HEADER LIGASE 30-MAR-12 4EG1
TITLE TRYPANOSOMA BRUCEI METHIONYL-TRNA SYNTHETASE IN COMPLEX WITH SUBSTRATE
TITLE 2 METHIONINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHIONYL-TRNA SYNTHETASE, PUTATIVE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 235-771;
COMPND 5 EC: 6.1.1.10;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI BRUCEI;
SOURCE 3 ORGANISM_TAXID: 999953;
SOURCE 4 STRAIN: 927/4 GUTAT10.1;
SOURCE 5 GENE: TB10.70.6470;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: AVA0421
KEYWDS AMINOACYL-TRNA SYNTHETASE, AARS, METRS, PARASITE, LIGASE, PROTEIN-
KEYWDS 2 INHIBITOR COMPLEX, ROSSMANN-FOLD, TRANSLATION, NUCLEOTIDE BINDING,
KEYWDS 3 ROSSMANN FOLD, TRNA BINDING ATP BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR C.Y.KOH,J.E.KIM,S.SHIBATA,E.FAN,C.L.M.J.VERLINDE,W.G.J.HOL
REVDAT 5 13-SEP-23 4EG1 1 REMARK SEQADV LINK
REVDAT 4 15-NOV-17 4EG1 1 REMARK
REVDAT 3 31-OCT-12 4EG1 1 JRNL
REVDAT 2 17-OCT-12 4EG1 1 REMARK
REVDAT 1 12-SEP-12 4EG1 0
JRNL AUTH C.Y.KOH,J.E.KIM,S.SHIBATA,R.M.RANADE,M.YU,J.LIU,
JRNL AUTH 2 J.R.GILLESPIE,F.S.BUCKNER,C.L.VERLINDE,E.FAN,W.G.HOL
JRNL TITL DISTINCT STATES OF METHIONYL-TRNA SYNTHETASE INDICATE
JRNL TITL 2 INHIBITOR BINDING BY CONFORMATIONAL SELECTION.
JRNL REF STRUCTURE V. 20 1681 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22902861
JRNL DOI 10.1016/J.STR.2012.07.011
REMARK 2
REMARK 2 RESOLUTION. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 39977
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2124
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2654
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.47
REMARK 3 BIN R VALUE (WORKING SET) : 0.3150
REMARK 3 BIN FREE R VALUE SET COUNT : 147
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8495
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 90
REMARK 3 SOLVENT ATOMS : 81
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.72000
REMARK 3 B22 (A**2) : -5.68000
REMARK 3 B33 (A**2) : -5.05000
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): 0.787
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.350
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.296
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.878
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8791 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 6025 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11923 ; 1.158 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14631 ; 0.821 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1059 ; 5.887 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 401 ;38.014 ;23.516
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1453 ;15.719 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;16.250 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1318 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9655 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1847 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 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 239 A 537
