 358 CG CD CE NZ
REMARK 470 GLU A 361 CD OE1 OE2
REMARK 470 LYS A 397 CE NZ
REMARK 470 GLU A 410 CD OE1 OE2
REMARK 470 ILE A 443 CD1
REMARK 470 ARG B 303 CZ NH1 NH2
REMARK 470 GLU B 306 CD OE1 OE2
REMARK 470 GLN B 310 CD OE1 NE2
REMARK 470 HIS B 316 ND1 CD2 CE1 NE2
REMARK 470 GLU B 333 CG CD OE1 OE2
REMARK 470 LYS B 334 CE NZ
REMARK 470 GLU B 341 CD OE1 OE2
REMARK 470 GLU B 361 OE1 OE2
REMARK 470 LYS B 383 CD CE NZ
REMARK 470 LYS B 397 CD CE NZ
REMARK 470 ASP B 401 CG OD1 OD2
REMARK 470 GLN B 405 CD OE1 NE2
REMARK 470 ILE B 443 CD1
REMARK 470 ARG C 50 CZ NH1 NH2
REMARK 470 GLU C 235 CD OE1 OE2
REMARK 470 GLU C 274 CD OE1 OE2
REMARK 470 GLU C 306 CD OE1 OE2
REMARK 470 GLN C 310 CD OE1 NE2
REMARK 470 LYS C 314 CE NZ
REMARK 470 GLU C 333 CG CD OE1 OE2
REMARK 470 LYS C 334 CD CE NZ
REMARK 470 GLU C 348 OE1 OE2
REMARK 470 LYS C 358 CD CE NZ
REMARK 470 ASP C 401 CG OD1 OD2
REMARK 470 GLN C 405 OE1 NE2
REMARK 470 GLU C 410 CG CD OE1 OE2
REMARK 470 SER D 5 OG
REMARK 470 ARG D 50 CZ NH1 NH2
REMARK 470 ARG D 91 NE CZ NH1 NH2
REMARK 470 GLU D 274 CD OE1 OE2
REMARK 470 ASP D 298 OD1
REMARK 470 GLU D 306 CD OE1 OE2
REMARK 470 ASN D 323 OD1 ND2
REMARK 470 GLU D 333 CG CD OE1 OE2
REMARK 470 LYS D 334 CE NZ
REMARK 470 ASP D 345 OD1 OD2
REMARK 470 GLU D 348 CD OE1 OE2
REMARK 470 LYS D 349 CE NZ
REMARK 470 LYS D 358 CE NZ
REMARK 470 GLU D 361 CG CD OE1 OE2
REMARK 470 LYS D 383 CG CD CE NZ
REMARK 470 LYS D 397 CE NZ
REMARK 470 ASP D 401 OD1 OD2
REMARK 470 ILE D 443 CD1
REMARK 470 GLU D 469 CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP A 54 O HOH A 527 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 34 -8.69 -148.46
REMARK 500 ALA A 212 -93.72 19.65
REMARK 500 LEU A 255 -149.63 -114.16
REMARK 500 LEU A 413 -85.60 -92.82
REMARK 500 LYS A 455 -135.00 56.89
REMARK 500 SER A 464 179.55 67.74
REMARK 500 ASN B 34 -12.00 -150.48
REMARK 500 LYS B 43 72.85 -103.40
REMARK 500 LEU B 255 -154.31 -114.72
REMARK 500 GLN B 286 57.23 -95.86
REMARK 500 LEU B 413 -86.62 -92.09
REMARK 500 LYS B 455 -141.80 55.99
REMARK 500 SER B 464 179.89 66.62
REMARK 500 ASN C 34 -7.17 -149.82
REMARK 500 ALA C 212 -88.35 -0.88
REMARK 500 LEU C 255 -154.33 -115.37
REMARK 500 LEU C 413 -89.66 -89.51
REMARK 500 LYS C 455 -134.75 56.73
REMARK 500 SER C 464 179.18 67.73
REMARK 500 ASN D 34 -9.60 -149.38
REMARK 500 ALA D 212 -118.44 47.83
REMARK 500 LEU D 255 -151.21 -114.44
REMARK 500 LEU D 413 -88.96 -90.61
REMARK 500 LYS D 455 -131.69 57.38
REMARK 500 SER D 464 175.40 69.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 482
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS SAID THEY BELIEVE THE MISMATCH OBSERVED REPRESENTS A
REMARK 999 NATURALLY OCCURRING VARIANT OF THE E. COLI SSADH GENE. AUTHORS
REMARK 999 SEQUENCED MANY SSADH CDNA SEQUENCES FROM GENOMIC DNA ISOLATED FROM
REMARK 999 THE E. COLI VARIANT MC1061 AND FOUND THIS MISMATCH OCCURRED IN ALL
REMARK 999 SEQUENCES. THE MISMATCH ARISES FROM A SINGLE NUCLEOTIDE CHANGE FROM
REMARK 999 GTG TO ATG RESULTING IN A CHANGE IN THE PROTEIN SEQUENCE VAL TO MET.
