HEADER LIGASE 17-APR-15 4ZDK
TITLE CRYSTAL STRUCTURE OF THE M. TUBERCULOSIS CTP SYNTHASE PYRG IN COMPLEX
TITLE 2 WITH UTP, AMP-PCP AND OXONORLEUCINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CTP SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CTP SYNTHETASE,UTP--AMMONIA LIGASE;
COMPND 5 EC: 6.3.4.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 GENE: PYRG, RV1699, MTCI125.21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS CTP SYNTHASE, PYRG, AMIDOTRANSFERASE, UTP, AMP-PCP, 5-OXO-L-
KEYWDS 2 NORLEUCINE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BELLINZONI,N.BARILONE,P.M.ALZARI
REVDAT 3 10-JAN-24 4ZDK 1 LINK
REVDAT 2 05-AUG-15 4ZDK 1 JRNL
REVDAT 1 01-JUL-15 4ZDK 0
JRNL AUTH G.MORI,L.R.CHIARELLI,M.ESPOSITO,V.MAKAROV,M.BELLINZONI,
JRNL AUTH 2 R.C.HARTKOORN,G.DEGIACOMI,F.BOLDRIN,S.EKINS,
JRNL AUTH 3 A.L.DE JESUS LOPES RIBEIRO,L.B.MARINO,I.CENTAROVA,
JRNL AUTH 4 Z.SVETLIKOVA,J.BLASKO,E.KAZAKOVA,A.LEPIOSHKIN,N.BARILONE,
JRNL AUTH 5 G.ZANONI,A.PORTA,M.FONDI,R.FANI,A.R.BAULARD,K.MIKUSOVA,
JRNL AUTH 6 P.M.ALZARI,R.MANGANELLI,L.P.DE CARVALHO,G.RICCARDI,S.T.COLE,
JRNL AUTH 7 M.R.PASCA
JRNL TITL THIOPHENECARBOXAMIDE DERIVATIVES ACTIVATED BY ETHA KILL
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS BY INHIBITING THE CTP SYNTHETASE
JRNL TITL 3 PYRG.
JRNL REF CHEM.BIOL. V. 22 917 2015
JRNL REFN ISSN 1074-5521
JRNL PMID 26097035
JRNL DOI 10.1016/J.CHEMBIOL.2015.05.016
REMARK 2
REMARK 2 RESOLUTION. 3.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 31682
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1598
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 16
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.49
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.60
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.86
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2879
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2522
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2740
REMARK 3 BIN R VALUE (WORKING SET) : 0.2497
REMARK 3 BIN FREE R VALUE : 0.3039
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.83
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 139
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7844
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 142
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 124.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 143.2
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 16.75460
REMARK 3 B22 (A**2) : 12.73560
REMARK 3 B33 (A**2) : -29.49020
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.968
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 2.937
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.364
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8161 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 11169 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3623 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 168 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1280 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8161 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1102 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 9294 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.13