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1558 -15.1574 53.2555
REMARK 3 T TENSOR
REMARK 3 T11: 0.2286 T22: 0.1699
REMARK 3 T33: 0.1399 T12: 0.0517
REMARK 3 T13: 0.0778 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.8266 L22: 1.7503
REMARK 3 L33: 0.5796 L12: 0.4454
REMARK 3 L13: -0.5257 L23: -0.6842
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: 0.0120 S13: 0.0646
REMARK 3 S21: 0.2302 S22: 0.0274 S23: 0.0670
REMARK 3 S31: 0.0870 S32: 0.0789 S33: -0.0292
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 538 A 735
REMARK 3 ORIGIN FOR THE GROUP (A): -17.0570 3.6713 34.3791
REMARK 3 T TENSOR
REMARK 3 T11: 0.0950 T22: 0.3009
REMARK 3 T33: 0.2529 T12: -0.0115
REMARK 3 T13: -0.0228 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.6726 L22: 0.4709
REMARK 3 L33: 1.8348 L12: 0.4761
REMARK 3 L13: -0.7468 L23: -0.5327
REMARK 3 S TENSOR
REMARK 3 S11: 0.1042 S12: 0.0886 S13: -0.1088
REMARK 3 S21: 0.1655 S22: -0.0469 S23: -0.1370
REMARK 3 S31: -0.0487 S32: 0.3442 S33: -0.0574
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 736 A 767
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1297 13.0398 38.4131
REMARK 3 T TENSOR
REMARK 3 T11: 0.2643 T22: 0.1606
REMARK 3 T33: 0.1937 T12: -0.1207
REMARK 3 T13: 0.1563 T23: -0.0672
REMARK 3 L TENSOR
REMARK 3 L11: 0.2902 L22: 3.4869
REMARK 3 L33: 1.2017 L12: -0.9860
REMARK 3 L13: -0.1869 L23: 0.9746
REMARK 3 S TENSOR
REMARK 3 S11: -0.0032 S12: -0.0653 S13: 0.0304
REMARK 3 S21: 0.0348 S22: 0.2684 S23: -0.1628
REMARK 3 S31: -0.2387 S32: 0.2011 S33: -0.2652
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 : B -4 B 367
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9645 14.6009 -11.7335
REMARK 3 T TENSOR
REMARK 3 T11: 0.1287 T22: 0.2416
REMARK 3 T33: 0.1904 T12: -0.0275
REMARK 3 T13: 0.0279 T23: 0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 0.9240 L22: 0.8565
REMARK 3 L33: 1.6326 L12: 0.3238
REMARK 3 L13: -0.7183 L23: -0.0521
REMARK 3 S TENSOR
REMARK 3 S11: -0.0782 S12: 0.0943 S13: -0.0711
REMARK 3 S21: -0.3090 S22: 0.1129 S23: 0.0535
REMARK 3 S31: -0.0301 S32: -0.0869 S33: -0.0347
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 368 B 395
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8228 12.9814 -6.9733
REMARK 3 T TENSOR
REMARK 3 T11: 0.1664 T22: 0.3662
REMARK 3 T33: 0.3181 T12: -0.1585
REMARK 3 T13: -0.0002 T23: 0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 4.6029 L22: 6.0595
REMARK 3 L33: 12.8758 L12: -5.1079
REMARK 3 L13: 3.6086 L23: -3.0637
REMARK 3 S TENSOR
REMARK 3 S11: 0.1438 S12: -0.3964 S13: -0.1292
REMARK 3 S21: 0.0619 S22: 0.1239 S23: 0.1053
REMARK 3 S31: 1.0243 S32: -0.1567 S33: -0.2677
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 396 B 533
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6832 23.6708 -6.7740
REMARK 3 T TENSOR
REMARK 3 T11: 0.0588 T22: 0.1473
REMARK 3 T33: 0.1599 T12: -0.0110