DBREF 3JZ4 A 1 481 UNP P25526 GABD_ECOLI 2 482
DBREF 3JZ4 B 1 481 UNP P25526 GABD_ECOLI 2 482
DBREF 3JZ4 C 1 481 UNP P25526 GABD_ECOLI 2 482
DBREF 3JZ4 D 1 481 UNP P25526 GABD_ECOLI 2 482
SEQADV 3JZ4 MET A 312 UNP P25526 VAL 313 SEE REMARK 999
SEQADV 3JZ4 MET B 312 UNP P25526 VAL 313 SEE REMARK 999
SEQADV 3JZ4 MET C 312 UNP P25526 VAL 313 SEE REMARK 999
SEQADV 3JZ4 MET D 312 UNP P25526 VAL 313 SEE REMARK 999
SEQRES 1 A 481 LYS LEU ASN ASP SER ASN LEU PHE ARG GLN GLN ALA LEU
SEQRES 2 A 481 ILE ASN GLY GLU TRP LEU ASP ALA ASN ASN GLY GLU ALA
SEQRES 3 A 481 ILE ASP VAL THR ASN PRO ALA ASN GLY ASP LYS LEU GLY
SEQRES 4 A 481 SER VAL PRO LYS MET GLY ALA ASP GLU THR ARG ALA ALA
SEQRES 5 A 481 ILE ASP ALA ALA ASN ARG ALA LEU PRO ALA TRP ARG ALA
SEQRES 6 A 481 LEU THR ALA LYS GLU ARG ALA THR ILE LEU ARG ASN TRP
SEQRES 7 A 481 PHE ASN LEU MET MET GLU HIS GLN ASP ASP LEU ALA ARG
SEQRES 8 A 481 LEU MET THR LEU GLU GLN GLY LYS PRO LEU ALA GLU ALA
SEQRES 9 A 481 LYS GLY GLU ILE SER TYR ALA ALA SER PHE ILE GLU TRP
SEQRES 10 A 481 PHE ALA GLU GLU GLY LYS ARG ILE TYR GLY ASP THR ILE
SEQRES 11 A 481 PRO GLY HIS GLN ALA ASP LYS ARG LEU ILE VAL ILE LYS
SEQRES 12 A 481 GLN PRO ILE GLY VAL THR ALA ALA ILE THR PRO TRP ASN
SEQRES 13 A 481 PHE PRO ALA ALA MET ILE THR ARG LYS ALA GLY PRO ALA
SEQRES 14 A 481 LEU ALA ALA GLY CYS THR MET VAL LEU LYS PRO ALA SER
SEQRES 15 A 481 GLN THR PRO PHE SER ALA LEU ALA LEU ALA GLU LEU ALA
SEQRES 16 A 481 ILE ARG ALA GLY VAL PRO ALA GLY VAL PHE ASN VAL VAL
SEQRES 17 A 481 THR GLY SER ALA GLY ALA VAL GLY ASN GLU LEU THR SER
SEQRES 18 A 481 ASN PRO LEU VAL ARG LYS LEU SER PHE THR GLY SER THR
SEQRES 19 A 481 GLU ILE GLY ARG GLN LEU MET GLU GLN CYS ALA LYS ASP
SEQRES 20 A 481 ILE LYS LYS VAL SER LEU GLU LEU GLY GLY ASN ALA PRO
SEQRES 21 A 481 PHE ILE VAL PHE ASP ASP ALA ASP LEU ASP LYS ALA VAL
SEQRES 22 A 481 GLU GLY ALA LEU ALA SER LYS PHE ARG ASN ALA GLY GLN
SEQRES 23 A 481 THR CYS VAL CYS ALA ASN ARG LEU TYR VAL GLN ASP GLY
SEQRES 24 A 481 VAL TYR ASP ARG PHE ALA GLU LYS LEU GLN GLN ALA MET
SEQRES 25 A 481 SER LYS LEU HIS ILE GLY ASP GLY LEU ASP ASN GLY VAL
SEQRES 26 A 481 THR ILE GLY PRO LEU ILE ASP GLU LYS ALA VAL ALA LYS
SEQRES 27 A 481 VAL GLU GLU HIS ILE ALA ASP ALA LEU GLU LYS GLY ALA
SEQRES 28 A 481 ARG VAL VAL CYS GLY GLY LYS ALA HIS GLU ARG GLY GLY
SEQRES 29 A 481 ASN PHE PHE GLN PRO THR ILE LEU VAL ASP VAL PRO ALA
SEQRES 30 A 481 ASN ALA LYS VAL SER LYS GLU GLU THR PHE GLY PRO LEU
SEQRES 31 A 481 ALA PRO LEU PHE ARG PHE LYS ASP GLU ALA ASP VAL ILE
SEQRES 32 A 481 ALA GLN ALA ASN ASP THR GLU PHE GLY LEU ALA ALA TYR
SEQRES 33 A 481 PHE TYR ALA ARG ASP LEU SER ARG VAL PHE ARG VAL GLY
SEQRES 34 A 481 GLU ALA LEU GLU TYR GLY ILE VAL GLY ILE ASN THR GLY
SEQRES 35 A 481 ILE ILE SER ASN GLU VAL ALA PRO PHE GLY GLY ILE LYS