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.48
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|7 - A|278 X|1 X|3 X|5 }
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3374 -40.6874 -21.1395
REMARK 3 T TENSOR
REMARK 3 T11: -0.1254 T22: -0.1475
REMARK 3 T33: 0.0993 T12: -0.1609
REMARK 3 T13: 0.0104 T23: 0.2625
REMARK 3 L TENSOR
REMARK 3 L11: 2.3691 L22: 2.3903
REMARK 3 L33: 2.0906 L12: 0.2430
REMARK 3 L13: 0.2337 L23: 0.1173
REMARK 3 S TENSOR
REMARK 3 S11: -0.4307 S12: -0.2351 S13: -0.3053
REMARK 3 S21: -0.1983 S22: -0.0380 S23: -0.2549
REMARK 3 S31: 0.1867 S32: 0.1577 S33: 0.4688
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|279 - A|298 }
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7802 -25.2887 -20.8782
REMARK 3 T TENSOR
REMARK 3 T11: 0.0860 T22: -0.0489
REMARK 3 T33: 0.1584 T12: -0.2470
REMARK 3 T13: -0.1338 T23: 0.3040
REMARK 3 L TENSOR
REMARK 3 L11: 4.8546 L22: 0.8666
REMARK 3 L33: 0.9013 L12: 1.1190
REMARK 3 L13: 0.8303 L23: -2.0025
REMARK 3 S TENSOR
REMARK 3 S11: -0.0517 S12: -0.0840 S13: 0.0035
REMARK 3 S21: -0.0345 S22: -0.0172 S23: -0.0635
REMARK 3 S31: 0.0651 S32: 0.2871 S33: 0.0689
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|299 - A|601 }
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6467 -15.4654 -45.2655
REMARK 3 T TENSOR
REMARK 3 T11: -0.0720 T22: -0.1581
REMARK 3 T33: 0.0113 T12: -0.1003
REMARK 3 T13: -0.0048 T23: 0.1188
REMARK 3 L TENSOR
REMARK 3 L11: 2.4058 L22: 4.2179
REMARK 3 L33: 3.1225 L12: -0.5945
REMARK 3 L13: 0.3950 L23: -1.0459
REMARK 3 S TENSOR
REMARK 3 S11: 0.1114 S12: 0.0156 S13: -0.1539
REMARK 3 S21: -0.2951 S22: -0.1921 S23: -0.0575
REMARK 3 S31: 0.0153 S32: -0.2218 S33: 0.0807
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { B|7 - B|278 X|2 X|4 X|6 }
REMARK 3 ORIGIN FOR THE GROUP (A): 69.7192 -33.0392 -6.6504
REMARK 3 T TENSOR
REMARK 3 T11: -0.5140 T22: 0.3059
REMARK 3 T33: 0.0760 T12: -0.0288
REMARK 3 T13: -0.2135 T23: 0.2142
REMARK 3 L TENSOR
REMARK 3 L11: 2.5093 L22: 3.4313
REMARK 3 L33: 2.4727 L12: -0.7350
REMARK 3 L13: -0.3607 L23: 0.0648
REMARK 3 S TENSOR
REMARK 3 S11: -0.0533 S12: 0.2855 S13: 0.5905
REMARK 3 S21: 0.0239 S22: -0.2494 S23: -0.7796
REMARK 3 S31: -0.2192 S32: 0.9053 S33: 0.3028
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { B|279 - B|298 }
REMARK 3 ORIGIN FOR THE GROUP (A): 76.7804 -9.6511 -6.3077
REMARK 3 T TENSOR
REMARK 3 T11: -0.2096 T22: 0.1071
REMARK 3 T33: 0.2413 T12: -0.2950
REMARK 3 T13: -0.2755 T23: 0.1732
REMARK 3 L TENSOR
REMARK 3 L11: 2.4149 L22: 2.7110
REMARK 3 L33: 0.0000 L12: 3.9433
REMARK 3 L13: 0.0700 L23: -0.0171
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: 0.0045 S13: 0.0365
REMARK 3 S21: -0.0236 S22: 0.0236 S23: -0.0386
REMARK 3 S31: -0.0348 S32: 0.1119 S33: -0.0188
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { B|299 - B|601 }
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1582 -11.1595 -30.6806
REMARK 3 T TENSOR
REMARK 3 T11: -0.3313 T22: -0.0341
REMARK 3 T33: 0.0730 T12: -0.1855
