HEADER OXIDOREDUCTASE 28-JUN-07 2QG4
TITLE CRYSTAL STRUCTURE OF HUMAN UDP-GLUCOSE DEHYDROGENASE PRODUCT COMPLEX
TITLE 2 WITH UDP-GLUCURONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-GLUCOSE 6-DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: UDP-GLC DEHYDROGENASE, UDP-GLCDH, UDPGDH;
COMPND 5 EC: 1.1.1.22;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: UGDH;
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: PBEN1-SGC
KEYWDS UDP-GLUCOSE 6-DEHYDROGENASE, HEXAMER, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM, SGC, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.KAVANAGH,K.GUO,G.BUNKOCZI,P.SAVITSKY,E.PILKA,C.BHATIA,F.NIESEN,
AUTHOR 2 C.SMEE,G.BERRIDGE,F.VON DELFT,J.WEIGELT,C.H.ARROWSMITH,M.SUNDSTROM,
AUTHOR 3 A.EDWARDS,U.OPPERMANN,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 7 30-AUG-23 2QG4 1 REMARK SEQADV
REVDAT 6 18-OCT-17 2QG4 1 REMARK
REVDAT 5 31-AUG-11 2QG4 1 JRNL
REVDAT 4 13-JUL-11 2QG4 1 VERSN
REVDAT 3 10-NOV-09 2QG4 1 AUTHOR JRNL
REVDAT 2 24-FEB-09 2QG4 1 VERSN
REVDAT 1 10-JUL-07 2QG4 0
JRNL AUTH S.EGGER,A.CHAIKUAD,K.L.KAVANAGH,U.OPPERMANN,B.NIDETZKY
JRNL TITL STRUCTURE AND MECHANISM OF HUMAN UDP-GLUCOSE
JRNL TITL 2 6-DEHYDROGENASE.
JRNL REF J.BIOL.CHEM. V. 286 23877 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21502315
JRNL DOI 10.1074/JBC.M111.234682
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 273217
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 14846
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 21279
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 28503
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 604
REMARK 3 SOLVENT ATOMS : 2999
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 17.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 0.23000
REMARK 3 B12 (A**2) : -0.08000
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): 0.177
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.234
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 29698 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 19837 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 40365 ; 1.238 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): 48321 ; 0.909 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3682 ; 5.576 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1277 ;34.586 ;24.315
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5025 ;12.491 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 187 ;16.870 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4672 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 32637 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5774 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5957 ; 0.191 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 20992 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 14551 ; 0.170 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 14798 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 2097 ; 0.143 ; 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): 114 ; 0.114 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 457 ; 0.235 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 321 ; 0.134 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): 1 ; 0.012 ; 0.200
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): 18856 ; 1.737 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7452 ; 0.505 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 29646 ; 2.559 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12299 ; 4.394 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10711 ; 5.926 ;11.000
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C E G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 466 5
REMARK 3 1 C 2 C 466 5
REMARK 3 1 E 2 E 466 5
REMARK 3 1 G 2 G 466 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2703 ; 0.13 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 2703 ; 0.13 ; 0.00
REMARK 3 MEDIUM POSITIONAL 1 E (A): 2703 ; 0.13 ; 0.00
REMARK 3 MEDIUM POSITIONAL 1 G (A): 2703 ; 0.13 ; 0.00
REMARK 3 LOOSE POSITIONAL 1 A (A): 3202 ; 0.22 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 3202 ; 0.20 ; 0.00
REMARK 3 LOOSE POSITIONAL 1 E (A): 3202 ; 0.18 ; 0.00
REMARK 3 LOOSE POSITIONAL 1 G (A): 3202 ; 0.20 ; 0.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2703 ; 0.54 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 2703 ; 0.49 ; 0.00
REMARK 3 MEDIUM THERMAL 1 E (A**2): 2703 ; 0.53 ; 0.00
REMARK 3 MEDIUM THERMAL 1 G (A**2): 2703 ; 0.51 ; 0.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 3202 ; 0.55 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 3202 ; 0.53 ; 0.00
REMARK 3 LOOSE THERMAL 1 E (A**2): 3202 ; 0.53 ; 0.00
REMARK 3 LOOSE THERMAL 1 G (A**2): 3202 ; 0.53 ; 0.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D F H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 2 B 466 5
REMARK 3 1 D 2 D 466 5
REMARK 3 1 F 2 F 466 5
REMARK 3 1 H 2 H 466 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 B (A): 2711 ; 0.07 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 D (A): 2711 ; 0.07 ; 0.00
REMARK 3 MEDIUM POSITIONAL 2 F (A): 2711 ; 0.07 ; 0.00
REMARK 3 MEDIUM POSITIONAL 2 H (A): 2711 ; 0.07 ; 0.00
REMARK 3 LOOSE POSITIONAL 2 B (A): 3284 ; 0.20 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 D (A): 3284 ; 0.27 ; 0.00
REMARK 3 LOOSE POSITIONAL 2 F (A): 3284 ; 0.22 ; 0.00
REMARK 3 LOOSE POSITIONAL 2 H (A): 3284 ; 0.22 ; 0.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 2711 ; 1.32 ; 2.00
REMARK 3 MEDIUM THERMAL 2 D (A**2): 2711 ; 1.57 ; 0.00
REMARK 3 MEDIUM THERMAL 2 F (A**2): 2711 ; 1.63 ; 0.00
REMARK 3 MEDIUM THERMAL 2 H (A**2): 2711 ; 1.37 ; 0.00
REMARK 3 LOOSE THERMAL 2 B (A**2): 3284 ; 1.85 ; 10.00
REMARK 3 LOOSE THERMAL 2 D (A**2): 3284 ; 1.91 ; 0.00
REMARK 3 LOOSE THERMAL 2 F (A**2): 3284 ; 1.93 ; 0.00
REMARK 3 LOOSE THERMAL 2 H (A**2): 3284 ; 1.80 ; 0.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
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 466
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7815 22.8347 51.8347
REMARK 3 T TENSOR
REMARK 3 T11: 0.0015 T22: -0.0183
REMARK 3 T33: -0.0685 T12: -0.0153
REMARK 3 T13: -0.0179 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.1430 L22: 0.5022
REMARK 3 L33: 0.1787 L12: 0.0463
REMARK 3 L13: 0.0394 L23: 0.2568
REMARK 3 S TENSOR
REMARK 3 S11: 0.0386 S12: -0.0652 S13: 0.0347
REMARK 3 S21: 0.0786 S22: -0.0421 S23: -0.0624
REMARK 3 S31: 0.0207 S32: -0.0207 S33: 0.0035
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 466
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5885 18.2483 14.4492
REMARK 3 T TENSOR
REMARK 3 T11: -0.0504 T22: -0.0219
REMARK 3 T33: -0.0481 T12: -0.0315
REMARK 3 T13: 0.0142 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 0.6606 L22: 0.4342
REMARK 3 L33: 0.2455 L12: -0.1331
REMARK 3 L13: -0.0509 L23: -0.0205
REMARK 3 S TENSOR
REMARK 3 S11: -0.0247 S12: 0.0938 S13: 0.0687
REMARK 3 S21: -0.0173 S22: -0.0051 S23: -0.0634
REMARK 3 S31: -0.0507 S32: 0.0277 S33: 0.0298
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 466
REMARK 3 ORIGIN FOR THE GROUP (A): 66.2036 48.4593 -51.9423
REMARK 3 T TENSOR
REMARK 3 T11: -0.0144 T22: 0.0224
REMARK 3 T33: -0.0159 T12: 0.0095
REMARK 3 T13: -0.0188 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.6863 L22: 0.4091
REMARK 3 L33: 0.1158 L12: -0.3002
REMARK 3 L13: 0.2523 L23: -0.0304
REMARK 3 S TENSOR
REMARK 3 S11: 0.0450 S12: 0.1852 S13: -0.0518
REMARK 3 S21: -0.1102 S22: -0.0278 S23: 0.0551
REMARK 3 S31: -0.0247 S32: 0.0136 S33: -0.0172
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 466
REMARK 3 ORIGIN FOR THE GROUP (A): 68.8711 43.6408 -14.5614
REMARK 3 T TENSOR