SEQRES 36 A 481 ALA SER GLY LEU GLY ARG GLU GLY SER LYS TYR GLY ILE
SEQRES 37 A 481 GLU ASP TYR LEU GLU ILE LYS TYR MET CYS ILE GLY LEU
SEQRES 1 B 481 LYS LEU ASN ASP SER ASN LEU PHE ARG GLN GLN ALA LEU
SEQRES 2 B 481 ILE ASN GLY GLU TRP LEU ASP ALA ASN ASN GLY GLU ALA
SEQRES 3 B 481 ILE ASP VAL THR ASN PRO ALA ASN GLY ASP LYS LEU GLY
SEQRES 4 B 481 SER VAL PRO LYS MET GLY ALA ASP GLU THR ARG ALA ALA
SEQRES 5 B 481 ILE ASP ALA ALA ASN ARG ALA LEU PRO ALA TRP ARG ALA
SEQRES 6 B 481 LEU THR ALA LYS GLU ARG ALA THR ILE LEU ARG ASN TRP
SEQRES 7 B 481 PHE ASN LEU MET MET GLU HIS GLN ASP ASP LEU ALA ARG
SEQRES 8 B 481 LEU MET THR LEU GLU GLN GLY LYS PRO LEU ALA GLU ALA
SEQRES 9 B 481 LYS GLY GLU ILE SER TYR ALA ALA SER PHE ILE GLU TRP
SEQRES 10 B 481 PHE ALA GLU GLU GLY LYS ARG ILE TYR GLY ASP THR ILE
SEQRES 11 B 481 PRO GLY HIS GLN ALA ASP LYS ARG LEU ILE VAL ILE LYS
SEQRES 12 B 481 GLN PRO ILE GLY VAL THR ALA ALA ILE THR PRO TRP ASN
SEQRES 13 B 481 PHE PRO ALA ALA MET ILE THR ARG LYS ALA GLY PRO ALA
SEQRES 14 B 481 LEU ALA ALA GLY CYS THR MET VAL LEU LYS PRO ALA SER
SEQRES 15 B 481 GLN THR PRO PHE SER ALA LEU ALA LEU ALA GLU LEU ALA
SEQRES 16 B 481 ILE ARG ALA GLY VAL PRO ALA GLY VAL PHE ASN VAL VAL
SEQRES 17 B 481 THR GLY SER ALA GLY ALA VAL GLY ASN GLU LEU THR SER
SEQRES 18 B 481 ASN PRO LEU VAL ARG LYS LEU SER PHE THR GLY SER THR
SEQRES 19 B 481 GLU ILE GLY ARG GLN LEU MET GLU GLN CYS ALA LYS ASP
SEQRES 20 B 481 ILE LYS LYS VAL SER LEU GLU LEU GLY GLY ASN ALA PRO
SEQRES 21 B 481 PHE ILE VAL PHE ASP ASP ALA ASP LEU ASP LYS ALA VAL
SEQRES 22 B 481 GLU GLY ALA LEU ALA SER LYS PHE ARG ASN ALA GLY GLN
SEQRES 23 B 481 THR CYS VAL CYS ALA ASN ARG LEU TYR VAL GLN ASP GLY
SEQRES 24 B 481 VAL TYR ASP ARG PHE ALA GLU LYS LEU GLN GLN ALA MET
SEQRES 25 B 481 SER LYS LEU HIS ILE GLY ASP GLY LEU ASP ASN GLY VAL
SEQRES 26 B 481 THR ILE GLY PRO LEU ILE ASP GLU LYS ALA VAL ALA LYS
SEQRES 27 B 481 VAL GLU GLU HIS ILE ALA ASP ALA LEU GLU LYS GLY ALA
SEQRES 28 B 481 ARG VAL VAL CYS GLY GLY LYS ALA HIS GLU ARG GLY GLY
SEQRES 29 B 481 ASN PHE PHE GLN PRO THR ILE LEU VAL ASP VAL PRO ALA
SEQRES 30 B 481 ASN ALA LYS VAL SER LYS GLU GLU THR PHE GLY PRO LEU
SEQRES 31 B 481 ALA PRO LEU PHE ARG PHE LYS ASP GLU ALA ASP VAL ILE
SEQRES 32 B 481 ALA GLN ALA ASN ASP THR GLU PHE GLY LEU ALA ALA TYR
SEQRES 33 B 481 PHE TYR ALA ARG ASP LEU SER ARG VAL PHE ARG VAL GLY
SEQRES 34 B 481 GLU ALA LEU GLU TYR GLY ILE VAL GLY ILE ASN THR GLY
SEQRES 35 B 481 ILE ILE SER ASN GLU VAL ALA PRO PHE GLY GLY ILE LYS
SEQRES 36 B 481 ALA SER GLY LEU GLY ARG GLU GLY SER LYS TYR GLY ILE
SEQRES 37 B 481 GLU ASP TYR LEU GLU ILE LYS TYR MET CYS ILE GLY LEU
SEQRES 1 C 481 LYS LEU ASN ASP SER ASN LEU PHE ARG GLN GLN ALA LEU