REMARK 3 T13: -0.0791 T23: 0.3040
REMARK 3 L TENSOR
REMARK 3 L11: 3.5700 L22: 4.5855
REMARK 3 L33: 3.7350 L12: -1.5910
REMARK 3 L13: 0.9695 L23: -2.0178
REMARK 3 S TENSOR
REMARK 3 S11: 0.1348 S12: 0.5310 S13: 0.5729
REMARK 3 S21: -0.5517 S22: -0.3389 S23: -0.1518
REMARK 3 S31: -0.3938 S32: 0.4887 S33: 0.2040
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4ZDK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209074.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9150
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31727
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.490
REMARK 200 RESOLUTION RANGE LOW (A) : 48.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.60
REMARK 200 R MERGE FOR SHELL (I) : 1.12800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 4ZDJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG2000 MME, 100 MM BICINE PH 9.0,
REMARK 280 100 MM NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-Z+1/2
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 60.86600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.72850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 97.36200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.72850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.86600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 97.36200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 60.86600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 97.36200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 103.72850
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 97.36200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 60.86600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 103.72850
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: TETRAMERIC
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 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 60.86600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -97.36200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 121.73200
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 -97.36200
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 60.86600
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 72120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -97.36200
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 -60.86600
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 -97.36200
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 60.86600
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 LYS A 3
REMARK 465 HIS A 4
REMARK 465 PRO A 5
REMARK 465 GLN A 6
REMARK 465 PRO A 430
REMARK 465 ASP A 431
REMARK 465 GLN A 432
REMARK 465 GLU A 433
REMARK 465 GLU A 434
REMARK 465 ILE A 435
REMARK 465 VAL A 436
REMARK 465 ALA A 437
REMARK 465 GLY A 438
REMARK 465 GLU A 439
REMARK 465 ALA A 440
REMARK 465 ASP A 441
REMARK 465 LEU A 442
REMARK 465 LEU A 554
REMARK 465 PRO A 555
REMARK 465 VAL A 556
REMARK 465 GLU A 557
REMARK 465 ILE A 558
REMARK 465 PRO A 559
REMARK 465 GLU A 560
REMARK 465 ILE A 561
REMARK 465 PRO A 562
REMARK 465 GLU A 563
REMARK 465 HIS A 564
REMARK 465 THR A 565