REMARK 3 T11: -0.0773 T22: -0.0303
REMARK 3 T33: -0.0140 T12: -0.0174
REMARK 3 T13: 0.0121 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 0.4343 L22: 0.6612
REMARK 3 L33: 0.2965 L12: 0.1438
REMARK 3 L13: -0.0478 L23: -0.0344
REMARK 3 S TENSOR
REMARK 3 S11: 0.0317 S12: -0.0808 S13: -0.0244
REMARK 3 S21: 0.0476 S22: -0.0296 S23: 0.0822
REMARK 3 S31: 0.0146 S32: -0.0618 S33: -0.0022
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 466
REMARK 3 ORIGIN FOR THE GROUP (A): 66.1870 48.5571-135.1550
REMARK 3 T TENSOR
REMARK 3 T11: -0.0374 T22: -0.0002
REMARK 3 T33: -0.0853 T12: -0.0046
REMARK 3 T13: -0.0196 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.4716 L22: 0.1749
REMARK 3 L33: 0.1954 L12: -0.1527
REMARK 3 L13: 0.2844 L23: -0.0591
REMARK 3 S TENSOR
REMARK 3 S11: -0.0100 S12: 0.1113 S13: -0.0370
REMARK 3 S21: -0.0463 S22: 0.0165 S23: 0.0679
REMARK 3 S31: -0.0161 S32: 0.0288 S33: -0.0065
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 466
REMARK 3 ORIGIN FOR THE GROUP (A): 68.8447 43.7379 -97.8525
REMARK 3 T TENSOR
REMARK 3 T11: -0.0513 T22: -0.0079
REMARK 3 T33: -0.0590 T12: -0.0300
REMARK 3 T13: 0.0201 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.3527 L22: 0.7183
REMARK 3 L33: 0.2453 L12: 0.0564
REMARK 3 L13: -0.0626 L23: -0.0221
REMARK 3 S TENSOR
REMARK 3 S11: 0.0213 S12: -0.0389 S13: -0.0252
REMARK 3 S21: 0.0712 S22: -0.0541 S23: 0.0783
REMARK 3 S31: -0.0031 S32: -0.0463 S33: 0.0328
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 1 G 466
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8510 22.8090 -31.4743
REMARK 3 T TENSOR
REMARK 3 T11: 0.0113 T22: -0.0232
REMARK 3 T33: -0.0306 T12: -0.0127
REMARK 3 T13: -0.0019 T23: -0.0218
REMARK 3 L TENSOR
REMARK 3 L11: 0.1761 L22: 0.8944
REMARK 3 L33: 0.1415 L12: -0.0377
REMARK 3 L13: 0.1102 L23: 0.2300
REMARK 3 S TENSOR
REMARK 3 S11: 0.0245 S12: -0.1021 S13: 0.0292
REMARK 3 S21: 0.2033 S22: 0.0025 S23: -0.0684
REMARK 3 S31: 0.0108 S32: -0.0273 S33: -0.0270
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 466
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6760 18.1554 -68.9122
REMARK 3 T TENSOR
REMARK 3 T11: -0.0525 T22: -0.0444
REMARK 3 T33: -0.0288 T12: -0.0278
REMARK 3 T13: 0.0270 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.7493 L22: 0.3598
REMARK 3 L33: 0.2758 L12: -0.0760
REMARK 3 L13: -0.0497 L23: -0.0571
REMARK 3 S TENSOR
REMARK 3 S11: -0.0335 S12: 0.0791 S13: 0.0508
REMARK 3 S21: -0.0351 S22: 0.0246 S23: -0.0573
REMARK 3 S31: -0.0421 S32: 0.0407 S33: 0.0088
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2QG4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043555.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 288088
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.13900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: PDB ENTRY 2Q3E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 10% ETHYLENE GLYCOL, 0.2
REMARK 280 M NABR, 0.1 M BIS-TRIS-PROPANE, PH 6.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 96.93400
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 55.96487
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 117.40767
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 96.93400
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 55.96487
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 117.40767
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 96.93400
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 55.96487
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 117.40767
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 111.92974
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 234.81533
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 111.92974
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 234.81533
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 111.92974
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 234.81533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 38120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 92690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -298.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 38090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 92250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -299.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 38110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 92070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -301.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 38100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 92850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -298.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 193.86800
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 96.93400
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 167.89461
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 193.86800
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 96.93400
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 167.89461
REMARK 350 BIOMT3 3 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 SER A 0
REMARK 465 PRO A 383
REMARK 465 GLY A 384
REMARK 465 VAL A 385
REMARK 465 SER A 386
REMARK 465 GLU A 387
REMARK 465 ASP A 388
REMARK 465 SER B 0
REMARK 465 PRO B 383
REMARK 465 GLY B 384
REMARK 465 VAL B 385
REMARK 465 SER B 386
REMARK 465 GLU B 387
REMARK 465 SER C 0
REMARK 465 PRO C 383
REMARK 465 GLY C 384
REMARK 465 VAL C 385
REMARK 465 SER C 386
REMARK 465 GLU C 387
REMARK 465 ASP C 388
REMARK 465 ASP C 389
REMARK 465 SER D 0
REMARK 465 PRO D 383
REMARK 465 GLY D 384
REMARK 465 VAL D 385
REMARK 465 SER D 386
REMARK 465 GLU D 387
REMARK 465 SER E 0
REMARK 465 PRO E 383
REMARK 465 GLY E 384
REMARK 465 VAL E 385
REMARK 465 SER E 386
REMARK 465 GLU E 387
REMARK 465 ASP E 388
REMARK 465 ASP E 389
REMARK 465 SER F 0
REMARK 465 PRO F 383
REMARK 465 GLY F 384
REMARK 465 VAL F 385
REMARK 465 SER F 386
REMARK 465 GLU F 387
REMARK 465 SER G 0
REMARK 465 PRO G 383
REMARK 465 GLY G 384
REMARK 465 VAL G 385
REMARK 465 SER G 386
REMARK 465 GLU G 387
REMARK 465 ASP G 388
REMARK 465 SER H 0
REMARK 465 PRO H 383
REMARK 465 GLY H 384
REMARK 465 VAL H 385
REMARK 465 SER H 386
REMARK 465 GLU H 387
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 MET A 1 CG SD CE
REMARK 470 LYS A 80 CE NZ
REMARK 470 LYS A 170 CG CD CE NZ
REMARK 470 GLU A 184 CG CD OE1 OE2
REMARK 470 GLN A 193 CD OE1 NE2
REMARK 470 LYS A 267 CD CE NZ
REMARK 470 LYS A 370 CD CE NZ
REMARK 470 HIS A 382 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 389 CG OD1 OD2
REMARK 470 GLN A 390 CG CD OE1 NE2
REMARK 470 LYS A 399 CG CD CE NZ
REMARK 470 GLN A 458 CG CD OE1 NE2
REMARK 470 LYS A 465 CD CE NZ
REMARK 470 VAL A 466 CG1 CG2
REMARK 470 MET B 1 CG SD CE
REMARK 470 LYS B 5 CE NZ
REMARK 470 GLU B 39 CD OE1 OE2
REMARK 470 LYS B 80 CG CD CE NZ
REMARK 470 GLN B 118 CD OE1 NE2
REMARK 470 ARG B 142 NE CZ NH1 NH2
REMARK 470 LYS B 170 CD CE NZ
REMARK 470 GLU B 184 CG CD OE1 OE2
REMARK 470 HIS B 382 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 421 CD CE NZ
REMARK 470 LYS B 430 CD CE NZ
REMARK 470 MET C 1 CG SD CE
REMARK 470 LYS C 80 CE NZ
REMARK 470 LYS C 170 CG CD CE NZ
REMARK 470 GLU C 184 CG CD OE1 OE2
REMARK 470 ARG C 190 CD NE CZ NH1 NH2
REMARK 470 GLN C 193 CD OE1 NE2
REMARK 470 LYS C 267 CD CE NZ
REMARK 470 ARG C 312 NE CZ NH1 NH2
REMARK 470 LYS C 370 CD CE NZ
REMARK 470 ARG C 373 CZ NH1 NH2
REMARK 470 GLU C 374 CG CD OE1 OE2
REMARK 470 HIS C 382 CG ND1 CD2 CE1 NE2
REMARK 470 GLN C 390 CG CD OE1 NE2
REMARK 470 ARG C 393 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 399 CG CD CE NZ
REMARK 470 LYS C 421 CE NZ
REMARK 470 LYS C 431 CE NZ
REMARK 470 GLN C 458 CG CD OE1 NE2
REMARK 470 LYS C 465 CD CE NZ