SEQRES 2 C 481 ILE ASN GLY GLU TRP LEU ASP ALA ASN ASN GLY GLU ALA
SEQRES 3 C 481 ILE ASP VAL THR ASN PRO ALA ASN GLY ASP LYS LEU GLY
SEQRES 4 C 481 SER VAL PRO LYS MET GLY ALA ASP GLU THR ARG ALA ALA
SEQRES 5 C 481 ILE ASP ALA ALA ASN ARG ALA LEU PRO ALA TRP ARG ALA
SEQRES 6 C 481 LEU THR ALA LYS GLU ARG ALA THR ILE LEU ARG ASN TRP
SEQRES 7 C 481 PHE ASN LEU MET MET GLU HIS GLN ASP ASP LEU ALA ARG
SEQRES 8 C 481 LEU MET THR LEU GLU GLN GLY LYS PRO LEU ALA GLU ALA
SEQRES 9 C 481 LYS GLY GLU ILE SER TYR ALA ALA SER PHE ILE GLU TRP
SEQRES 10 C 481 PHE ALA GLU GLU GLY LYS ARG ILE TYR GLY ASP THR ILE
SEQRES 11 C 481 PRO GLY HIS GLN ALA ASP LYS ARG LEU ILE VAL ILE LYS
SEQRES 12 C 481 GLN PRO ILE GLY VAL THR ALA ALA ILE THR PRO TRP ASN
SEQRES 13 C 481 PHE PRO ALA ALA MET ILE THR ARG LYS ALA GLY PRO ALA
SEQRES 14 C 481 LEU ALA ALA GLY CYS THR MET VAL LEU LYS PRO ALA SER
SEQRES 15 C 481 GLN THR PRO PHE SER ALA LEU ALA LEU ALA GLU LEU ALA
SEQRES 16 C 481 ILE ARG ALA GLY VAL PRO ALA GLY VAL PHE ASN VAL VAL
SEQRES 17 C 481 THR GLY SER ALA GLY ALA VAL GLY ASN GLU LEU THR SER
SEQRES 18 C 481 ASN PRO LEU VAL ARG LYS LEU SER PHE THR GLY SER THR
SEQRES 19 C 481 GLU ILE GLY ARG GLN LEU MET GLU GLN CYS ALA LYS ASP
SEQRES 20 C 481 ILE LYS LYS VAL SER LEU GLU LEU GLY GLY ASN ALA PRO
SEQRES 21 C 481 PHE ILE VAL PHE ASP ASP ALA ASP LEU ASP LYS ALA VAL
SEQRES 22 C 481 GLU GLY ALA LEU ALA SER LYS PHE ARG ASN ALA GLY GLN
SEQRES 23 C 481 THR CYS VAL CYS ALA ASN ARG LEU TYR VAL GLN ASP GLY
SEQRES 24 C 481 VAL TYR ASP ARG PHE ALA GLU LYS LEU GLN GLN ALA MET
SEQRES 25 C 481 SER LYS LEU HIS ILE GLY ASP GLY LEU ASP ASN GLY VAL
SEQRES 26 C 481 THR ILE GLY PRO LEU ILE ASP GLU LYS ALA VAL ALA LYS
SEQRES 27 C 481 VAL GLU GLU HIS ILE ALA ASP ALA LEU GLU LYS GLY ALA
SEQRES 28 C 481 ARG VAL VAL CYS GLY GLY LYS ALA HIS GLU ARG GLY GLY
SEQRES 29 C 481 ASN PHE PHE GLN PRO THR ILE LEU VAL ASP VAL PRO ALA
SEQRES 30 C 481 ASN ALA LYS VAL SER LYS GLU GLU THR PHE GLY PRO LEU
SEQRES 31 C 481 ALA PRO LEU PHE ARG PHE LYS ASP GLU ALA ASP VAL ILE
SEQRES 32 C 481 ALA GLN ALA ASN ASP THR GLU PHE GLY LEU ALA ALA TYR
SEQRES 33 C 481 PHE TYR ALA ARG ASP LEU SER ARG VAL PHE ARG VAL GLY
SEQRES 34 C 481 GLU ALA LEU GLU TYR GLY ILE VAL GLY ILE ASN THR GLY
SEQRES 35 C 481 ILE ILE SER ASN GLU VAL ALA PRO PHE GLY GLY ILE LYS
SEQRES 36 C 481 ALA SER GLY LEU GLY ARG GLU GLY SER LYS TYR GLY ILE
SEQRES 37 C 481 GLU ASP TYR LEU GLU ILE LYS TYR MET CYS ILE GLY LEU
SEQRES 1 D 481 LYS LEU ASN ASP SER ASN LEU PHE ARG GLN GLN ALA LEU
SEQRES 2 D 481 ILE ASN GLY GLU TRP LEU ASP ALA ASN ASN GLY GLU ALA
SEQRES 3 D 481 ILE ASP VAL THR ASN PRO ALA ASN GLY ASP LYS LEU GLY
SEQRES 4 D 481 SER VAL PRO LYS MET GLY ALA ASP GLU THR ARG ALA ALA
SEQRES 5 D 481 ILE ASP ALA ALA ASN ARG ALA LEU PRO ALA TRP ARG ALA