REMARK 465 PRO A 566
REMARK 465 ASN A 567
REMARK 465 GLY A 568
REMARK 465 SER A 569
REMARK 465 SER A 570
REMARK 465 HIS A 571
REMARK 465 ARG A 572
REMARK 465 ASP A 573
REMARK 465 GLY A 574
REMARK 465 VAL A 575
REMARK 465 GLY A 576
REMARK 465 GLN A 577
REMARK 465 PRO A 578
REMARK 465 LEU A 579
REMARK 465 PRO A 580
REMARK 465 GLU A 581
REMARK 465 PRO A 582
REMARK 465 ALA A 583
REMARK 465 SER A 584
REMARK 465 ARG A 585
REMARK 465 GLY A 586
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 LYS B 3
REMARK 465 HIS B 4
REMARK 465 PRO B 5
REMARK 465 GLN B 6
REMARK 465 PRO B 430
REMARK 465 ASP B 431
REMARK 465 GLN B 432
REMARK 465 GLU B 433
REMARK 465 GLU B 434
REMARK 465 ILE B 435
REMARK 465 VAL B 436
REMARK 465 ALA B 437
REMARK 465 GLY B 438
REMARK 465 GLU B 439
REMARK 465 ALA B 440
REMARK 465 ASP B 441
REMARK 465 LEU B 442
REMARK 465 LEU B 554
REMARK 465 PRO B 555
REMARK 465 VAL B 556
REMARK 465 GLU B 557
REMARK 465 ILE B 558
REMARK 465 PRO B 559
REMARK 465 GLU B 560
REMARK 465 ILE B 561
REMARK 465 PRO B 562
REMARK 465 GLU B 563
REMARK 465 HIS B 564
REMARK 465 THR B 565
REMARK 465 PRO B 566
REMARK 465 ASN B 567
REMARK 465 GLY B 568
REMARK 465 SER B 569
REMARK 465 SER B 570
REMARK 465 HIS B 571
REMARK 465 ARG B 572
REMARK 465 ASP B 573
REMARK 465 GLY B 574
REMARK 465 VAL B 575
REMARK 465 GLY B 576
REMARK 465 GLN B 577
REMARK 465 PRO B 578
REMARK 465 LEU B 579
REMARK 465 PRO B 580
REMARK 465 GLU B 581
REMARK 465 PRO B 582
REMARK 465 ALA B 583
REMARK 465 SER B 584
REMARK 465 ARG B 585
REMARK 465 GLY B 586
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 SER A 93 OG
REMARK 470 GLN A 138 CG CD OE1 NE2
REMARK 470 ASP A 142 CG OD1 OD2
REMARK 470 ARG A 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 LEU A 192 CG CD1 CD2
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 LYS A 199 CG CD CE NZ
REMARK 470 LEU A 232 CG CD1 CD2
REMARK 470 LYS A 235 CG CD CE NZ
REMARK 470 LEU A 238 CG CD1 CD2
REMARK 470 MET A 239 CG SD CE
REMARK 470 ARG A 274 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 281 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 309 CG CD CE NZ
REMARK 470 TYR A 310 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 311 CG1 CG2
REMARK 470 GLU A 312 CG CD OE1 OE2
REMARK 470 LEU A 313 CG CD1 CD2
REMARK 470 GLU A 336 CG CD OE1 OE2
REMARK 470 ASP A 357 CG OD1 OD2
REMARK 470 ILE A 369 CG1 CG2 CD1
REMARK 470 ARG A 370 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 409 CG CD1 CD2
REMARK 470 THR A 410 OG1 CG2
REMARK 470 ASN A 411 CG OD1 ND2
REMARK 470 MET A 429 CG SD CE
REMARK 470 THR A 468 OG1 CG2
REMARK 470 ARG A 485 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 487 CG CD CE NZ
REMARK 470 ARG A 494 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 553 CG CD1 CD2
REMARK 470 LEU B 31 CG CD1 CD2
REMARK 470 LEU B 35 CG CD1 CD2
REMARK 470 LEU B 40 CG CD1 CD2
REMARK 470 THR B 43 OG1 CG2
REMARK 470 SER B 93 OG
REMARK 470 TYR B 102 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 138 CG CD OE1 NE2
REMARK 470 ASP B 142 CG OD1 OD2
REMARK 470 ARG B 178 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 179 CG CD OE1 OE2