REMARK 470 VAL C 466 CG1 CG2
REMARK 470 MET D 1 CG SD CE
REMARK 470 LYS D 80 NZ
REMARK 470 GLN D 118 CD OE1 NE2
REMARK 470 ARG D 142 NE CZ NH1 NH2
REMARK 470 LYS D 170 CG CD CE NZ
REMARK 470 GLU D 184 CG CD OE1 OE2
REMARK 470 HIS D 382 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 399 CG CD CE NZ
REMARK 470 LYS D 421 CD CE NZ
REMARK 470 LYS D 430 CD CE NZ
REMARK 470 MET E 1 CG SD CE
REMARK 470 GLU E 59 CD OE1 OE2
REMARK 470 LYS E 80 CE NZ
REMARK 470 LYS E 170 CG CD CE NZ
REMARK 470 GLU E 184 CG CD OE1 OE2
REMARK 470 GLN E 193 CG CD OE1 NE2
REMARK 470 LYS E 267 CD CE NZ
REMARK 470 ARG E 373 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 374 CG CD OE1 OE2
REMARK 470 HIS E 382 CG ND1 CD2 CE1 NE2
REMARK 470 ARG E 393 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 399 CG CD CE NZ
REMARK 470 GLN E 458 CG CD OE1 NE2
REMARK 470 LYS E 465 CD CE NZ
REMARK 470 VAL E 466 CG1 CG2
REMARK 470 MET F 1 CG SD CE
REMARK 470 LYS F 5 CE NZ
REMARK 470 GLU F 39 CG CD OE1 OE2
REMARK 470 GLN F 118 CD OE1 NE2
REMARK 470 ARG F 142 NE CZ NH1 NH2
REMARK 470 LYS F 170 CD CE NZ
REMARK 470 GLU F 184 CG CD OE1 OE2
REMARK 470 HIS F 382 CG ND1 CD2 CE1 NE2
REMARK 470 LYS F 421 CD CE NZ
REMARK 470 LYS F 430 CD CE NZ
REMARK 470 MET G 1 CG SD CE
REMARK 470 LYS G 80 CE NZ
REMARK 470 LYS G 170 CG CD CE NZ
REMARK 470 GLU G 184 CG CD OE1 OE2
REMARK 470 GLN G 193 CG CD OE1 NE2
REMARK 470 LYS G 267 CD CE NZ
REMARK 470 ARG G 312 NE CZ NH1 NH2
REMARK 470 LYS G 370 CD CE NZ
REMARK 470 ARG G 373 CG CD NE CZ NH1 NH2
REMARK 470 HIS G 382 CG ND1 CD2 CE1 NE2
REMARK 470 ASP G 389 CG OD1 OD2
REMARK 470 GLN G 390 CG CD OE1 NE2
REMARK 470 ARG G 393 CZ NH1 NH2
REMARK 470 LYS G 399 CG CD CE NZ
REMARK 470 LYS G 431 CE NZ
REMARK 470 LYS G 465 CD CE NZ
REMARK 470 VAL G 466 CG1 CG2
REMARK 470 MET H 1 CG SD CE
REMARK 470 LYS H 5 CE NZ
REMARK 470 ARG H 142 NE CZ NH1 NH2
REMARK 470 LYS H 170 CD CE NZ
REMARK 470 GLU H 184 CG CD OE1 OE2
REMARK 470 HIS H 382 CG ND1 CD2 CE1 NE2
REMARK 470 LYS H 421 CD CE NZ
REMARK 470 LYS H 430 CD CE NZ
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 ALA A 12 51.84 -97.05
REMARK 500 LYS A 67 -70.94 -97.52
REMARK 500 ARG A 102 -42.30 -137.84
REMARK 500 GLU A 184 42.11 -89.93
REMARK 500 TRP A 202 -4.82 -142.05
REMARK 500 LEU A 293 70.18 -117.67
REMARK 500 LEU A 322 47.11 -86.54
REMARK 500 ASP A 328 16.00 59.47
REMARK 500 GLU A 347 28.26 48.46
REMARK 500 GLU A 416 38.90 -83.46
REMARK 500 ALA B 12 53.64 -108.60
REMARK 500 LYS B 67 -71.71 -106.27
REMARK 500 LYS B 67 -72.18 -106.04
REMARK 500 ARG B 102 -61.44 -138.21
REMARK 500 ARG B 135 2.49 84.40
REMARK 500 ASN B 159 68.17 -150.02
REMARK 500 TRP B 202 -10.84 -143.40
REMARK 500 LEU B 322 48.12 -80.00
REMARK 500 GLU B 416 41.89 -85.17
REMARK 500 ALA C 12 47.83 -100.97
REMARK 500 CYS C 64 -10.39 -141.04
REMARK 500 LYS C 67 -67.73 -101.20
REMARK 500 ARG C 102 -47.37 -139.28
REMARK 500 LEU C 322 45.15 -85.93
REMARK 500 GLU C 416 36.24 -84.25
REMARK 500 ALA D 12 53.01 -115.31
REMARK 500 LYS D 67 -76.90 -100.36
REMARK 500 ARG D 102 -58.35 -142.78
REMARK 500 ARG D 135 3.15 83.10
REMARK 500 ASN D 159 72.82 -155.10
REMARK 500 TRP D 202 -9.67 -143.63
REMARK 500 LEU D 322 46.97 -84.47
REMARK 500 GLU D 416 40.79 -81.21
REMARK 500 ALA E 12 47.65 -96.90
REMARK 500 LYS E 67 -70.60 -95.45
REMARK 500 ARG E 102 -42.12 -139.25
REMARK 500 TRP E 202 -7.53 -143.34
REMARK 500 LEU E 322 46.97 -89.87
REMARK 500 GLU E 416 40.99 -86.18
REMARK 500 ALA F 12 52.05 -108.50
REMARK 500 LYS F 67 -73.78 -101.94
REMARK 500 ARG F 102 -60.18 -139.04
REMARK 500 ARG F 135 1.48 86.53
REMARK 500 ASN F 159 71.62 -150.33
REMARK 500 TRP F 202 -7.42 -144.66
REMARK 500 LEU F 322 45.33 -81.41
REMARK 500 GLU F 416 37.73 -84.77
REMARK 500 ALA G 12 36.22 -95.10
REMARK 500 LYS G 67 -66.83 -103.37
REMARK 500 ARG G 102 -45.69 -139.71
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAD A 500
REMARK 610 NAD C 500
REMARK 610 NAD E 500
REMARK 610 NAD G 500
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 4003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 4004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 4006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 4007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 4008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA G 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD H 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UGA H 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 5002
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 5003
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 5004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Q3E RELATED DB: PDB
REMARK 900 HUMAN UDP-GLUCOSE DEHYDROGENASE COMPLEXED WITH NADH AND UDP-GLUCOSE
REMARK 900 (SUBSTRATE COMPLEX)
DBREF 2QG4 A 1 466 UNP O60701 UGDH_HUMAN 1 466
DBREF 2QG4 B 1 466 UNP O60701 UGDH_HUMAN 1 466
DBREF 2QG4 C 1 466 UNP O60701 UGDH_HUMAN 1 466
DBREF 2QG4 D 1 466 UNP O60701 UGDH_HUMAN 1 466
DBREF 2QG4 E 1 466 UNP O60701 UGDH_HUMAN 1 466
DBREF 2QG4 F 1 466 UNP O60701 UGDH_HUMAN 1 466
DBREF 2QG4 G 1 466 UNP O60701 UGDH_HUMAN 1 466
DBREF 2QG4 H 1 466 UNP O60701 UGDH_HUMAN 1 466
SEQADV 2QG4 SER A 0 UNP O60701 CLONING ARTIFACT
SEQADV 2QG4 SER B 0 UNP O60701 CLONING ARTIFACT
SEQADV 2QG4 SER C 0 UNP O60701 CLONING ARTIFACT
SEQADV 2QG4 SER D 0 UNP O60701 CLONING ARTIFACT
SEQADV 2QG4 SER E 0 UNP O60701 CLONING ARTIFACT
SEQADV 2QG4 SER F 0 UNP O60701 CLONING ARTIFACT
SEQADV 2QG4 SER G 0 UNP O60701 CLONING ARTIFACT
SEQADV 2QG4 SER H 0 UNP O60701 CLONING ARTIFACT
SEQRES 1 A 467 SER MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA
SEQRES 2 A 467 GLY TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS
SEQRES 3 A 467 MET CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN
SEQRES 4 A 467 GLU SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO
SEQRES 5 A 467 ILE TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS
SEQRES 6 A 467 ARG GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP
SEQRES 7 A 467 ALA ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN
SEQRES 8 A 467 THR PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA
SEQRES 9 A 467 ALA ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE
SEQRES 10 A 467 VAL GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS
SEQRES 11 A 467 SER THR VAL PRO VAL ARG ALA ALA GLU SER ILE ARG ARG
SEQRES 12 A 467 ILE PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN
SEQRES 13 A 467 VAL LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA
SEQRES 14 A 467 ILE LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY
SEQRES 15 A 467 GLY ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA
SEQRES 16 A 467 LEU CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS
SEQRES 17 A 467 ILE LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS
SEQRES 18 A 467 LEU ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER
SEQRES 19 A 467 ILE ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA
SEQRES 20 A 467 ASP VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN
SEQRES 21 A 467 ARG ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE
SEQRES 22 A 467 GLY GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL
SEQRES 23 A 467 TYR LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG
SEQRES 24 A 467 TYR TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG
SEQRES 25 A 467 ARG ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN
SEQRES 26 A 467 THR VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA
SEQRES 27 A 467 PHE LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER
SEQRES 28 A 467 ILE TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS
SEQRES 29 A 467 LEU HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE
SEQRES 30 A 467 VAL VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP
SEQRES 31 A 467 GLN VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR
SEQRES 32 A 467 GLU ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR
SEQRES 33 A 467 GLU TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE
SEQRES 34 A 467 HIS LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY
SEQRES 35 A 467 ARG ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR
SEQRES 36 A 467 ILE GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL
SEQRES 1 B 467 SER MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA
SEQRES 2 B 467 GLY TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS
SEQRES 3 B 467 MET CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN
SEQRES 4 B 467 GLU SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO
SEQRES 5 B 467 ILE TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS
SEQRES 6 B 467 ARG GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP
SEQRES 7 B 467 ALA ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN
SEQRES 8 B 467 THR PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA
SEQRES 9 B 467 ALA ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE
SEQRES 10 B 467 VAL GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS
SEQRES 11 B 467 SER THR VAL PRO VAL ARG ALA ALA GLU SER ILE ARG ARG
SEQRES 12 B 467 ILE PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN
SEQRES 13 B 467 VAL LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA
SEQRES 14 B 467 ILE LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY
SEQRES 15 B 467 GLY ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA
SEQRES 16 B 467 LEU CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS
SEQRES 17 B 467 ILE LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS
SEQRES 18 B 467 LEU ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER
SEQRES 19 B 467 ILE ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA
SEQRES 20 B 467 ASP VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN
SEQRES 21 B 467 ARG ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE
SEQRES 22 B 467 GLY GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL
SEQRES 23 B 467 TYR LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG
SEQRES 24 B 467 TYR TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG
SEQRES 25 B 467 ARG ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN
SEQRES 26 B 467 THR VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA
SEQRES 27 B 467 PHE LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER
SEQRES 28 B 467 ILE TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS
SEQRES 29 B 467 LEU HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE
SEQRES 30 B 467 VAL VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP
SEQRES 31 B 467 GLN VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR
SEQRES 32 B 467 GLU ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR
SEQRES 33 B 467 GLU TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE
SEQRES 34 B 467 HIS LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY
SEQRES 35 B 467 ARG ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR
SEQRES 36 B 467 ILE GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL
SEQRES 1 C 467 SER MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA
SEQRES 2 C 467 GLY TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS
SEQRES 3 C 467 MET CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN
SEQRES 4 C 467 GLU SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO
SEQRES 5 C 467 ILE TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS
SEQRES 6 C 467 ARG GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP
SEQRES 7 C 467 ALA ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN
SEQRES 8 C 467 THR PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA
SEQRES 9 C 467 ALA ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE
SEQRES 10 C 467 VAL GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS
SEQRES 11 C 467 SER THR VAL PRO VAL ARG ALA ALA GLU SER ILE ARG ARG
SEQRES 12 C 467 ILE PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN
SEQRES 13 C 467 VAL LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA
SEQRES 14 C 467 ILE LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY
SEQRES 15 C 467 GLY ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA
SEQRES 16 C 467 LEU CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS
SEQRES 17 C 467 ILE LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS
SEQRES 18 C 467 LEU ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER
SEQRES 19 C 467 ILE ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA
SEQRES 20 C 467 ASP VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN
SEQRES 21 C 467 ARG ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE
SEQRES 22 C 467 GLY GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL
SEQRES 23 C 467 TYR LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG
SEQRES 24 C 467 TYR TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG
SEQRES 25 C 467 ARG ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN
SEQRES 26 C 467 THR VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA
SEQRES 27 C 467 PHE LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER
SEQRES 28 C 467 ILE TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS
SEQRES 29 C 467 LEU HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE
SEQRES 30 C 467 VAL VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP
SEQRES 31 C 467 GLN VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR
SEQRES 32 C 467 GLU ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR
SEQRES 33 C 467 GLU TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE
SEQRES 34 C 467 HIS LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY
SEQRES 35 C 467 ARG ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR
SEQRES 36 C 467 ILE GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL
SEQRES 1 D 467 SER MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA
SEQRES 2 D 467 GLY TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS
SEQRES 3 D 467 MET CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN
SEQRES 4 D 467 GLU SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO
SEQRES 5 D 467 ILE TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS
SEQRES 6 D 467 ARG GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP
SEQRES 7 D 467 ALA ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN
SEQRES 8 D 467 THR PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA
SEQRES 9 D 467 ALA ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE
SEQRES 10 D 467 VAL GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS
SEQRES 11 D 467 SER THR VAL PRO VAL ARG ALA ALA GLU SER ILE ARG ARG
SEQRES 12 D 467 ILE PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN
SEQRES 13 D 467 VAL LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA
SEQRES 14 D 467 ILE LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY
SEQRES 15 D 467 GLY ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA
SEQRES 16 D 467 LEU CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS
SEQRES 17 D 467 ILE LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS
SEQRES 18 D 467 LEU ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER
SEQRES 19 D 467 ILE ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA
SEQRES 20 D 467 ASP VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN
SEQRES 21 D 467 ARG ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE
SEQRES 22 D 467 GLY GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL
SEQRES 23 D 467 TYR LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG
SEQRES 24 D 467 TYR TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG
SEQRES 25 D 467 ARG ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN
SEQRES 26 D 467 THR VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA
SEQRES 27 D 467 PHE LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER
SEQRES 28 D 467 ILE TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS
SEQRES 29 D 467 LEU HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE
SEQRES 30 D 467 VAL VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP
SEQRES 31 D 467 GLN VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR
SEQRES 32 D 467 GLU ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR
SEQRES 33 D 467 GLU TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE
SEQRES 34 D 467 HIS LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY
SEQRES 35 D 467 ARG ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR
SEQRES 36 D 467 ILE GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL
SEQRES 1 E 467 SER MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA
SEQRES 2 E 467 GLY TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS
SEQRES 3 E 467 MET CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN
SEQRES 4 E 467 GLU SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO
SEQRES 5 E 467 ILE TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS
SEQRES 6 E 467 ARG GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP
SEQRES 7 E 467 ALA ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN
SEQRES 8 E 467 THR PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA
SEQRES 9 E 467 ALA ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE
SEQRES 10 E 467 VAL GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS
SEQRES 11 E 467 SER THR VAL PRO VAL ARG ALA ALA GLU SER ILE ARG ARG
SEQRES 12 E 467 ILE PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN
SEQRES 13 E 467 VAL LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA
SEQRES 14 E 467 ILE LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY
SEQRES 15 E 467 GLY ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA
SEQRES 16 E 467 LEU CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS
SEQRES 17 E 467 ILE LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS
SEQRES 18 E 467 LEU ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER
SEQRES 19 E 467 ILE ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA
SEQRES 20 E 467 ASP VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN
SEQRES 21 E 467 ARG ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE
SEQRES 22 E 467 GLY GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL
SEQRES 23 E 467 TYR LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG
SEQRES 24 E 467 TYR TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG
SEQRES 25 E 467 ARG ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN
SEQRES 26 E 467 THR VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA
SEQRES 27 E 467 PHE LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER
SEQRES 28 E 467 ILE TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS
SEQRES 29 E 467 LEU HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE
SEQRES 30 E 467 VAL VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP
SEQRES 31 E 467 GLN VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR
SEQRES 32 E 467 GLU ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR
SEQRES 33 E 467 GLU TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE
SEQRES 34 E 467 HIS LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY
SEQRES 35 E 467 ARG ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR
SEQRES 36 E 467 ILE GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL
SEQRES 1 F 467 SER MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA
SEQRES 2 F 467 GLY TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS
SEQRES 3 F 467 MET CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN
SEQRES 4 F 467 GLU SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO
SEQRES 5 F 467 ILE TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS
SEQRES 6 F 467 ARG GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP
SEQRES 7 F 467 ALA ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN
SEQRES 8 F 467 THR PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA
SEQRES 9 F 467 ALA ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE
SEQRES 10 F 467 VAL GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS
SEQRES 11 F 467 SER THR VAL PRO VAL ARG ALA ALA GLU SER ILE ARG ARG
SEQRES 12 F 467 ILE PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN
SEQRES 13 F 467 VAL LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA
SEQRES 14 F 467 ILE LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY
SEQRES 15 F 467 GLY ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA
SEQRES 16 F 467 LEU CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS
SEQRES 17 F 467 ILE LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS
SEQRES 18 F 467 LEU ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER
SEQRES 19 F 467 ILE ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA
SEQRES 20 F 467 ASP VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN
SEQRES 21 F 467 ARG ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE
SEQRES 22 F 467 GLY GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL
SEQRES 23 F 467 TYR LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG
SEQRES 24 F 467 TYR TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG
SEQRES 25 F 467 ARG ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN
SEQRES 26 F 467 THR VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA
SEQRES 27 F 467 PHE LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER
SEQRES 28 F 467 ILE TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS
SEQRES 29 F 467 LEU HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE
SEQRES 30 F 467 VAL VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP
SEQRES 31 F 467 GLN VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR
SEQRES 32 F 467 GLU ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR
SEQRES 33 F 467 GLU TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE
SEQRES 34 F 467 HIS LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY
SEQRES 35 F 467 ARG ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR
SEQRES 36 F 467 ILE GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL
SEQRES 1 G 467 SER MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA
SEQRES 2 G 467 GLY TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS
SEQRES 3 G 467 MET CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN
SEQRES 4 G 467 GLU SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO
SEQRES 5 G 467 ILE TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS
SEQRES 6 G 467 ARG GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP
SEQRES 7 G 467 ALA ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN
SEQRES 8 G 467 THR PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA
SEQRES 9 G 467 ALA ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE
SEQRES 10 G 467 VAL GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS
SEQRES 11 G 467 SER THR VAL PRO VAL ARG ALA ALA GLU SER ILE ARG ARG
SEQRES 12 G 467 ILE PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN
SEQRES 13 G 467 VAL LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA
SEQRES 14 G 467 ILE LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY
SEQRES 15 G 467 GLY ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA
SEQRES 16 G 467 LEU CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS
SEQRES 17 G 467 ILE LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS
SEQRES 18 G 467 LEU ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER
SEQRES 19 G 467 ILE ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA
SEQRES 20 G 467 ASP VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN
SEQRES 21 G 467 ARG ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE
SEQRES 22 G 467 GLY GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL
SEQRES 23 G 467 TYR LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG
SEQRES 24 G 467 TYR TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG
SEQRES 25 G 467 ARG ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN
SEQRES 26 G 467 THR VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA
SEQRES 27 G 467 PHE LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER
SEQRES 28 G 467 ILE TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS
SEQRES 29 G 467 LEU HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE
SEQRES 30 G 467 VAL VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP
SEQRES 31 G 467 GLN VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR
SEQRES 32 G 467 GLU ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR
SEQRES 33 G 467 GLU TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE
SEQRES 34 G 467 HIS LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY
SEQRES 35 G 467 ARG ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR
SEQRES 36 G 467 ILE GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL
SEQRES 1 H 467 SER MET PHE GLU ILE LYS LYS ILE CYS CYS ILE GLY ALA
SEQRES 2 H 467 GLY TYR VAL GLY GLY PRO THR CYS SER VAL ILE ALA HIS
SEQRES 3 H 467 MET CYS PRO GLU ILE ARG VAL THR VAL VAL ASP VAL ASN
SEQRES 4 H 467 GLU SER ARG ILE ASN ALA TRP ASN SER PRO THR LEU PRO
SEQRES 5 H 467 ILE TYR GLU PRO GLY LEU LYS GLU VAL VAL GLU SER CYS
SEQRES 6 H 467 ARG GLY LYS ASN LEU PHE PHE SER THR ASN ILE ASP ASP
SEQRES 7 H 467 ALA ILE LYS GLU ALA ASP LEU VAL PHE ILE SER VAL ASN
SEQRES 8 H 467 THR PRO THR LYS THR TYR GLY MET GLY LYS GLY ARG ALA
SEQRES 9 H 467 ALA ASP LEU LYS TYR ILE GLU ALA CYS ALA ARG ARG ILE
SEQRES 10 H 467 VAL GLN ASN SER ASN GLY TYR LYS ILE VAL THR GLU LYS
SEQRES 11 H 467 SER THR VAL PRO VAL ARG ALA ALA GLU SER ILE ARG ARG
SEQRES 12 H 467 ILE PHE ASP ALA ASN THR LYS PRO ASN LEU ASN LEU GLN
SEQRES 13 H 467 VAL LEU SER ASN PRO GLU PHE LEU ALA GLU GLY THR ALA
SEQRES 14 H 467 ILE LYS ASP LEU LYS ASN PRO ASP ARG VAL LEU ILE GLY
SEQRES 15 H 467 GLY ASP GLU THR PRO GLU GLY GLN ARG ALA VAL GLN ALA
SEQRES 16 H 467 LEU CYS ALA VAL TYR GLU HIS TRP VAL PRO ARG GLU LYS
SEQRES 17 H 467 ILE LEU THR THR ASN THR TRP SER SER GLU LEU SER LYS
SEQRES 18 H 467 LEU ALA ALA ASN ALA PHE LEU ALA GLN ARG ILE SER SER
SEQRES 19 H 467 ILE ASN SER ILE SER ALA LEU CYS GLU ALA THR GLY ALA
SEQRES 20 H 467 ASP VAL GLU GLU VAL ALA THR ALA ILE GLY MET ASP GLN
SEQRES 21 H 467 ARG ILE GLY ASN LYS PHE LEU LYS ALA SER VAL GLY PHE
SEQRES 22 H 467 GLY GLY SER CYS PHE GLN LYS ASP VAL LEU ASN LEU VAL
SEQRES 23 H 467 TYR LEU CYS GLU ALA LEU ASN LEU PRO GLU VAL ALA ARG
SEQRES 24 H 467 TYR TRP GLN GLN VAL ILE ASP MET ASN ASP TYR GLN ARG
SEQRES 25 H 467 ARG ARG PHE ALA SER ARG ILE ILE ASP SER LEU PHE ASN
SEQRES 26 H 467 THR VAL THR ASP LYS LYS ILE ALA ILE LEU GLY PHE ALA
SEQRES 27 H 467 PHE LYS LYS ASP THR GLY ASP THR ARG GLU SER SER SER
SEQRES 28 H 467 ILE TYR ILE SER LYS TYR LEU MET ASP GLU GLY ALA HIS
SEQRES 29 H 467 LEU HIS ILE TYR ASP PRO LYS VAL PRO ARG GLU GLN ILE
SEQRES 30 H 467 VAL VAL ASP LEU SER HIS PRO GLY VAL SER GLU ASP ASP
SEQRES 31 H 467 GLN VAL SER ARG LEU VAL THR ILE SER LYS ASP PRO TYR
SEQRES 32 H 467 GLU ALA CYS ASP GLY ALA HIS ALA VAL VAL ILE CYS THR
SEQRES 33 H 467 GLU TRP ASP MET PHE LYS GLU LEU ASP TYR GLU ARG ILE
SEQRES 34 H 467 HIS LYS LYS MET LEU LYS PRO ALA PHE ILE PHE ASP GLY
SEQRES 35 H 467 ARG ARG VAL LEU ASP GLY LEU HIS ASN GLU LEU GLN THR
SEQRES 36 H 467 ILE GLY PHE GLN ILE GLU THR ILE GLY LYS LYS VAL
HET NAD A 500 27
HET UGA A 501 37
HET CL B4002 1
HET CL B4005 1
HET NAD B 500 44
HET UGA B 501 37
HET EDO B5001 4
HET NAD C 500 27
HET UGA C 501 37
HET EDO C5002 4
HET CL D4001 1
HET CL D4006 1
HET NAD D 500 44
HET UGA D 501 37
HET NAD E 500 27
HET UGA E 501 37
HET CL F4003 1
HET CL F4007 1
HET NAD F 500 44
HET UGA F 501 37
HET EDO F5003 4
HET NAD G 500 27
HET UGA G 501 37
HET EDO G5004 4
HET CL H4004 1
HET CL H4008 1
HET NAD H 500 44
HET UGA H 501 37
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM UGA URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN UGA UDP-GLUCURONIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 9 NAD 8(C21 H27 N7 O14 P2)
FORMUL 10 UGA 8(C15 H22 N2 O18 P2)
FORMUL 11 CL 8(CL 1-)
FORMUL 15 EDO 4(C2 H6 O2)
FORMUL 37 HOH *2999(H2 O)
HELIX 1 1 VAL A 15 CYS A 27 1 13
HELIX 2 2 ASN A 38 ASN A 46 1 9
HELIX 3 3 GLY A 56 ARG A 65 1 10
HELIX 4 4 ASN A 74 ALA A 82 1 9
HELIX 5 5 LEU A 106 ASN A 119 1 14
HELIX 6 6 ARG A 135 ASN A 147 1 13
HELIX 7 7 THR A 167 ASN A 174 1 8
HELIX 8 8 THR A 185 GLU A 200 1 16
HELIX 9 9 PRO A 204 GLU A 206 5 3
HELIX 10 10 ASN A 212 GLY A 245 1 34
HELIX 11 11 ASP A 247 MET A 257 1 11
HELIX 12 12 CYS A 276 LEU A 291 1 16
HELIX 13 13 LEU A 293 LEU A 322 1 30
HELIX 14 14 SER A 348 ASP A 359 1 12
HELIX 15 15 PRO A 372 LEU A 380 1 9
HELIX 16 16 ASP A 389 LEU A 394 1 6
HELIX 17 17 ASP A 400 ASP A 406 1 7
HELIX 18 18 TRP A 417 LEU A 423 5 7
HELIX 19 19 ASP A 424 MET A 432 1 9
HELIX 20 20 LEU A 448 GLY A 456 1 9
HELIX 21 21 VAL B 15 CYS B 27 1 13
HELIX 22 22 ASN B 38 ASN B 46 1 9
HELIX 23 23 GLY B 56 ARG B 65 1 10
HELIX 24 24 ASN B 74 ALA B 82 1 9
HELIX 25 25 LEU B 106 SER B 120 1 15
HELIX 26 26 ARG B 135 ALA B 146 1 12
HELIX 27 27 THR B 167 ASN B 174 1 8
HELIX 28 28 THR B 185 GLU B 200 1 16
HELIX 29 29 PRO B 204 GLU B 206 5 3
HELIX 30 30 ASN B 212 GLY B 245 1 34
HELIX 31 31 ASP B 247 MET B 257 1 11
HELIX 32 32 CYS B 276 LEU B 291 1 16
HELIX 33 33 LEU B 293 LEU B 322 1 30
HELIX 34 34 SER B 348 GLU B 360 1 13
HELIX 35 35 PRO B 372 SER B 381 1 10
HELIX 36 36 ASP B 388 LEU B 394 1 7
HELIX 37 37 ASP B 400 ASP B 406 1 7
HELIX 38 38 TRP B 417 LEU B 423 5 7
HELIX 39 39 ASP B 424 MET B 432 1 9
HELIX 40 40 LEU B 448 GLY B 456 1 9
HELIX 41 41 VAL C 15 CYS C 27 1 13
HELIX 42 42 ASN C 38 ASN C 46 1 9
HELIX 43 43 GLY C 56 ARG C 65 1 10
HELIX 44 44 ASN C 74 ALA C 82 1 9
HELIX 45 45 LEU C 106 SER C 120 1 15
HELIX 46 46 ARG C 135 ASN C 147 1 13
HELIX 47 47 THR C 167 ASN C 174 1 8
HELIX 48 48 THR C 185 GLU C 200 1 16
HELIX 49 49 PRO C 204 GLU C 206 5 3
HELIX 50 50 ASN C 212 GLY C 245 1 34
HELIX 51 51 ASP C 247 MET C 257 1 11
HELIX 52 52 CYS C 276 LEU C 291 1 16
HELIX 53 53 LEU C 293 LEU C 322 1 30
HELIX 54 54 SER C 348 GLU C 360 1 13
HELIX 55 55 PRO C 372 LEU C 380 1 9
HELIX 56 56 GLN C 390 LEU C 394 1 5
HELIX 57 57 ASP C 400 ASP C 406 1 7
HELIX 58 58 TRP C 417 LEU C 423 5 7
HELIX 59 59 ASP C 424 MET C 432 1 9
HELIX 60 60 LEU C 448 GLY C 456 1 9
HELIX 61 61 VAL D 15 CYS D 27 1 13
HELIX 62 62 ASN D 38 ASN D 46 1 9
HELIX 63 63 GLY D 56 ARG D 65 1 10
HELIX 64 64 ASN D 74 ALA D 82 1 9
HELIX 65 65 LEU D 106 ASN D 119 1 14
HELIX 66 66 ARG D 135 ASN D 147 1 13
HELIX 67 67 THR D 167 ASN D 174 1 8
HELIX 68 68 THR D 185 GLU D 200 1 16
HELIX 69 69 PRO D 204 GLU D 206 5 3
HELIX 70 70 ASN D 212 GLY D 245 1 34
HELIX 71 71 ASP D 247 MET D 257 1 11
HELIX 72 72 CYS D 276 LEU D 291 1 16
HELIX 73 73 LEU D 293 LEU D 322 1 30
HELIX 74 74 SER D 348 GLU D 360 1 13
HELIX 75 75 PRO D 372 SER D 381 1 10
HELIX 76 76 ASP D 388 LEU D 394 1 7
HELIX 77 77 ASP D 400 ASP D 406 1 7
HELIX 78 78 ASP D 424 MET D 432 1 9
HELIX 79 79 LEU D 448 GLY D 456 1 9
HELIX 80 80 VAL E 15 CYS E 27 1 13
HELIX 81 81 ASN E 38 ASN E 46 1 9
HELIX 82 82 GLY E 56 ARG E 65 1 10
HELIX 83 83 ASN E 74 ALA E 82 1 9
HELIX 84 84 LEU E 106 ASN E 119 1 14