SEQRES 6 D 481 LEU THR ALA LYS GLU ARG ALA THR ILE LEU ARG ASN TRP
SEQRES 7 D 481 PHE ASN LEU MET MET GLU HIS GLN ASP ASP LEU ALA ARG
SEQRES 8 D 481 LEU MET THR LEU GLU GLN GLY LYS PRO LEU ALA GLU ALA
SEQRES 9 D 481 LYS GLY GLU ILE SER TYR ALA ALA SER PHE ILE GLU TRP
SEQRES 10 D 481 PHE ALA GLU GLU GLY LYS ARG ILE TYR GLY ASP THR ILE
SEQRES 11 D 481 PRO GLY HIS GLN ALA ASP LYS ARG LEU ILE VAL ILE LYS
SEQRES 12 D 481 GLN PRO ILE GLY VAL THR ALA ALA ILE THR PRO TRP ASN
SEQRES 13 D 481 PHE PRO ALA ALA MET ILE THR ARG LYS ALA GLY PRO ALA
SEQRES 14 D 481 LEU ALA ALA GLY CYS THR MET VAL LEU LYS PRO ALA SER
SEQRES 15 D 481 GLN THR PRO PHE SER ALA LEU ALA LEU ALA GLU LEU ALA
SEQRES 16 D 481 ILE ARG ALA GLY VAL PRO ALA GLY VAL PHE ASN VAL VAL
SEQRES 17 D 481 THR GLY SER ALA GLY ALA VAL GLY ASN GLU LEU THR SER
SEQRES 18 D 481 ASN PRO LEU VAL ARG LYS LEU SER PHE THR GLY SER THR
SEQRES 19 D 481 GLU ILE GLY ARG GLN LEU MET GLU GLN CYS ALA LYS ASP
SEQRES 20 D 481 ILE LYS LYS VAL SER LEU GLU LEU GLY GLY ASN ALA PRO
SEQRES 21 D 481 PHE ILE VAL PHE ASP ASP ALA ASP LEU ASP LYS ALA VAL
SEQRES 22 D 481 GLU GLY ALA LEU ALA SER LYS PHE ARG ASN ALA GLY GLN
SEQRES 23 D 481 THR CYS VAL CYS ALA ASN ARG LEU TYR VAL GLN ASP GLY
SEQRES 24 D 481 VAL TYR ASP ARG PHE ALA GLU LYS LEU GLN GLN ALA MET
SEQRES 25 D 481 SER LYS LEU HIS ILE GLY ASP GLY LEU ASP ASN GLY VAL
SEQRES 26 D 481 THR ILE GLY PRO LEU ILE ASP GLU LYS ALA VAL ALA LYS
SEQRES 27 D 481 VAL GLU GLU HIS ILE ALA ASP ALA LEU GLU LYS GLY ALA
SEQRES 28 D 481 ARG VAL VAL CYS GLY GLY LYS ALA HIS GLU ARG GLY GLY
SEQRES 29 D 481 ASN PHE PHE GLN PRO THR ILE LEU VAL ASP VAL PRO ALA
SEQRES 30 D 481 ASN ALA LYS VAL SER LYS GLU GLU THR PHE GLY PRO LEU
SEQRES 31 D 481 ALA PRO LEU PHE ARG PHE LYS ASP GLU ALA ASP VAL ILE
SEQRES 32 D 481 ALA GLN ALA ASN ASP THR GLU PHE GLY LEU ALA ALA TYR
SEQRES 33 D 481 PHE TYR ALA ARG ASP LEU SER ARG VAL PHE ARG VAL GLY
SEQRES 34 D 481 GLU ALA LEU GLU TYR GLY ILE VAL GLY ILE ASN THR GLY
SEQRES 35 D 481 ILE ILE SER ASN GLU VAL ALA PRO PHE GLY GLY ILE LYS
SEQRES 36 D 481 ALA SER GLY LEU GLY ARG GLU GLY SER LYS TYR GLY ILE
SEQRES 37 D 481 GLU ASP TYR LEU GLU ILE LYS TYR MET CYS ILE GLY LEU
HET NAP A 482 48
HET NAP B 482 48
HET NAP C 482 48
HET NAP D 482 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 5 NAP 4(C21 H28 N7 O17 P3)
FORMUL 9 HOH *331(H2 O)
HELIX 1 1 ASP A 4 PHE A 8 5 5
HELIX 2 2 GLY A 45 LEU A 66 1 22
HELIX 3 3 THR A 67 HIS A 85 1 19
HELIX 4 4 HIS A 85 GLY A 98 1 14
HELIX 5 5 PRO A 100 GLY A 122 1 23
HELIX 6 6 LYS A 123 ILE A 125 5 3
HELIX 7 7 ALA A 159 GLY A 173 1 15
HELIX 8 8 PRO A 185 GLY A 199 1 15
HELIX 9 9 ALA A 212 ASN A 222 1 11
HELIX 10 10 SER A 233 ALA A 245 1 13
HELIX 11 11 ASP A 268 ARG A 282 1 15
HELIX 12 12 ASN A 283 GLN A 286 5 4