REMARK 3 T13: 0.0313 T23: 0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 1.9462 L22: 1.5650
REMARK 3 L33: 1.8723 L12: 0.8538
REMARK 3 L13: -0.4849 L23: -0.2242
REMARK 3 S TENSOR
REMARK 3 S11: -0.0430 S12: -0.0473 S13: 0.0624
REMARK 3 S21: -0.2369 S22: 0.1268 S23: -0.0453
REMARK 3 S31: -0.1395 S32: 0.1020 S33: -0.0838
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 534 B 730
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2389 -3.7461 9.2284
REMARK 3 T TENSOR
REMARK 3 T11: 0.0925 T22: 0.2337
REMARK 3 T33: 0.1732 T12: -0.0030
REMARK 3 T13: 0.0468 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.5078 L22: 0.9890
REMARK 3 L33: 1.6318 L12: 0.3848
REMARK 3 L13: -0.6423 L23: -0.8843
REMARK 3 S TENSOR
REMARK 3 S11: -0.1423 S12: -0.0792 S13: -0.0763
REMARK 3 S21: -0.1558 S22: 0.0125 S23: -0.1154
REMARK 3 S31: 0.3731 S32: 0.0056 S33: 0.1298
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 731 B 768
REMARK 3 ORIGIN FOR THE GROUP (A): -36.9665 -5.1744 5.1878
REMARK 3 T TENSOR
REMARK 3 T11: 0.1179 T22: 0.2825
REMARK 3 T33: 0.2391 T12: -0.0293
REMARK 3 T13: -0.0012 T23: 0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 3.6224 L22: 1.1784
REMARK 3 L33: 0.8550 L12: 0.7644
REMARK 3 L13: 0.0368 L23: -0.9206
REMARK 3 S TENSOR
REMARK 3 S11: -0.1164 S12: 0.1487 S13: -0.2436
REMARK 3 S21: -0.1716 S22: 0.3275 S23: 0.1732
REMARK 3 S31: 0.1121 S32: -0.2972 S33: -0.2111
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 4EG1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071571.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0 TO 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : VARIMAX HF (OSMIC)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42449
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.14400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.72600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: PDB ENTRY 3KFL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 TO 2.3M AMMONIUM SULFATE, 0.2M
REMARK 280 SODIUM CHLORIDE AND 0.1M SODIUM CACODYLATE PH 6.0 TO 6.6, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 42.51850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.59000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.96750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.59000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.51850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.96750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLY A -4
REMARK 465 PRO A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 MET A 0
REMARK 465 LYS A 237
REMARK 465 VAL A 238
REMARK 465 GLU A 768
REMARK 465 ASN A 769
REMARK 465 THR A 770
REMARK 465 LYS A 771
REMARK 465 SER A 772
REMARK 465 THR A 773
REMARK 465 LYS B 382
REMARK 465 ASP B 383
REMARK 465 GLY B 384
REMARK 465 ASN B 385
REMARK 465 ASN B 769
REMARK 465 THR B 770
REMARK 465 LYS B 771
REMARK 465 SER B 772
REMARK 465 THR B 773
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 553 CG CD CE NZ
REMARK 470 LYS A 554 CG CD CE NZ