REMARK 470 LEU B 192 CG CD1 CD2
REMARK 470 LEU B 198 CG CD1 CD2
REMARK 470 LYS B 199 CG CD CE NZ
REMARK 470 LEU B 232 CG CD1 CD2
REMARK 470 LYS B 235 CG CD CE NZ
REMARK 470 ILE B 236 CG1 CG2 CD1
REMARK 470 MET B 239 CG SD CE
REMARK 470 LYS B 261 CG CD CE NZ
REMARK 470 ARG B 265 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 266 CG CD OE1 OE2
REMARK 470 ARG B 274 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 281 CG CD NE CZ NH1 NH2
REMARK 470 TRP B 288 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 288 CZ3 CH2
REMARK 470 ASP B 357 CG OD1 OD2
REMARK 470 ILE B 369 CG1 CG2 CD1
REMARK 470 ARG B 370 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 375 CG CD CE NZ
REMARK 470 LEU B 396 CG CD1 CD2
REMARK 470 VAL B 400 CG1 CG2
REMARK 470 LEU B 409 CG CD1 CD2
REMARK 470 THR B 410 OG1 CG2
REMARK 470 ASN B 411 CG OD1 ND2
REMARK 470 VAL B 425 CG1 CG2
REMARK 470 MET B 429 CG SD CE
REMARK 470 ARG B 447 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 455 CG CD1 CD2
REMARK 470 GLU B 456 CG CD OE1 OE2
REMARK 470 ASP B 458 CG OD1 OD2
REMARK 470 VAL B 461 CG1 CG2
REMARK 470 GLN B 463 CG CD OE1 NE2
REMARK 470 GLN B 466 CG CD OE1 NE2
REMARK 470 THR B 468 OG1 CG2
REMARK 470 GLN B 469 CG CD OE1 NE2
REMARK 470 GLU B 479 CG CD OE1 OE2
REMARK 470 VAL B 480 CG1 CG2
REMARK 470 ARG B 485 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 487 CG CD CE NZ
REMARK 470 GLU B 490 CG CD OE1 OE2
REMARK 470 LEU B 493 CG CD1 CD2
REMARK 470 ARG B 494 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 495 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS B 503 CG ND1 CD2 CE1 NE2
REMARK 470 LEU B 504 CG CD1 CD2
REMARK 470 PHE B 507 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 509 CG CD OE1 OE2
REMARK 470 LEU B 553 CG CD1 CD2
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 VAL A 18 -63.01 73.33
REMARK 500 LEU A 313 17.96 96.33
REMARK 500 CYS A 393 -93.43 56.22
REMARK 500 ARG A 475 73.86 -158.50
REMARK 500 HIS A 524 79.17 -117.94
REMARK 500 VAL B 18 -62.33 73.01
REMARK 500 CYS B 393 -92.03 56.42
REMARK 500 ARG B 475 73.32 -157.54
REMARK 500 HIS B 524 78.88 -118.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 604 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 78 OD1
REMARK 620 2 ASP A 78 OD2 51.2
REMARK 620 3 GLU A 152 OE1 107.5 86.7
REMARK 620 4 GLU A 152 OE2 151.1 108.9 45.3
REMARK 620 5 ACP A 602 O3G 106.8 76.0 116.8 84.0
REMARK 620 6 ACP A 602 O1B 143.6 145.6 105.8 65.1 69.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 604 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 78 OD2
REMARK 620 2 GLU B 152 OE2 100.3
REMARK 620 3 ACP B 602 O1B 134.5 67.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ONL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACP A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UTP A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACP B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UTP B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ONL B 601 and CYS B
REMARK 800 393
DBREF 4ZDK A 1 586 UNP P9WHK7 PYRG_MYCTU 1 586
DBREF 4ZDK B 1 586 UNP P9WHK7 PYRG_MYCTU 1 586