HELIX 13 13 VAL A 300 SER A 313 1 14
HELIX 14 14 ASP A 332 LYS A 349 1 18
HELIX 15 15 ALA A 379 LYS A 383 5 5
HELIX 16 16 ASP A 398 ASP A 408 1 11
HELIX 17 17 ASP A 421 LEU A 432 1 12
HELIX 18 18 ILE A 454 ALA A 456 5 3
HELIX 19 19 GLY A 463 ASP A 470 1 8
HELIX 20 20 ASP B 4 PHE B 8 5 5
HELIX 21 21 GLY B 45 LEU B 66 1 22
HELIX 22 22 THR B 67 HIS B 85 1 19
HELIX 23 23 HIS B 85 GLY B 98 1 14
HELIX 24 24 PRO B 100 GLY B 122 1 23
HELIX 25 25 LYS B 123 ILE B 125 5 3
HELIX 26 26 ALA B 159 GLY B 173 1 15
HELIX 27 27 PRO B 185 GLY B 199 1 15
HELIX 28 28 SER B 211 ASN B 222 1 12
HELIX 29 29 SER B 233 ALA B 245 1 13
HELIX 30 30 LYS B 246 ILE B 248 5 3
HELIX 31 31 ASP B 268 ARG B 282 1 15
HELIX 32 32 ASN B 283 GLN B 286 5 4
HELIX 33 33 VAL B 300 SER B 313 1 14
HELIX 34 34 ASP B 332 LYS B 349 1 18
HELIX 35 35 ALA B 379 GLU B 384 1 6
HELIX 36 36 ASP B 398 ASN B 407 1 10
HELIX 37 37 ASP B 421 LEU B 432 1 12
HELIX 38 38 ILE B 454 ALA B 456 5 3
HELIX 39 39 LYS B 465 ASP B 470 5 6
HELIX 40 40 ASP C 4 PHE C 8 5 5
HELIX 41 41 GLY C 45 ALA C 65 1 21
HELIX 42 42 THR C 67 HIS C 85 1 19
HELIX 43 43 HIS C 85 GLY C 98 1 14
HELIX 44 44 PRO C 100 GLY C 122 1 23
HELIX 45 45 LYS C 123 ILE C 125 5 3
HELIX 46 46 ALA C 159 GLY C 173 1 15
HELIX 47 47 THR C 184 GLY C 199 1 16
HELIX 48 48 SER C 211 ASN C 222 1 12
HELIX 49 49 SER C 233 ALA C 245 1 13
HELIX 50 50 ASP C 268 ARG C 282 1 15
HELIX 51 51 ASN C 283 GLN C 286 5 4
HELIX 52 52 VAL C 300 SER C 313 1 14
HELIX 53 53 ASP C 332 LYS C 349 1 18
HELIX 54 54 ALA C 379 GLU C 384 1 6
HELIX 55 55 ASP C 398 ASP C 408 1 11
HELIX 56 56 ASP C 421 LEU C 432 1 12
HELIX 57 57 ILE C 454 ALA C 456 5 3
HELIX 58 58 GLY C 463 ASP C 470 1 8
HELIX 59 59 ASP D 4 PHE D 8 5 5
HELIX 60 60 GLY D 45 ALA D 65 1 21
HELIX 61 61 THR D 67 HIS D 85 1 19
HELIX 62 62 HIS D 85 GLY D 98 1 14
HELIX 63 63 PRO D 100 GLY D 122 1 23
HELIX 64 64 LYS D 123 ILE D 125 5 3
HELIX 65 65 ALA D 159 GLY D 173 1 15
HELIX 66 66 PRO D 185 GLY D 199 1 15
HELIX 67 67 ALA D 212 ASN D 222 1 11
HELIX 68 68 SER D 233 ALA D 245 1 13
HELIX 69 69 ASP D 268 ARG D 282 1 15
HELIX 70 70 ASN D 283 GLN D 286 5 4
HELIX 71 71 VAL D 300 MET D 312 1 13
HELIX 72 72 SER D 313 LEU D 315 5 3
HELIX 73 73 ASP D 332 LYS D 349 1 18
HELIX 74 74 ALA D 379 LYS D 383 5 5
HELIX 75 75 ASP D 398 ASP D 408 1 11
HELIX 76 76 ASP D 421 LEU D 432 1 12
HELIX 77 77 ILE D 454 ALA D 456 5 3
HELIX 78 78 GLY D 463 ILE D 468 1 6
SHEET 1 A 2 ALA A 12 ILE A 14 0
SHEET 2 A 2 GLU A 17 LEU A 19 -1 O GLU A 17 N ILE A 14
SHEET 1 B 2 ALA A 26 THR A 30 0
SHEET 2 B 2 LYS A 37 PRO A 42 -1 O GLY A 39 N VAL A 29
SHEET 1 C20 ARG B 352 CYS B 355 0
SHEET 2 C20 THR B 370 VAL B 373 -1 O VAL B 373 N ARG B 352
SHEET 3 C20 LEU B 390 PHE B 396 1 O ALA B 391 N LEU B 372
SHEET 4 C20 ALA B 291 GLN B 297 1 N LEU B 294 O PHE B 394