REMARK 470 LYS A 557 CG 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 GLN A 301 47.00 72.52
REMARK 500 GLU A 368 51.65 39.06
REMARK 500 ASP A 381 157.75 -48.17
REMARK 500 ASP A 383 -127.18 -118.46
REMARK 500 TRP A 459 68.42 -109.43
REMARK 500 ASN A 466 87.56 -151.74
REMARK 500 SER A 497 138.54 -176.14
REMARK 500 ILE A 525 -60.44 -125.59
REMARK 500 ALA A 632 -156.87 -76.62
REMARK 500 ASP A 691 75.04 -155.10
REMARK 500 MET B 0 133.67 -36.46
REMARK 500 TRP B 459 59.32 -108.19
REMARK 500 ARG B 507 -61.21 -104.95
REMARK 500 ILE B 525 -63.16 -130.15
REMARK 500 ALA B 632 -166.07 -100.48
REMARK 500 ASP B 691 99.91 -161.42
REMARK 500 LEU B 717 62.85 -115.54
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 GOL A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MET A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MET B 806
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EG1 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH SUBSTRATE METHIONINE
REMARK 900 RELATED ID: 4EG3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH SUBSTRATE METHIONYL-ADENYLATE
REMARK 900 RELATED ID: 4EG4 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH INHIBITOR CHEM 1289
REMARK 900 RELATED ID: 4EG5 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH INHIBITOR CHEM 1312
REMARK 900 RELATED ID: 4EG6 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH INHIBITOR CHEM 1325
REMARK 900 RELATED ID: 4EG7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH INHIBITOR CHEM 1331
REMARK 900 RELATED ID: 4EG8 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH LOW MOLECULAR WEIGHT FRAGMENT 89
REMARK 900 RELATED ID: 4EGA RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH INHIBITOR CHEM 1320
DBREF 4EG1 A 237 773 UNP Q38C91 Q38C91_TRYB2 237 773
DBREF 4EG1 B 237 773 UNP Q38C91 Q38C91_TRYB2 237 773
SEQADV 4EG1 GLY A -4 UNP Q38C91 EXPRESSION TAG
SEQADV 4EG1 PRO A -3 UNP Q38C91 EXPRESSION TAG
SEQADV 4EG1 GLY A -2 UNP Q38C91 EXPRESSION TAG
SEQADV 4EG1 SER A -1 UNP Q38C91 EXPRESSION TAG
SEQADV 4EG1 MET A 0 UNP Q38C91 EXPRESSION TAG
SEQADV 4EG1 THR A 309 UNP Q38C91 ALA 309 CONFLICT
SEQADV 4EG1 ALA A 452 UNP Q38C91 LYS 452 ENGINEERED MUTATION
SEQADV 4EG1 ARG A 453 UNP Q38C91 LYS 453 ENGINEERED MUTATION
SEQADV 4EG1 ALA A 454 UNP Q38C91 GLU 454 ENGINEERED MUTATION
SEQADV 4EG1 VAL A 499 UNP Q38C91 ALA 499 CONFLICT
SEQADV 4EG1 ASN A 503 UNP Q38C91 SER 503 CONFLICT
SEQADV 4EG1 GLY B -4 UNP Q38C91 EXPRESSION TAG
SEQADV 4EG1 PRO B -3 UNP Q38C91 EXPRESSION TAG
SEQADV 4EG1 GLY B -2 UNP Q38C91 EXPRESSION TAG
SEQADV 4EG1 SER B -1 UNP Q38C91 EXPRESSION TAG
SEQADV 4EG1 MET B 0 UNP Q38C91 EXPRESSION TAG
SEQADV 4EG1 THR B 309 UNP Q38C91 ALA 309 CONFLICT
SEQADV 4EG1 ALA B 452 UNP Q38C91 LYS 452 ENGINEERED MUTATION
SEQADV 4EG1 ARG B 453 UNP Q38C91 LYS 453 ENGINEERED MUTATION
SEQADV 4EG1 ALA B 454 UNP Q38C91 GLU 454 ENGINEERED MUTATION
SEQADV 4EG1 VAL B 499 UNP Q38C91 ALA 499 CONFLICT
SEQADV 4EG1 ASN B 503 UNP Q38C91 SER 503 CONFLICT