SEQRES 1 A 586 MET ARG LYS HIS PRO GLN THR ALA THR LYS HIS LEU PHE
SEQRES 2 A 586 VAL SER GLY GLY VAL ALA SER SER LEU GLY LYS GLY LEU
SEQRES 3 A 586 THR ALA SER SER LEU GLY GLN LEU LEU THR ALA ARG GLY
SEQRES 4 A 586 LEU HIS VAL THR MET GLN LYS LEU ASP PRO TYR LEU ASN
SEQRES 5 A 586 VAL ASP PRO GLY THR MET ASN PRO PHE GLN HIS GLY GLU
SEQRES 6 A 586 VAL PHE VAL THR GLU ASP GLY ALA GLU THR ASP LEU ASP
SEQRES 7 A 586 VAL GLY HIS TYR GLU ARG PHE LEU ASP ARG ASN LEU PRO
SEQRES 8 A 586 GLY SER ALA ASN VAL THR THR GLY GLN VAL TYR SER THR
SEQRES 9 A 586 VAL ILE ALA LYS GLU ARG ARG GLY GLU TYR LEU GLY ASP
SEQRES 10 A 586 THR VAL GLN VAL ILE PRO HIS ILE THR ASP GLU ILE LYS
SEQRES 11 A 586 ARG ARG ILE LEU ALA MET ALA GLN PRO ASP ALA ASP GLY
SEQRES 12 A 586 ASN ARG PRO ASP VAL VAL ILE THR GLU ILE GLY GLY THR
SEQRES 13 A 586 VAL GLY ASP ILE GLU SER GLN PRO PHE LEU GLU ALA ALA
SEQRES 14 A 586 ARG GLN VAL ARG HIS TYR LEU GLY ARG GLU ASP VAL PHE
SEQRES 15 A 586 PHE LEU HIS VAL SER LEU VAL PRO TYR LEU ALA PRO SER
SEQRES 16 A 586 GLY GLU LEU LYS THR LYS PRO THR GLN HIS SER VAL ALA
SEQRES 17 A 586 ALA LEU ARG SER ILE GLY ILE THR PRO ASP ALA LEU ILE
SEQRES 18 A 586 LEU ARG CYS ASP ARG ASP VAL PRO GLU ALA LEU LYS ASN
SEQRES 19 A 586 LYS ILE ALA LEU MET CYS ASP VAL ASP ILE ASP GLY VAL
SEQRES 20 A 586 ILE SER THR PRO ASP ALA PRO SER ILE TYR ASP ILE PRO
SEQRES 21 A 586 LYS VAL LEU HIS ARG GLU GLU LEU ASP ALA PHE VAL VAL
SEQRES 22 A 586 ARG ARG LEU ASN LEU PRO PHE ARG ASP VAL ASP TRP THR
SEQRES 23 A 586 GLU TRP ASP ASP LEU LEU ARG ARG VAL HIS GLU PRO HIS
SEQRES 24 A 586 GLU THR VAL ARG ILE ALA LEU VAL GLY LYS TYR VAL GLU
SEQRES 25 A 586 LEU SER ASP ALA TYR LEU SER VAL ALA GLU ALA LEU ARG
SEQRES 26 A 586 ALA GLY GLY PHE LYS HIS ARG ALA LYS VAL GLU ILE CYS
SEQRES 27 A 586 TRP VAL ALA SER ASP GLY CYS GLU THR THR SER GLY ALA
SEQRES 28 A 586 ALA ALA ALA LEU GLY ASP VAL HIS GLY VAL LEU ILE PRO
SEQRES 29 A 586 GLY GLY PHE GLY ILE ARG GLY ILE GLU GLY LYS ILE GLY
SEQRES 30 A 586 ALA ILE ALA TYR ALA ARG ALA ARG GLY LEU PRO VAL LEU
SEQRES 31 A 586 GLY LEU CYS LEU GLY LEU GLN CYS ILE VAL ILE GLU ALA
SEQRES 32 A 586 ALA ARG SER VAL GLY LEU THR ASN ALA ASN SER ALA GLU
SEQRES 33 A 586 PHE ASP PRO ASP THR PRO ASP PRO VAL ILE ALA THR MET
SEQRES 34 A 586 PRO ASP GLN GLU GLU ILE VAL ALA GLY GLU ALA ASP LEU
SEQRES 35 A 586 GLY GLY THR MET ARG LEU GLY SER TYR PRO ALA VAL LEU
SEQRES 36 A 586 GLU PRO ASP SER VAL VAL ALA GLN ALA TYR GLN THR THR
SEQRES 37 A 586 GLN VAL SER GLU ARG HIS ARG HIS ARG TYR GLU VAL ASN
SEQRES 38 A 586 ASN ALA TYR ARG ASP LYS ILE ALA GLU SER GLY LEU ARG
SEQRES 39 A 586 PHE SER GLY THR SER PRO ASP GLY HIS LEU VAL GLU PHE
SEQRES 40 A 586 VAL GLU TYR PRO PRO ASP ARG HIS PRO PHE VAL VAL GLY
SEQRES 41 A 586 THR GLN ALA HIS PRO GLU LEU LYS SER ARG PRO THR ARG
SEQRES 42 A 586 PRO HIS PRO LEU PHE VAL ALA PHE VAL GLY ALA ALA ILE
SEQRES 43 A 586 ASP TYR LYS ALA GLY GLU LEU LEU PRO VAL GLU ILE PRO
SEQRES 44 A 586 GLU ILE PRO GLU HIS THR PRO ASN GLY SER SER HIS ARG
SEQRES 45 A 586 ASP GLY VAL GLY GLN PRO LEU PRO GLU PRO ALA SER ARG
SEQRES 46 A 586 GLY
SEQRES 1 B 586 MET ARG LYS HIS PRO GLN THR ALA THR LYS HIS LEU PHE