SHEET 5 C20 ALA B 259 VAL B 263 1 N VAL B 263 O TYR B 295
SHEET 6 C20 ALA B 414 TYR B 418 1 O TYR B 416 N ILE B 262
SHEET 7 C20 ILE B 436 ILE B 439 1 O GLY B 438 N ALA B 415
SHEET 8 C20 LEU A 472 GLY A 480 1 N TYR A 476 O VAL B 437
SHEET 9 C20 LYS A 137 PRO A 145 -1 N ILE A 140 O MET A 477
SHEET 10 C20 GLY A 127 ILE A 130 -1 N ASP A 128 O VAL A 141
SHEET 11 C20 GLY C 127 ILE C 130 -1 O GLY C 127 N THR A 129
SHEET 12 C20 LYS C 137 PRO C 145 -1 O VAL C 141 N ASP C 128
SHEET 13 C20 LEU C 472 GLY C 480 -1 O MET C 477 N ILE C 140
SHEET 14 C20 ILE D 436 ILE D 439 1 O ILE D 439 N GLY C 480
SHEET 15 C20 ALA D 414 TYR D 418 1 N ALA D 415 O GLY D 438
SHEET 16 C20 ALA D 259 VAL D 263 1 N ILE D 262 O TYR D 416
SHEET 17 C20 ALA D 291 GLN D 297 1 O TYR D 295 N VAL D 263
SHEET 18 C20 LEU D 390 PHE D 396 1 O PHE D 394 N LEU D 294
SHEET 19 C20 THR D 370 VAL D 373 1 N THR D 370 O ALA D 391
SHEET 20 C20 ARG D 352 CYS D 355 -1 N VAL D 354 O ILE D 371
SHEET 1 D 6 PHE A 205 VAL A 207 0
SHEET 2 D 6 THR A 175 LYS A 179 1 N LEU A 178 O ASN A 206
SHEET 3 D 6 VAL A 148 ILE A 152 1 N ALA A 151 O LYS A 179
SHEET 4 D 6 VAL A 225 THR A 231 1 O LYS A 227 N ALA A 150
SHEET 5 D 6 LYS A 250 GLU A 254 1 O SER A 252 N LEU A 228
SHEET 6 D 6 GLY A 458 LEU A 459 -1 O LEU A 459 N LEU A 253
SHEET 1 E20 ARG A 352 CYS A 355 0
SHEET 2 E20 THR A 370 VAL A 373 -1 O ILE A 371 N VAL A 354
SHEET 3 E20 LEU A 390 PHE A 396 1 O ALA A 391 N THR A 370
SHEET 4 E20 ALA A 291 GLN A 297 1 N LEU A 294 O PHE A 394
SHEET 5 E20 ALA A 259 VAL A 263 1 N VAL A 263 O TYR A 295
SHEET 6 E20 ALA A 414 TYR A 418 1 O TYR A 416 N ILE A 262
SHEET 7 E20 ILE A 436 ILE A 439 1 O GLY A 438 N ALA A 415
SHEET 8 E20 LEU B 472 GLY B 480 1 O GLY B 480 N ILE A 439
SHEET 9 E20 LYS B 137 PRO B 145 -1 N ILE B 140 O MET B 477
SHEET 10 E20 GLY B 127 ILE B 130 -1 N ASP B 128 O VAL B 141
SHEET 11 E20 GLY D 127 ILE D 130 -1 O THR D 129 N GLY B 127
SHEET 12 E20 LYS D 137 PRO D 145 -1 O VAL D 141 N ASP D 128
SHEET 13 E20 LEU D 472 GLY D 480 -1 O MET D 477 N ILE D 140
SHEET 14 E20 ILE C 436 ILE C 439 1 N ILE C 439 O GLY D 480
SHEET 15 E20 ALA C 414 TYR C 418 1 N ALA C 415 O GLY C 438
SHEET 16 E20 ALA C 259 VAL C 263 1 N ILE C 262 O TYR C 418
SHEET 17 E20 ALA C 291 GLN C 297 1 O TYR C 295 N VAL C 263
SHEET 18 E20 LEU C 390 PHE C 396 1 O PHE C 394 N LEU C 294
SHEET 19 E20 THR C 370 VAL C 373 1 N THR C 370 O ALA C 391
SHEET 20 E20 ARG C 352 CYS C 355 -1 N VAL C 354 O ILE C 371
SHEET 1 F 2 ALA B 12 ILE B 14 0
SHEET 2 F 2 GLU B 17 LEU B 19 -1 O GLU B 17 N ILE B 14
SHEET 1 G 2 ALA B 26 THR B 30 0
SHEET 2 G 2 LYS B 37 PRO B 42 -1 O VAL B 41 N ILE B 27
SHEET 1 H 6 PHE B 205 VAL B 207 0
SHEET 2 H 6 THR B 175 LYS B 179 1 N LEU B 178 O ASN B 206
SHEET 3 H 6 VAL B 148 ILE B 152 1 N ALA B 151 O LYS B 179