SEQRES 1 A 542 GLY PRO GLY SER MET LYS VAL GLU LYS VAL PHE PHE VAL
SEQRES 2 A 542 THR SER PRO ILE TYR TYR VAL ASN ALA ALA PRO HIS ILE
SEQRES 3 A 542 GLY HIS VAL TYR SER THR LEU ILE THR ASP VAL ILE GLY
SEQRES 4 A 542 ARG TYR HIS ARG VAL LYS GLY GLU ARG VAL PHE ALA LEU
SEQRES 5 A 542 THR GLY THR ASP GLU HIS GLY GLN LYS VAL ALA GLU ALA
SEQRES 6 A 542 ALA LYS GLN LYS GLN VAL SER PRO TYR ASP PHE THR THR
SEQRES 7 A 542 ALA VAL ALA GLY GLU PHE LYS LYS CYS PHE GLU GLN MET
SEQRES 8 A 542 ASP TYR SER ILE ASP TYR PHE ILE ARG THR THR ASN GLU
SEQRES 9 A 542 GLN HIS LYS ALA VAL VAL LYS GLU LEU TRP THR LYS LEU
SEQRES 10 A 542 GLU GLN LYS GLY ASP ILE TYR LEU GLY ARG TYR GLU GLY
SEQRES 11 A 542 TRP TYR SER ILE SER ASP GLU SER PHE LEU THR PRO GLN
SEQRES 12 A 542 ASN ILE THR ASP GLY VAL ASP LYS ASP GLY ASN PRO CYS
SEQRES 13 A 542 LYS VAL SER LEU GLU SER GLY HIS VAL VAL THR TRP VAL
SEQRES 14 A 542 SER GLU GLU ASN TYR MET PHE ARG LEU SER ALA PHE ARG
SEQRES 15 A 542 GLU ARG LEU LEU GLU TRP TYR HIS ALA ASN PRO GLY CYS
SEQRES 16 A 542 ILE VAL PRO GLU PHE ARG ARG ARG GLU VAL ILE ARG ALA
SEQRES 17 A 542 VAL GLU LYS GLY LEU PRO ASP LEU SER VAL SER ARG ALA
SEQRES 18 A 542 ARG ALA THR LEU HIS ASN TRP ALA ILE PRO VAL PRO GLY
SEQRES 19 A 542 ASN PRO ASP HIS CAS VAL TYR VAL TRP LEU ASP ALA LEU
SEQRES 20 A 542 THR ASN TYR LEU THR GLY SER ARG LEU ARG VAL ASP GLU
SEQRES 21 A 542 SER GLY LYS GLU VAL SER LEU VAL ASP ASP PHE ASN GLU
SEQRES 22 A 542 LEU GLU ARG PHE PRO ALA ASP VAL HIS VAL ILE GLY LYS
SEQRES 23 A 542 ASP ILE LEU LYS PHE HIS ALA ILE TYR TRP PRO ALA PHE
SEQRES 24 A 542 LEU LEU SER ALA GLY LEU PRO LEU PRO LYS LYS ILE VAL
SEQRES 25 A 542 ALA HIS GLY TRP TRP THR LYS ASP ARG LYS LYS ILE SER
SEQRES 26 A 542 LYS SER LEU GLY ASN VAL PHE ASP PRO VAL GLU LYS ALA
SEQRES 27 A 542 GLU GLU PHE GLY TYR ASP ALA LEU LYS TYR PHE LEU LEU
SEQRES 28 A 542 ARG GLU SER GLY PHE SER ASP ASP GLY ASP TYR SER ASP
SEQRES 29 A 542 LYS ASN MET ILE ALA ARG LEU ASN GLY GLU LEU ALA ASP
SEQRES 30 A 542 THR LEU GLY ASN LEU VAL MET ARG CYS THR SER ALA LYS
SEQRES 31 A 542 ILE ASN VAL ASN GLY GLU TRP PRO SER PRO ALA ALA TYR
SEQRES 32 A 542 THR GLU GLU ASP GLU SER LEU ILE GLN LEU ILE LYS ASP
SEQRES 33 A 542 LEU PRO GLY THR ALA ASP HIS TYR TYR LEU ILE PRO ASP
SEQRES 34 A 542 ILE GLN LYS ALA ILE ILE ALA VAL PHE ASP VAL LEU ARG
SEQRES 35 A 542 ALA ILE ASN ALA TYR VAL THR ASP MET ALA PRO TRP LYS
SEQRES 36 A 542 LEU VAL LYS THR ASP PRO GLU ARG LEU ARG THR VAL LEU
SEQRES 37 A 542 TYR ILE THR LEU GLU GLY VAL ARG VAL THR THR LEU LEU
SEQRES 38 A 542 LEU SER PRO ILE LEU PRO ARG LYS SER VAL VAL ILE PHE
SEQRES 39 A 542 ASP MET LEU GLY VAL PRO GLU VAL HIS ARG LYS GLY ILE
SEQRES 40 A 542 GLU ASN PHE GLU PHE GLY ALA VAL PRO PRO GLY THR ARG
SEQRES 41 A 542 LEU GLY PRO ALA VAL GLU GLY GLU VAL LEU PHE SER LYS
SEQRES 42 A 542 ARG SER THR GLU ASN THR LYS SER THR
SEQRES 1 B 542 GLY PRO GLY SER MET LYS VAL GLU LYS VAL PHE PHE VAL
SEQRES 2 B 542 THR SER PRO ILE TYR TYR VAL ASN ALA ALA PRO HIS ILE