SEQRES 2 B 586 VAL SER GLY GLY VAL ALA SER SER LEU GLY LYS GLY LEU
SEQRES 3 B 586 THR ALA SER SER LEU GLY GLN LEU LEU THR ALA ARG GLY
SEQRES 4 B 586 LEU HIS VAL THR MET GLN LYS LEU ASP PRO TYR LEU ASN
SEQRES 5 B 586 VAL ASP PRO GLY THR MET ASN PRO PHE GLN HIS GLY GLU
SEQRES 6 B 586 VAL PHE VAL THR GLU ASP GLY ALA GLU THR ASP LEU ASP
SEQRES 7 B 586 VAL GLY HIS TYR GLU ARG PHE LEU ASP ARG ASN LEU PRO
SEQRES 8 B 586 GLY SER ALA ASN VAL THR THR GLY GLN VAL TYR SER THR
SEQRES 9 B 586 VAL ILE ALA LYS GLU ARG ARG GLY GLU TYR LEU GLY ASP
SEQRES 10 B 586 THR VAL GLN VAL ILE PRO HIS ILE THR ASP GLU ILE LYS
SEQRES 11 B 586 ARG ARG ILE LEU ALA MET ALA GLN PRO ASP ALA ASP GLY
SEQRES 12 B 586 ASN ARG PRO ASP VAL VAL ILE THR GLU ILE GLY GLY THR
SEQRES 13 B 586 VAL GLY ASP ILE GLU SER GLN PRO PHE LEU GLU ALA ALA
SEQRES 14 B 586 ARG GLN VAL ARG HIS TYR LEU GLY ARG GLU ASP VAL PHE
SEQRES 15 B 586 PHE LEU HIS VAL SER LEU VAL PRO TYR LEU ALA PRO SER
SEQRES 16 B 586 GLY GLU LEU LYS THR LYS PRO THR GLN HIS SER VAL ALA
SEQRES 17 B 586 ALA LEU ARG SER ILE GLY ILE THR PRO ASP ALA LEU ILE
SEQRES 18 B 586 LEU ARG CYS ASP ARG ASP VAL PRO GLU ALA LEU LYS ASN
SEQRES 19 B 586 LYS ILE ALA LEU MET CYS ASP VAL ASP ILE ASP GLY VAL
SEQRES 20 B 586 ILE SER THR PRO ASP ALA PRO SER ILE TYR ASP ILE PRO
SEQRES 21 B 586 LYS VAL LEU HIS ARG GLU GLU LEU ASP ALA PHE VAL VAL
SEQRES 22 B 586 ARG ARG LEU ASN LEU PRO PHE ARG ASP VAL ASP TRP THR
SEQRES 23 B 586 GLU TRP ASP ASP LEU LEU ARG ARG VAL HIS GLU PRO HIS
SEQRES 24 B 586 GLU THR VAL ARG ILE ALA LEU VAL GLY LYS TYR VAL GLU
SEQRES 25 B 586 LEU SER ASP ALA TYR LEU SER VAL ALA GLU ALA LEU ARG
SEQRES 26 B 586 ALA GLY GLY PHE LYS HIS ARG ALA LYS VAL GLU ILE CYS
SEQRES 27 B 586 TRP VAL ALA SER ASP GLY CYS GLU THR THR SER GLY ALA
SEQRES 28 B 586 ALA ALA ALA LEU GLY ASP VAL HIS GLY VAL LEU ILE PRO
SEQRES 29 B 586 GLY GLY PHE GLY ILE ARG GLY ILE GLU GLY LYS ILE GLY
SEQRES 30 B 586 ALA ILE ALA TYR ALA ARG ALA ARG GLY LEU PRO VAL LEU
SEQRES 31 B 586 GLY LEU CYS LEU GLY LEU GLN CYS ILE VAL ILE GLU ALA
SEQRES 32 B 586 ALA ARG SER VAL GLY LEU THR ASN ALA ASN SER ALA GLU
SEQRES 33 B 586 PHE ASP PRO ASP THR PRO ASP PRO VAL ILE ALA THR MET
SEQRES 34 B 586 PRO ASP GLN GLU GLU ILE VAL ALA GLY GLU ALA ASP LEU
SEQRES 35 B 586 GLY GLY THR MET ARG LEU GLY SER TYR PRO ALA VAL LEU
SEQRES 36 B 586 GLU PRO ASP SER VAL VAL ALA GLN ALA TYR GLN THR THR
SEQRES 37 B 586 GLN VAL SER GLU ARG HIS ARG HIS ARG TYR GLU VAL ASN
SEQRES 38 B 586 ASN ALA TYR ARG ASP LYS ILE ALA GLU SER GLY LEU ARG
SEQRES 39 B 586 PHE SER GLY THR SER PRO ASP GLY HIS LEU VAL GLU PHE
SEQRES 40 B 586 VAL GLU TYR PRO PRO ASP ARG HIS PRO PHE VAL VAL GLY
SEQRES 41 B 586 THR GLN ALA HIS PRO GLU LEU LYS SER ARG PRO THR ARG
SEQRES 42 B 586 PRO HIS PRO LEU PHE VAL ALA PHE VAL GLY ALA ALA ILE
SEQRES 43 B 586 ASP TYR LYS ALA GLY GLU LEU LEU PRO VAL GLU ILE PRO
SEQRES 44 B 586 GLU ILE PRO GLU HIS THR PRO ASN GLY SER SER HIS ARG
SEQRES 45 B 586 ASP GLY VAL GLY GLN PRO LEU PRO GLU PRO ALA SER ARG
SEQRES 46 B 586 GLY
HET ONL A 601 10
HET ACP A 602 31
HET UTP A 603 29
HET MG A 604 1
HET ONL B 601 10