HELIX 85 85 ARG E 135 ASN E 147 1 13
HELIX 86 86 THR E 167 ASN E 174 1 8
HELIX 87 87 THR E 185 GLU E 200 1 16
HELIX 88 88 PRO E 204 GLU E 206 5 3
HELIX 89 89 ASN E 212 GLY E 245 1 34
HELIX 90 90 ASP E 247 MET E 257 1 11
HELIX 91 91 CYS E 276 LEU E 291 1 16
HELIX 92 92 LEU E 293 LEU E 322 1 30
HELIX 93 93 SER E 348 ASP E 359 1 12
HELIX 94 94 PRO E 372 SER E 381 1 10
HELIX 95 95 GLN E 390 LEU E 394 1 5
HELIX 96 96 ASP E 400 ASP E 406 1 7
HELIX 97 97 TRP E 417 LEU E 423 5 7
HELIX 98 98 ASP E 424 MET E 432 1 9
HELIX 99 99 LEU E 448 GLY E 456 1 9
HELIX 100 100 VAL F 15 CYS F 27 1 13
HELIX 101 101 ASN F 38 ASN F 46 1 9
HELIX 102 102 GLY F 56 ARG F 65 1 10
HELIX 103 103 ASN F 74 ALA F 82 1 9
HELIX 104 104 LEU F 106 SER F 120 1 15
HELIX 105 105 ARG F 135 ASN F 147 1 13
HELIX 106 106 THR F 167 ASN F 174 1 8
HELIX 107 107 THR F 185 GLU F 200 1 16
HELIX 108 108 PRO F 204 GLU F 206 5 3
HELIX 109 109 ASN F 212 GLY F 245 1 34
HELIX 110 110 ASP F 247 MET F 257 1 11
HELIX 111 111 CYS F 276 LEU F 291 1 16
HELIX 112 112 LEU F 293 LEU F 322 1 30
HELIX 113 113 SER F 348 GLU F 360 1 13
HELIX 114 114 PRO F 372 SER F 381 1 10
HELIX 115 115 ASP F 388 LEU F 394 1 7
HELIX 116 116 ASP F 400 ASP F 406 1 7
HELIX 117 117 TRP F 417 LEU F 423 5 7
HELIX 118 118 ASP F 424 MET F 432 1 9
HELIX 119 119 LEU F 448 GLY F 456 1 9
HELIX 120 120 VAL G 15 CYS G 27 1 13
HELIX 121 121 ASN G 38 ASN G 46 1 9
HELIX 122 122 GLY G 56 ARG G 65 1 10
HELIX 123 123 ASN G 74 ALA G 82 1 9
HELIX 124 124 LEU G 106 ASN G 119 1 14
HELIX 125 125 ARG G 135 ASN G 147 1 13
HELIX 126 126 THR G 167 ASN G 174 1 8
HELIX 127 127 THR G 185 GLU G 200 1 16
HELIX 128 128 PRO G 204 GLU G 206 5 3
HELIX 129 129 ASN G 212 GLY G 245 1 34
HELIX 130 130 ASP G 247 MET G 257 1 11
HELIX 131 131 CYS G 276 LEU G 291 1 16
HELIX 132 132 LEU G 293 LEU G 322 1 30
HELIX 133 133 SER G 348 GLU G 360 1 13
HELIX 134 134 PRO G 372 SER G 381 1 10
HELIX 135 135 ASP G 389 LEU G 394 1 6
HELIX 136 136 ASP G 400 ASP G 406 1 7
HELIX 137 137 TRP G 417 LEU G 423 5 7
HELIX 138 138 ASP G 424 MET G 432 1 9
HELIX 139 139 LEU G 448 GLY G 456 1 9
HELIX 140 140 VAL H 15 CYS H 27 1 13
HELIX 141 141 ASN H 38 ASN H 46 1 9
HELIX 142 142 GLY H 56 ARG H 65 1 10
HELIX 143 143 ASN H 74 ALA H 82 1 9
HELIX 144 144 LEU H 106 ASN H 119 1 14
HELIX 145 145 ARG H 135 ASN H 147 1 13
HELIX 146 146 THR H 167 ASN H 174 1 8
HELIX 147 147 THR H 185 GLU H 200 1 16
HELIX 148 148 PRO H 204 GLU H 206 5 3
HELIX 149 149 ASN H 212 GLY H 245 1 34
HELIX 150 150 ASP H 247 MET H 257 1 11
HELIX 151 151 CYS H 276 LEU H 291 1 16
HELIX 152 152 LEU H 293 LEU H 322 1 30
HELIX 153 153 SER H 348 ASP H 359 1 12
HELIX 154 154 PRO H 372 SER H 381 1 10
HELIX 155 155 ASP H 388 LEU H 394 1 7
HELIX 156 156 ASP H 400 ASP H 406 1 7
HELIX 157 157 TRP H 417 LEU H 423 5 7
HELIX 158 158 ASP H 424 MET H 432 1 9
HELIX 159 159 LEU H 448 GLY H 456 1 9
SHEET 1 A 6 LEU A 69 SER A 72 0
SHEET 2 A 6 ARG A 31 VAL A 35 1 N VAL A 34 O PHE A 70
SHEET 3 A 6 LYS A 6 ILE A 10 1 N CYS A 9 O VAL A 35
SHEET 4 A 6 LEU A 84 ILE A 87 1 O PHE A 86 N ILE A 10
SHEET 5 A 6 TYR A 123 GLU A 128 1 O ILE A 125 N VAL A 85
SHEET 6 A 6 ASN A 153 SER A 158 1 O GLN A 155 N VAL A 126
SHEET 1 B 2 VAL A 178 GLY A 181 0
SHEET 2 B 2 ILE A 208 THR A 211 1 O LEU A 209 N VAL A 178
SHEET 1 C 6 VAL A 395 ILE A 397 0
SHEET 2 C 6 HIS A 363 TYR A 367 1 N LEU A 364 O THR A 396
SHEET 3 C 6 LYS A 330 LEU A 334 1 N ILE A 333 O TYR A 367
SHEET 4 C 6 ALA A 410 ILE A 413 1 O VAL A 412 N ALA A 332
SHEET 5 C 6 PHE A 437 ASP A 440 1 O PHE A 439 N VAL A 411
SHEET 6 C 6 GLN A 458 THR A 461 1 O GLU A 460 N ILE A 438
SHEET 1 D 6 LEU B 69 SER B 72 0
SHEET 2 D 6 ARG B 31 VAL B 35 1 N VAL B 34 O PHE B 70
SHEET 3 D 6 LYS B 6 ILE B 10 1 N ILE B 7 O ARG B 31
SHEET 4 D 6 LEU B 84 ILE B 87 1 O PHE B 86 N CYS B 8
SHEET 5 D 6 TYR B 123 GLU B 128 1 O THR B 127 N VAL B 85
SHEET 6 D 6 ASN B 153 SER B 158 1 O GLN B 155 N VAL B 126
SHEET 1 E 2 VAL B 178 GLY B 181 0
SHEET 2 E 2 ILE B 208 THR B 211 1 O LEU B 209 N VAL B 178
SHEET 1 F 6 VAL B 395 ILE B 397 0
SHEET 2 F 6 HIS B 363 TYR B 367 1 N ILE B 366 O THR B 396
SHEET 3 F 6 LYS B 330 LEU B 334 1 N ILE B 333 O HIS B 365
SHEET 4 F 6 ALA B 410 ILE B 413 1 O VAL B 412 N ALA B 332
SHEET 5 F 6 PHE B 437 ASP B 440 1 O PHE B 439 N VAL B 411
SHEET 6 F 6 GLN B 458 THR B 461 1 O GLN B 458 N ILE B 438
SHEET 1 G 6 LEU C 69 SER C 72 0
SHEET 2 G 6 ARG C 31 VAL C 35 1 N VAL C 34 O PHE C 70
SHEET 3 G 6 LYS C 6 ILE C 10 1 N CYS C 9 O VAL C 35
SHEET 4 G 6 LEU C 84 ILE C 87 1 O PHE C 86 N CYS C 8
SHEET 5 G 6 TYR C 123 GLU C 128 1 O THR C 127 N VAL C 85
SHEET 6 G 6 ASN C 153 SER C 158 1 O GLN C 155 N VAL C 126
SHEET 1 H 2 VAL C 178 GLY C 181 0
SHEET 2 H 2 ILE C 208 THR C 211 1 O LEU C 209 N VAL C 178
SHEET 1 I 6 VAL C 395 ILE C 397 0
SHEET 2 I 6 HIS C 363 TYR C 367 1 N ILE C 366 O THR C 396
SHEET 3 I 6 LYS C 330 LEU C 334 1 N ILE C 333 O TYR C 367
SHEET 4 I 6 ALA C 410 ILE C 413 1 O VAL C 412 N ALA C 332
SHEET 5 I 6 PHE C 437 ASP C 440 1 O PHE C 439 N VAL C 411
SHEET 6 I 6 GLN C 458 THR C 461 1 O GLU C 460 N ILE C 438
SHEET 1 J 6 LEU D 69 SER D 72 0
SHEET 2 J 6 ARG D 31 VAL D 35 1 N VAL D 34 O PHE D 70
SHEET 3 J 6 LYS D 6 ILE D 10 1 N ILE D 7 O ARG D 31
SHEET 4 J 6 LEU D 84 ILE D 87 1 O LEU D 84 N CYS D 8
SHEET 5 J 6 TYR D 123 GLU D 128 1 O THR D 127 N VAL D 85
SHEET 6 J 6 ASN D 153 SER D 158 1 O GLN D 155 N VAL D 126
SHEET 1 K 2 VAL D 178 GLY D 181 0
SHEET 2 K 2 ILE D 208 THR D 211 1 O LEU D 209 N VAL D 178
SHEET 1 L 6 VAL D 395 ILE D 397 0
SHEET 2 L 6 HIS D 363 TYR D 367 1 N LEU D 364 O THR D 396
SHEET 3 L 6 LYS D 330 LEU D 334 1 N ILE D 331 O HIS D 363
SHEET 4 L 6 ALA D 410 ILE D 413 1 O VAL D 412 N ALA D 332
SHEET 5 L 6 PHE D 437 ASP D 440 1 O PHE D 439 N VAL D 411
SHEET 6 L 6 GLN D 458 THR D 461 1 O GLU D 460 N ASP D 440
SHEET 1 M 6 LEU E 69 SER E 72 0
SHEET 2 M 6 ARG E 31 VAL E 35 1 N VAL E 34 O PHE E 70
SHEET 3 M 6 LYS E 6 ILE E 10 1 N CYS E 9 O VAL E 35
SHEET 4 M 6 LEU E 84 ILE E 87 1 O PHE E 86 N CYS E 8
SHEET 5 M 6 TYR E 123 GLU E 128 1 O ILE E 125 N VAL E 85
SHEET 6 M 6 ASN E 153 SER E 158 1 O GLN E 155 N VAL E 126
SHEET 1 N 2 VAL E 178 GLY E 181 0
SHEET 2 N 2 ILE E 208 THR E 211 1 O LEU E 209 N VAL E 178
SHEET 1 O 6 VAL E 395 ILE E 397 0
SHEET 2 O 6 HIS E 363 TYR E 367 1 N LEU E 364 O THR E 396
SHEET 3 O 6 LYS E 330 LEU E 334 1 N ILE E 333 O HIS E 365
SHEET 4 O 6 ALA E 410 ILE E 413 1 O VAL E 412 N ALA E 332
SHEET 5 O 6 PHE E 437 ASP E 440 1 O PHE E 439 N VAL E 411
SHEET 6 O 6 GLN E 458 THR E 461 1 O GLU E 460 N ILE E 438
SHEET 1 P 6 LEU F 69 SER F 72 0
SHEET 2 P 6 ARG F 31 VAL F 35 1 N VAL F 34 O PHE F 70
SHEET 3 P 6 LYS F 6 ILE F 10 1 N ILE F 7 O ARG F 31
SHEET 4 P 6 LEU F 84 ILE F 87 1 O PHE F 86 N CYS F 8
SHEET 5 P 6 TYR F 123 GLU F 128 1 O THR F 127 N VAL F 85
SHEET 6 P 6 ASN F 153 SER F 158 1 O GLN F 155 N VAL F 126
SHEET 1 Q 2 VAL F 178 GLY F 181 0
SHEET 2 Q 2 ILE F 208 THR F 211 1 O LEU F 209 N VAL F 178
SHEET 1 R 6 VAL F 395 ILE F 397 0
SHEET 2 R 6 HIS F 363 TYR F 367 1 N ILE F 366 O THR F 396
SHEET 3 R 6 LYS F 330 LEU F 334 1 N ILE F 333 O HIS F 365
SHEET 4 R 6 ALA F 410 ILE F 413 1 O VAL F 412 N ALA F 332
SHEET 5 R 6 PHE F 437 ASP F 440 1 O PHE F 439 N VAL F 411
SHEET 6 R 6 GLN F 458 THR F 461 1 O GLU F 460 N ASP F 440
SHEET 1 S 6 LEU G 69 SER G 72 0
SHEET 2 S 6 ARG G 31 VAL G 35 1 N VAL G 34 O PHE G 70
SHEET 3 S 6 LYS G 6 ILE G 10 1 N CYS G 9 O VAL G 35
SHEET 4 S 6 LEU G 84 ILE G 87 1 O PHE G 86 N CYS G 8
SHEET 5 S 6 TYR G 123 GLU G 128 1 O THR G 127 N ILE G 87
SHEET 6 S 6 ASN G 153 SER G 158 1 O GLN G 155 N VAL G 126
SHEET 1 T 2 VAL G 178 GLY G 181 0
SHEET 2 T 2 ILE G 208 THR G 211 1 O LEU G 209 N VAL G 178
SHEET 1 U 6 VAL G 395 ILE G 397 0
SHEET 2 U 6 HIS G 363 TYR G 367 1 N LEU G 364 O THR G 396