SEQRES 3 B 542 GLY HIS VAL TYR SER THR LEU ILE THR ASP VAL ILE GLY
SEQRES 4 B 542 ARG TYR HIS ARG VAL LYS GLY GLU ARG VAL PHE ALA LEU
SEQRES 5 B 542 THR GLY THR ASP GLU HIS GLY GLN LYS VAL ALA GLU ALA
SEQRES 6 B 542 ALA LYS GLN LYS GLN VAL SER PRO TYR ASP PHE THR THR
SEQRES 7 B 542 ALA VAL ALA GLY GLU PHE LYS LYS CYS PHE GLU GLN MET
SEQRES 8 B 542 ASP TYR SER ILE ASP TYR PHE ILE ARG THR THR ASN GLU
SEQRES 9 B 542 GLN HIS LYS ALA VAL VAL LYS GLU LEU TRP THR LYS LEU
SEQRES 10 B 542 GLU GLN LYS GLY ASP ILE TYR LEU GLY ARG TYR GLU GLY
SEQRES 11 B 542 TRP TYR SER ILE SER ASP GLU SER PHE LEU THR PRO GLN
SEQRES 12 B 542 ASN ILE THR ASP GLY VAL ASP LYS ASP GLY ASN PRO CYS
SEQRES 13 B 542 LYS VAL SER LEU GLU SER GLY HIS VAL VAL THR TRP VAL
SEQRES 14 B 542 SER GLU GLU ASN TYR MET PHE ARG LEU SER ALA PHE ARG
SEQRES 15 B 542 GLU ARG LEU LEU GLU TRP TYR HIS ALA ASN PRO GLY CYS
SEQRES 16 B 542 ILE VAL PRO GLU PHE ARG ARG ARG GLU VAL ILE ARG ALA
SEQRES 17 B 542 VAL GLU LYS GLY LEU PRO ASP LEU SER VAL SER ARG ALA
SEQRES 18 B 542 ARG ALA THR LEU HIS ASN TRP ALA ILE PRO VAL PRO GLY
SEQRES 19 B 542 ASN PRO ASP HIS CAS VAL TYR VAL TRP LEU ASP ALA LEU
SEQRES 20 B 542 THR ASN TYR LEU THR GLY SER ARG LEU ARG VAL ASP GLU
SEQRES 21 B 542 SER GLY LYS GLU VAL SER LEU VAL ASP ASP PHE ASN GLU
SEQRES 22 B 542 LEU GLU ARG PHE PRO ALA ASP VAL HIS VAL ILE GLY LYS
SEQRES 23 B 542 ASP ILE LEU LYS PHE HIS ALA ILE TYR TRP PRO ALA PHE
SEQRES 24 B 542 LEU LEU SER ALA GLY LEU PRO LEU PRO LYS LYS ILE VAL
SEQRES 25 B 542 ALA HIS GLY TRP TRP THR LYS ASP ARG LYS LYS ILE SER
SEQRES 26 B 542 LYS SER LEU GLY ASN VAL PHE ASP PRO VAL GLU LYS ALA
SEQRES 27 B 542 GLU GLU PHE GLY TYR ASP ALA LEU LYS TYR PHE LEU LEU
SEQRES 28 B 542 ARG GLU SER GLY PHE SER ASP ASP GLY ASP TYR SER ASP
SEQRES 29 B 542 LYS ASN MET ILE ALA ARG LEU ASN GLY GLU LEU ALA ASP
SEQRES 30 B 542 THR LEU GLY ASN LEU VAL MET ARG CYS THR SER ALA LYS
SEQRES 31 B 542 ILE ASN VAL ASN GLY GLU TRP PRO SER PRO ALA ALA TYR
SEQRES 32 B 542 THR GLU GLU ASP GLU SER LEU ILE GLN LEU ILE LYS ASP
SEQRES 33 B 542 LEU PRO GLY THR ALA ASP HIS TYR TYR LEU ILE PRO ASP
SEQRES 34 B 542 ILE GLN LYS ALA ILE ILE ALA VAL PHE ASP VAL LEU ARG
SEQRES 35 B 542 ALA ILE ASN ALA TYR VAL THR ASP MET ALA PRO TRP LYS
SEQRES 36 B 542 LEU VAL LYS THR ASP PRO GLU ARG LEU ARG THR VAL LEU
SEQRES 37 B 542 TYR ILE THR LEU GLU GLY VAL ARG VAL THR THR LEU LEU
SEQRES 38 B 542 LEU SER PRO ILE LEU PRO ARG LYS SER VAL VAL ILE PHE
SEQRES 39 B 542 ASP MET LEU GLY VAL PRO GLU VAL HIS ARG LYS GLY ILE
SEQRES 40 B 542 GLU ASN PHE GLU PHE GLY ALA VAL PRO PRO GLY THR ARG
SEQRES 41 B 542 LEU GLY PRO ALA VAL GLU GLY GLU VAL LEU PHE SER LYS
SEQRES 42 B 542 ARG SER THR GLU ASN THR LYS SER THR
MODRES 4EG1 CAS A 470 CYS S-(DIMETHYLARSENIC)CYSTEINE
MODRES 4EG1 CAS B 470 CYS S-(DIMETHYLARSENIC)CYSTEINE
HET CAS A 470 9
HET CAS B 470 9
HET GOL A 801 6
HET GOL A 802 6
HET GOL A 803 6
HET GOL A 804 6
HET GOL A 805 6
HET GOL A 806 6
HET GOL A 807 6
HET MET A 808 9
HET GOL B 801 6