SHEET 4 H 6 VAL B 225 THR B 231 1 O LYS B 227 N ALA B 150
SHEET 5 H 6 LYS B 250 GLU B 254 1 O SER B 252 N LEU B 228
SHEET 6 H 6 GLY B 458 LEU B 459 -1 O LEU B 459 N LEU B 253
SHEET 1 I 2 ALA C 12 ILE C 14 0
SHEET 2 I 2 GLU C 17 LEU C 19 -1 O GLU C 17 N ILE C 14
SHEET 1 J 2 ALA C 26 THR C 30 0
SHEET 2 J 2 LYS C 37 PRO C 42 -1 O VAL C 41 N ILE C 27
SHEET 1 K 6 PHE C 205 VAL C 207 0
SHEET 2 K 6 THR C 175 LYS C 179 1 N LEU C 178 O ASN C 206
SHEET 3 K 6 VAL C 148 ILE C 152 1 N ALA C 151 O LYS C 179
SHEET 4 K 6 VAL C 225 THR C 231 1 O LYS C 227 N ALA C 150
SHEET 5 K 6 LYS C 250 GLU C 254 1 O SER C 252 N LEU C 228
SHEET 6 K 6 GLY C 458 LEU C 459 -1 O LEU C 459 N LEU C 253
SHEET 1 L 2 ALA D 12 ILE D 14 0
SHEET 2 L 2 GLU D 17 LEU D 19 -1 O GLU D 17 N ILE D 14
SHEET 1 M 2 ALA D 26 THR D 30 0
SHEET 2 M 2 LYS D 37 PRO D 42 -1 O VAL D 41 N ILE D 27
SHEET 1 N 6 PHE D 205 VAL D 207 0
SHEET 2 N 6 THR D 175 LYS D 179 1 N LEU D 178 O ASN D 206
SHEET 3 N 6 VAL D 148 ILE D 152 1 N ALA D 151 O LYS D 179
SHEET 4 N 6 VAL D 225 THR D 231 1 O LYS D 227 N ALA D 150
SHEET 5 N 6 LYS D 250 GLU D 254 1 O SER D 252 N LEU D 228
SHEET 6 N 6 GLY D 458 LEU D 459 -1 O LEU D 459 N LEU D 253
SITE 1 AC1 27 THR A 153 PRO A 154 TRP A 155 ASN A 156
SITE 2 AC1 27 LYS A 179 ALA A 181 SER A 182 GLY A 210
SITE 3 AC1 27 ALA A 212 GLY A 216 PHE A 230 THR A 231
SITE 4 AC1 27 GLY A 232 SER A 233 ILE A 236 GLU A 254
SITE 5 AC1 27 LEU A 255 CYS A 288 LYS A 338 GLU A 385
SITE 6 AC1 27 PHE A 387 HOH A 496 HOH A 520 HOH A 543
SITE 7 AC1 27 HOH A 580 HOH A 611 HOH A 616
SITE 1 AC2 24 ILE B 152 THR B 153 PRO B 154 TRP B 155
SITE 2 AC2 24 ASN B 156 LYS B 179 ALA B 181 SER B 182
SITE 3 AC2 24 ALA B 212 GLY B 216 PHE B 230 GLY B 232
SITE 4 AC2 24 SER B 233 ILE B 236 GLU B 254 LEU B 255
SITE 5 AC2 24 CYS B 288 LYS B 338 GLU B 385 PHE B 387
SITE 6 AC2 24 HOH B 499 HOH B 523 HOH B 536 HOH B 609
SITE 1 AC3 21 THR C 153 PRO C 154 TRP C 155 ASN C 156
SITE 2 AC3 21 LYS C 179 ALA C 181 SER C 182 GLY C 210
SITE 3 AC3 21 ALA C 212 GLY C 216 PHE C 230 THR C 231
SITE 4 AC3 21 GLY C 232 SER C 233 ILE C 236 LEU C 255
SITE 5 AC3 21 CYS C 288 LYS C 338 GLU C 385 PHE C 387
SITE 6 AC3 21 HOH C 487
SITE 1 AC4 23 ILE D 152 PRO D 154 TRP D 155 ASN D 156
SITE 2 AC4 23 LYS D 179 ALA D 181 SER D 182 GLY D 210
SITE 3 AC4 23 SER D 211 ALA D 212 GLY D 213 GLY D 216
SITE 4 AC4 23 PHE D 230 THR D 231 GLY D 232 SER D 233
SITE 5 AC4 23 ILE D 236 GLU D 254 LEU D 255 CYS D 288
SITE 6 AC4 23 LYS D 338 GLU D 385 PHE D 387
CRYST1 151.885 151.885 165.772 90.00 90.00 90.00 P 4 21 2 32
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 0.006584 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006584 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006032 0.00000
(ATOM LINES ARE NOT SHOWN.)
END