SHEET 3 U 6 LYS G 330 LEU G 334 1 N ILE G 333 O HIS G 365
SHEET 4 U 6 ALA G 410 ILE G 413 1 O VAL G 412 N LEU G 334
SHEET 5 U 6 PHE G 437 ASP G 440 1 O PHE G 439 N VAL G 411
SHEET 6 U 6 GLN G 458 THR G 461 1 O GLU G 460 N ILE G 438
SHEET 1 V 6 LEU H 69 SER H 72 0
SHEET 2 V 6 ARG H 31 VAL H 35 1 N VAL H 34 O PHE H 70
SHEET 3 V 6 LYS H 6 ILE H 10 1 N ILE H 7 O ARG H 31
SHEET 4 V 6 LEU H 84 ILE H 87 1 O LEU H 84 N CYS H 8
SHEET 5 V 6 TYR H 123 GLU H 128 1 O THR H 127 N ILE H 87
SHEET 6 V 6 ASN H 153 SER H 158 1 O GLN H 155 N VAL H 126
SHEET 1 W 2 VAL H 178 GLY H 181 0
SHEET 2 W 2 ILE H 208 THR H 211 1 O LEU H 209 N VAL H 178
SHEET 1 X 6 VAL H 395 ILE H 397 0
SHEET 2 X 6 HIS H 363 TYR H 367 1 N LEU H 364 O THR H 396
SHEET 3 X 6 LYS H 330 LEU H 334 1 N ILE H 333 O TYR H 367
SHEET 4 X 6 ALA H 410 ILE H 413 1 O VAL H 412 N ALA H 332
SHEET 5 X 6 PHE H 437 ASP H 440 1 O PHE H 439 N VAL H 411
SHEET 6 X 6 GLN H 458 THR H 461 1 O GLU H 460 N ASP H 440
CISPEP 1 LYS A 434 PRO A 435 0 4.01
CISPEP 2 LYS B 434 PRO B 435 0 -3.16
CISPEP 3 LYS C 434 PRO C 435 0 4.42
CISPEP 4 LYS D 434 PRO D 435 0 0.69
CISPEP 5 LYS E 434 PRO E 435 0 2.66
CISPEP 6 LYS F 434 PRO F 435 0 -2.03
CISPEP 7 LYS G 434 PRO G 435 0 1.96
CISPEP 8 LYS H 434 PRO H 435 0 1.25
SITE 1 AC1 2 MET D 419 HOH D4143
SITE 1 AC2 1 MET B 419
SITE 1 AC3 1 MET F 419
SITE 1 AC4 1 MET H 419
SITE 1 AC5 3 ASP B 183 THR B 213 TRP B 214
SITE 1 AC6 2 ASP D 183 THR D 213
SITE 1 AC7 3 ASP F 183 THR F 213 TRP F 214
SITE 1 AC8 3 ASP H 183 THR H 213 TRP H 214
SITE 1 AC9 13 ILE A 10 GLY A 11 GLY A 13 TYR A 14
SITE 2 AC9 13 VAL A 15 ASP A 36 VAL A 37 ARG A 41
SITE 3 AC9 13 VAL A 89 ASN A 90 TYR A 108 HOH A 563
SITE 4 AC9 13 HOH A 832
SITE 1 BC1 27 GLU A 161 PHE A 162 LEU A 163 GLU A 165
SITE 2 BC1 27 LYS A 220 ASN A 224 ILE A 231 PHE A 265
SITE 3 BC1 27 LEU A 266 LYS A 267 SER A 269 PHE A 272
SITE 4 BC1 27 GLY A 273 CYS A 276 PHE A 277 PHE A 338
SITE 5 BC1 27 LYS A 339 ARG A 442 HOH A 503 HOH A 520
SITE 6 BC1 27 HOH A 534 HOH A 548 HOH A 575 HOH A 600
SITE 7 BC1 27 HOH A 658 HOH A 707 ARG B 260
SITE 1 BC2 31 ILE B 10 GLY B 11 GLY B 13 TYR B 14
SITE 2 BC2 31 VAL B 15 ASP B 36 VAL B 37 ARG B 41
SITE 3 BC2 31 SER B 88 VAL B 89 ASN B 90 THR B 91
SITE 4 BC2 31 TYR B 108 SER B 130 THR B 131 GLU B 161
SITE 5 BC2 31 LEU B 163 GLU B 165 CYS B 276 LYS B 279
SITE 6 BC2 31 ARG B 346 UGA B 501 HOH B5012 HOH B5041
SITE 7 BC2 31 HOH B5052 HOH B5070 HOH B5079 HOH B5091
SITE 8 BC2 31 HOH B5098 HOH B5163 HOH B5179
SITE 1 BC3 29 ARG A 260 GLU B 161 PHE B 162 LEU B 163
SITE 2 BC3 29 ALA B 164 GLU B 165 LYS B 220 ASN B 224
SITE 3 BC3 29 ILE B 231 PHE B 265 LEU B 266 LYS B 267
SITE 4 BC3 29 SER B 269 PHE B 272 GLY B 273 CYS B 276
SITE 5 BC3 29 PHE B 277 PHE B 338 LYS B 339 ARG B 442
SITE 6 BC3 29 NAD B 500 HOH B5016 HOH B5063 HOH B5070
SITE 7 BC3 29 HOH B5098 HOH B5106 HOH B5128 HOH B5130
SITE 8 BC3 29 HOH B5139
SITE 1 BC4 16 ILE C 10 GLY C 11 GLY C 13 TYR C 14
SITE 2 BC4 16 VAL C 15 ASP C 36 VAL C 37 ARG C 41
SITE 3 BC4 16 ILE C 75 SER C 88 VAL C 89 ASN C 90
SITE 4 BC4 16 HOH C5084 HOH C5156 HOH C5206 HOH C5287
SITE 1 BC5 28 GLU C 161 PHE C 162 LEU C 163 GLU C 165
SITE 2 BC5 28 LYS C 220 ASN C 224 ILE C 231 PHE C 265
SITE 3 BC5 28 LEU C 266 LYS C 267 SER C 269 PHE C 272
SITE 4 BC5 28 GLY C 273 CYS C 276 PHE C 277 PHE C 338
SITE 5 BC5 28 LYS C 339 ARG C 442 HOH C5003 HOH C5024
SITE 6 BC5 28 HOH C5029 HOH C5039 HOH C5050 HOH C5053
SITE 7 BC5 28 HOH C5081 HOH C5094 HOH C5142 ARG D 260
SITE 1 BC6 32 ILE D 10 GLY D 11 GLY D 13 TYR D 14
SITE 2 BC6 32 VAL D 15 ASP D 36 VAL D 37 ARG D 41
SITE 3 BC6 32 SER D 88 VAL D 89 ASN D 90 THR D 91
SITE 4 BC6 32 TYR D 108 SER D 130 THR D 131 GLU D 161
SITE 5 BC6 32 LEU D 163 GLU D 165 SER D 275 CYS D 276
SITE 6 BC6 32 LYS D 279 ARG D 346 UGA D 501 HOH D4055
SITE 7 BC6 32 HOH D4069 HOH D4084 HOH D4086 HOH D4109
SITE 8 BC6 32 HOH D4114 HOH D4131 HOH D4182 HOH D4352
SITE 1 BC7 30 ARG C 260 GLU D 161 PHE D 162 LEU D 163
SITE 2 BC7 30 ALA D 164 GLU D 165 LYS D 220 ASN D 224
SITE 3 BC7 30 ILE D 231 PHE D 265 LEU D 266 LYS D 267
SITE 4 BC7 30 SER D 269 PHE D 272 GLY D 273 CYS D 276
SITE 5 BC7 30 PHE D 277 PHE D 338 LYS D 339 ARG D 442
SITE 6 BC7 30 NAD D 500 HOH D4059 HOH D4082 HOH D4084
SITE 7 BC7 30 HOH D4098 HOH D4114 HOH D4136 HOH D4158
SITE 8 BC7 30 HOH D4159 HOH D4189
SITE 1 BC8 15 ILE E 10 GLY E 11 GLY E 13 TYR E 14
SITE 2 BC8 15 VAL E 15 ASP E 36 VAL E 37 ARG E 41
SITE 3 BC8 15 VAL E 89 ASN E 90 TYR E 108 HOH E 547
SITE 4 BC8 15 HOH E 655 HOH E 726 HOH E 741
SITE 1 BC9 28 GLU E 161 PHE E 162 LEU E 163 GLU E 165
SITE 2 BC9 28 LYS E 220 ASN E 224 ILE E 231 PHE E 265
SITE 3 BC9 28 LEU E 266 LYS E 267 SER E 269 PHE E 272
SITE 4 BC9 28 GLY E 273 CYS E 276 PHE E 277 PHE E 338
SITE 5 BC9 28 LYS E 339 ARG E 442 HOH E 502 HOH E 511
SITE 6 BC9 28 HOH E 532 HOH E 538 HOH E 543 HOH E 552
SITE 7 BC9 28 HOH E 631 HOH E 669 HOH E 725 ARG F 260
SITE 1 CC1 32 ILE F 10 GLY F 11 GLY F 13 TYR F 14
SITE 2 CC1 32 VAL F 15 ASP F 36 VAL F 37 ARG F 41
SITE 3 CC1 32 SER F 88 VAL F 89 ASN F 90 THR F 91
SITE 4 CC1 32 TYR F 108 SER F 130 THR F 131 GLU F 161
SITE 5 CC1 32 LEU F 163 GLU F 165 CYS F 276 LYS F 279
SITE 6 CC1 32 ARG F 346 UGA F 501 HOH F5006 HOH F5048
SITE 7 CC1 32 HOH F5081 HOH F5098 HOH F5108 HOH F5109
SITE 8 CC1 32 HOH F5173 HOH F5210 HOH F5222 HOH F5303
SITE 1 CC2 30 ARG E 260 GLU F 161 PHE F 162 LEU F 163
SITE 2 CC2 30 ALA F 164 GLU F 165 LYS F 220 ASN F 224
SITE 3 CC2 30 ILE F 231 PHE F 265 LEU F 266 LYS F 267
SITE 4 CC2 30 SER F 269 PHE F 272 GLY F 273 CYS F 276
SITE 5 CC2 30 PHE F 277 PHE F 338 LYS F 339 ARG F 442
SITE 6 CC2 30 NAD F 500 HOH F5009 HOH F5076 HOH F5081
SITE 7 CC2 30 HOH F5091 HOH F5108 HOH F5117 HOH F5133
SITE 8 CC2 30 HOH F5136 HOH F5197
SITE 1 CC3 15 ILE G 10 GLY G 11 GLY G 13 TYR G 14
SITE 2 CC3 15 VAL G 15 ASP G 36 VAL G 37 ARG G 41
SITE 3 CC3 15 ILE G 75 VAL G 89 ASN G 90 TYR G 108
SITE 4 CC3 15 HOH G5005 HOH G5162 HOH G5262
SITE 1 CC4 25 GLU G 161 PHE G 162 LEU G 163 GLU G 165
SITE 2 CC4 25 LYS G 220 ASN G 224 ILE G 231 PHE G 265
SITE 3 CC4 25 LYS G 267 SER G 269 PHE G 272 GLY G 273
SITE 4 CC4 25 CYS G 276 PHE G 277 PHE G 338 LYS G 339
SITE 5 CC4 25 ARG G 442 HOH G5006 HOH G5026 HOH G5037
SITE 6 CC4 25 HOH G5052 HOH G5067 HOH G5094 HOH G5129
SITE 7 CC4 25 ARG H 260
SITE 1 CC5 32 ILE H 10 GLY H 11 GLY H 13 TYR H 14
SITE 2 CC5 32 VAL H 15 ASP H 36 VAL H 37 ARG H 41
SITE 3 CC5 32 SER H 88 VAL H 89 ASN H 90 THR H 91
SITE 4 CC5 32 TYR H 108 ALA H 111 SER H 130 THR H 131
SITE 5 CC5 32 GLU H 161 LEU H 163 GLU H 165 CYS H 276
SITE 6 CC5 32 LYS H 279 ARG H 346 UGA H 501 HOH H4042
SITE 7 CC5 32 HOH H4045 HOH H4090 HOH H4092 HOH H4114
SITE 8 CC5 32 HOH H4116 HOH H4139 HOH H4197 HOH H4217
SITE 1 CC6 29 ARG G 260 GLU H 161 PHE H 162 LEU H 163
SITE 2 CC6 29 ALA H 164 GLU H 165 LYS H 220 ASN H 224
SITE 3 CC6 29 ILE H 231 PHE H 265 LEU H 266 LYS H 267
SITE 4 CC6 29 SER H 269 PHE H 272 GLY H 273 CYS H 276
SITE 5 CC6 29 PHE H 277 PHE H 338 LYS H 339 ARG H 442
SITE 6 CC6 29 NAD H 500 HOH H4011 HOH H4024 HOH H4041
SITE 7 CC6 29 HOH H4079 HOH H4092 HOH H4099 HOH H4109
SITE 8 CC6 29 HOH H4116
SITE 1 CC7 7 GLN A 229 TYR A 299 VAL A 303 GLN B 229
SITE 2 CC7 7 TYR B 299 GLN B 302 VAL B 303
SITE 1 CC8 6 GLN C 229 TYR C 299 VAL C 303 GLN D 229
SITE 2 CC8 6 TYR D 299 VAL D 303
SITE 1 CC9 5 GLN E 229 TYR E 299 GLN F 229 TYR F 299
SITE 2 CC9 5 VAL F 303
SITE 1 DC1 6 GLN G 229 TYR G 299 VAL G 303 GLN H 229
SITE 2 DC1 6 TYR H 299 VAL H 303
CRYST1 193.868 193.868 352.223 90.00 90.00 120.00 H 3 72
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 0.005158 0.002978 0.000000 0.00000
SCALE2 0.000000 0.005956 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002839 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