HET GOL B 802 6
HET GOL B 803 6
HET GOL B 804 6
HET GOL B 805 6
HET MET B 806 9
HETNAM CAS S-(DIMETHYLARSENIC)CYSTEINE
HETNAM GOL GLYCEROL
HETNAM MET METHIONINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 CAS 2(C5 H12 AS N O2 S)
FORMUL 3 GOL 12(C3 H8 O3)
FORMUL 10 MET 2(C5 H11 N O2 S)
FORMUL 17 HOH *81(H2 O)
HELIX 1 1 HIS A 256 GLY A 277 1 22
HELIX 2 2 GLY A 290 GLN A 301 1 12
HELIX 3 3 SER A 303 MET A 322 1 20
HELIX 4 4 ASN A 334 LYS A 351 1 18
HELIX 5 5 THR A 372 GLN A 374 5 3
HELIX 6 6 LEU A 409 ALA A 411 5 3
HELIX 7 7 PHE A 412 ASN A 423 1 12
HELIX 8 8 PRO A 429 GLY A 443 1 15
HELIX 9 9 TYR A 472 THR A 479 1 8
HELIX 10 10 THR A 479 SER A 485 1 7
HELIX 11 11 ASP A 501 LEU A 505 5 5
HELIX 12 12 ILE A 519 ILE A 525 1 7
HELIX 13 13 ILE A 525 ALA A 534 1 10
HELIX 14 14 ASP A 564 GLY A 573 1 10
HELIX 15 15 GLY A 573 SER A 585 1 13
HELIX 16 16 SER A 594 GLU A 605 1 12
HELIX 17 17 THR A 609 CYS A 617 1 9
HELIX 18 18 THR A 635 ILE A 658 1 24
HELIX 19 19 ASP A 660 ALA A 683 1 24
HELIX 20 20 ALA A 683 ASP A 691 1 9
HELIX 21 21 ASP A 691 SER A 714 1 24
HELIX 22 22 LEU A 717 GLY A 729 1 13
HELIX 23 23 PRO A 731 LYS A 736 5 6
HELIX 24 24 GLY A 737 GLU A 742 5 6
HELIX 25 25 HIS B 256 GLY B 277 1 22
HELIX 26 26 GLY B 290 GLN B 301 1 12
HELIX 27 27 SER B 303 MET B 322 1 20
HELIX 28 28 ASN B 334 LYS B 351 1 18
HELIX 29 29 THR B 372 GLN B 374 5 3
HELIX 30 30 LEU B 409 ALA B 411 5 3
HELIX 31 31 PHE B 412 ASN B 423 1 12
HELIX 32 32 PRO B 429 GLY B 443 1 15
HELIX 33 33 ARG B 453 HIS B 457 1 5
HELIX 34 34 TYR B 472 ARG B 486 1 15
HELIX 35 35 ASP B 501 LEU B 505 5 5
HELIX 36 36 ILE B 519 ILE B 525 1 7
HELIX 37 37 ILE B 525 GLY B 535 1 11
HELIX 38 38 ASP B 564 GLY B 573 1 10
HELIX 39 39 GLY B 573 SER B 585 1 13
HELIX 40 40 SER B 594 GLU B 605 1 12
HELIX 41 41 THR B 609 SER B 619 1 11
HELIX 42 42 THR B 635 ILE B 658 1 24
HELIX 43 43 ASP B 660 ALA B 683 1 24
HELIX 44 44 ALA B 683 ASP B 691 1 9
HELIX 45 45 ASP B 691 SER B 714 1 24
HELIX 46 46 ARG B 719 GLY B 729 1 11
HELIX 47 47 PRO B 731 ARG B 735 5 5
HELIX 48 48 GLY B 737 PHE B 741 5 5
SHEET 1 A 3 TYR A 249 TYR A 250 0
SHEET 2 A 3 VAL A 280 ASP A 287 1 O ASP A 287 N TYR A 249
SHEET 3 A 3 TYR A 328 ARG A 331 1 O ILE A 330 N THR A 286
SHEET 1 B 6 TYR A 249 TYR A 250 0
SHEET 2 B 6 VAL A 280 ASP A 287 1 O ASP A 287 N TYR A 249
SHEET 3 B 6 PHE A 242 THR A 245 1 N VAL A 244 O PHE A 281
SHEET 4 B 6 VAL A 512 GLY A 516 1 O VAL A 514 N THR A 245
SHEET 5 B 6 ILE A 542 HIS A 545 1 O VAL A 543 N ILE A 515
SHEET 6 B 6 ILE A 427 VAL A 428 1 N VAL A 428 O ILE A 542
SHEET 1 C 3 ILE A 354 LEU A 356 0
SHEET 2 C 3 TYR A 405 PHE A 407 -1 O MET A 406 N TYR A 355
SHEET 3 C 3 LEU A 447 SER A 448 -1 O LEU A 447 N PHE A 407
SHEET 1 D 3 SER A 369 LEU A 371 0
SHEET 2 D 3 TYR A 359 SER A 364 -1 N SER A 364 O SER A 369
SHEET 3 D 3 VAL A 397 GLU A 402 -1 O VAL A 400 N GLY A 361
SHEET 1 E 2 ILE A 376 VAL A 380 0
SHEET 2 E 2 PRO A 386 SER A 390 -1 O VAL A 389 N THR A 377
SHEET 1 F 3 SER A 450 ALA A 452 0
SHEET 2 F 3 ASN A 466 VAL A 471 -1 O CAS A 470 N ARG A 451
SHEET 3 F 3 PRO A 462 VAL A 463 -1 N VAL A 463 O ASN A 466
SHEET 1 G 2 LEU A 487 VAL A 489 0
SHEET 2 G 2 GLU A 495 LEU A 498 -1 O VAL A 496 N ARG A 488
SHEET 1 H 3 LYS A 553 LYS A 554 0
SHEET 2 H 3 THR A 549 LYS A 550 -1 N LYS A 550 O LYS A 553
SHEET 3 H 3 ASP A 592 TYR A 593 1 O TYR A 593 N THR A 549
SHEET 1 I 3 TYR B 249 TYR B 250 0
SHEET 2 I 3 ARG B 279 ASP B 287 1 O GLY B 285 N TYR B 249
SHEET 3 I 3 TYR B 328 ARG B 331 1 O ILE B 330 N THR B 284
SHEET 1 J 6 TYR B 249 TYR B 250 0
SHEET 2 J 6 ARG B 279 ASP B 287 1 O GLY B 285 N TYR B 249
SHEET 3 J 6 VAL B 241 THR B 245 1 N PHE B 242 O PHE B 281
SHEET 4 J 6 VAL B 512 GLY B 516 1 O VAL B 514 N THR B 245
SHEET 5 J 6 LYS B 541 HIS B 545 1 O LYS B 541 N HIS B 513
SHEET 6 J 6 ILE B 427 VAL B 428 1 N VAL B 428 O ALA B 544
SHEET 1 K 4 SER B 369 LEU B 371 0
SHEET 2 K 4 ILE B 354 SER B 364 -1 N SER B 364 O SER B 369
SHEET 3 K 4 THR B 398 PHE B 407 -1 O MET B 406 N TYR B 355
SHEET 4 K 4 LEU B 447 SER B 448 -1 O LEU B 447 N PHE B 407
SHEET 1 L 2 ILE B 376 GLY B 379 0
SHEET 2 L 2 CYS B 387 SER B 390 -1 O VAL B 389 N THR B 377
SHEET 1 M 3 SER B 450 ALA B 452 0
SHEET 2 M 3 ASN B 466 VAL B 471 -1 O CAS B 470 N ARG B 451
SHEET 3 M 3 PRO B 462 VAL B 463 -1 N VAL B 463 O ASN B 466
SHEET 1 N 2 LEU B 487 VAL B 489 0
SHEET 2 N 2 GLU B 495 LEU B 498 -1 O SER B 497 N ARG B 488
SHEET 1 O 2 THR B 549 LYS B 550 0
SHEET 2 O 2 ASP B 592 TYR B 593 1 O TYR B 593 N THR B 549
LINK C HIS A 469 N CAS A 470 1555 1555 1.33
LINK C CAS A 470 N VAL A 471 1555 1555 1.34
LINK C HIS B 469 N CAS B 470 1555 1555 1.33
LINK C CAS B 470 N VAL B 471 1555 1555 1.33
CISPEP 1 VAL A 428 PRO A 429 0 -11.18
CISPEP 2 PHE A 508 PRO A 509 0 -4.07
CISPEP 3 ILE A 658 PRO A 659 0 -4.61
CISPEP 4 VAL B 428 PRO B 429 0 -6.34
CISPEP 5 PHE B 508 PRO B 509 0 -0.54
CISPEP 6 ILE B 658 PRO B 659 0 -0.89
SITE 1 AC1 5 ARG A 271 VAL A 275 SER A 714 PRO A 718
SITE 2 AC1 5 VAL A 722
SITE 1 AC2 1 ARG A 719
SITE 1 AC3 2 ARG A 583 ARG A 601
SITE 1 AC4 3 HIS A 395 VAL A 396 HOH A1017
SITE 1 AC5 2 LYS A 276 ILE A 738
SITE 1 AC6 1 GLU A 732
SITE 1 AC7 7 HIS A 289 LYS A 338 ASN A 458 TRP A 459
SITE 2 AC7 7 ALA A 460 CAS A 470 ASN B 458
SITE 1 AC8 10 ILE A 248 TYR A 249 TYR A 250 ASP A 287
SITE 2 AC8 10 TRP A 474 ALA A 477 ASN A 480 TYR A 481
SITE 3 AC8 10 ILE A 519 HIS A 523
SITE 1 AC9 2 ASP B 500 PHE B 502
SITE 1 BC1 2 ARG B 583 ARG B 601
SITE 1 BC2 7 TYR B 579 ARG B 583 GLU B 605 ILE B 665
SITE 2 BC2 7 ILE B 666 PHE B 669 ARG B 673
SITE 1 BC3 1 HOH B1035
SITE 1 BC4 5 HIS B 289 THR B 333 LYS B 338 TRP B 459
SITE 2 BC4 5 ALA B 460
SITE 1 BC5 9 ILE B 248 TYR B 250 ASP B 287 TRP B 474
SITE 2 BC5 9 ALA B 477 LEU B 478 TYR B 481 ILE B 519
SITE 3 BC5 9 HIS B 523
CRYST1 85.037 105.935 207.180 90.00 90.00 90.00 P 21 21 21 8
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 0.011760 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004827 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