HET ACP B 602 31
HET UTP B 603 29
HET MG B 604 1
HETNAM ONL 5-OXO-L-NORLEUCINE
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETNAM UTP URIDINE 5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
FORMUL 3 ONL 2(C6 H11 N O3)
FORMUL 4 ACP 2(C11 H18 N5 O12 P3)
FORMUL 5 UTP 2(C9 H15 N2 O15 P3)
FORMUL 6 MG 2(MG 2+)
HELIX 1 AA1 GLY A 23 ARG A 38 1 16
HELIX 2 AA2 ASP A 54 MET A 58 5 5
HELIX 3 AA3 ASN A 59 GLY A 64 1 6
HELIX 4 AA4 LEU A 77 ASP A 87 1 11
HELIX 5 AA5 PRO A 91 SER A 93 5 3
HELIX 6 AA6 THR A 98 ARG A 111 1 14
HELIX 7 AA7 GLN A 120 ALA A 135 1 16
HELIX 8 AA8 MET A 136 GLN A 138 5 3
HELIX 9 AA9 SER A 162 GLY A 177 1 16
HELIX 10 AB1 THR A 200 ILE A 213 1 14
HELIX 11 AB2 PRO A 229 ASP A 241 1 13
HELIX 12 AB3 ASP A 243 ASP A 245 5 3
HELIX 13 AB4 SER A 255 TYR A 257 5 3
HELIX 14 AB5 ASP A 258 GLU A 266 1 9
HELIX 15 AB6 GLU A 267 LEU A 276 1 10
HELIX 16 AB7 TRP A 285 GLU A 297 1 13
HELIX 17 AB8 SER A 314 ALA A 316 5 3
HELIX 18 AB9 TYR A 317 HIS A 331 1 15
HELIX 19 AC1 ASP A 343 GLU A 346 5 4
HELIX 20 AC2 THR A 347 GLY A 356 1 10
HELIX 21 AC3 ILE A 372 GLY A 386 1 15
HELIX 22 AC4 CYS A 393 VAL A 407 1 15
HELIX 23 AC5 SER A 459 GLN A 466 1 8
HELIX 24 AC6 TYR A 484 ALA A 489 1 6
HELIX 25 AC7 GLU A 490 GLY A 492 5 3
HELIX 26 AC8 HIS A 524 SER A 529 5 6
HELIX 27 AC9 HIS A 535 LEU A 553 1 19
HELIX 28 AD1 GLY B 23 ARG B 38 1 16
HELIX 29 AD2 ASP B 54 MET B 58 5 5
HELIX 30 AD3 ASN B 59 GLY B 64 1 6
HELIX 31 AD4 LEU B 77 ASP B 87 1 11
HELIX 32 AD5 PRO B 91 SER B 93 5 3
HELIX 33 AD6 THR B 98 ARG B 111 1 14
HELIX 34 AD7 GLN B 120 ALA B 135 1 16
HELIX 35 AD8 MET B 136 GLN B 138 5 3
HELIX 36 AD9 SER B 162 GLY B 177 1 16
HELIX 37 AE1 THR B 200 ILE B 213 1 14
HELIX 38 AE2 PRO B 229 ASP B 241 1 13
HELIX 39 AE3 ASP B 243 ASP B 245 5 3
HELIX 40 AE4 SER B 255 TYR B 257 5 3
HELIX 41 AE5 ASP B 258 GLU B 266 1 9
HELIX 42 AE6 GLU B 267 LEU B 276 1 10
HELIX 43 AE7 TRP B 285 GLU B 297 1 13
HELIX 44 AE8 SER B 314 ALA B 316 5 3
HELIX 45 AE9 TYR B 317 HIS B 331 1 15
HELIX 46 AF1 ASP B 343 GLU B 346 5 4
HELIX 47 AF2 THR B 347 GLY B 356 1 10
HELIX 48 AF3 ILE B 372 GLY B 386 1 15
HELIX 49 AF4 CYS B 393 VAL B 407 1 15
HELIX 50 AF5 SER B 459 GLN B 466 1 8
HELIX 51 AF6 TYR B 484 ALA B 489 1 6
HELIX 52 AF7 GLU B 490 GLY B 492 5 3
HELIX 53 AF8 HIS B 524 SER B 529 5 6
HELIX 54 AF9 HIS B 535 GLU B 552 1 18
SHEET 1 AA1 7 ASN A 95 THR A 97 0
SHEET 2 AA1 7 VAL A 42 ASP A 48 1 N ASP A 48 O VAL A 96
SHEET 3 AA1 7 VAL A 148 ILE A 153 1 O GLU A 152 N GLN A 45
SHEET 4 AA1 7 LYS A 10 GLY A 16 1 N VAL A 14 O ILE A 153
SHEET 5 AA1 7 VAL A 181 LEU A 188 1 O LEU A 184 N PHE A 13
SHEET 6 AA1 7 ALA A 219 CYS A 224 1 O ILE A 221 N SER A 187
SHEET 7 AA1 7 VAL A 247 PRO A 251 1 O ILE A 248 N LEU A 222
SHEET 1 AA2 2 VAL A 66 VAL A 68 0
SHEET 2 AA2 2 GLU A 74 ASP A 76 -1 O THR A 75 N PHE A 67
SHEET 1 AA3 2 TYR A 191 LEU A 192 0
SHEET 2 AA3 2 GLU A 197 LEU A 198 -1 O GLU A 197 N LEU A 192
SHEET 1 AA4 9 ALA A 333 ALA A 341 0
SHEET 2 AA4 9 GLU A 300 GLY A 308 1 N VAL A 302 O GLU A 336
SHEET 3 AA4 9 GLY A 360 ILE A 363 1 O LEU A 362 N ALA A 305
SHEET 4 AA4 9 VAL A 389 LEU A 392 1 O LEU A 392 N ILE A 363
SHEET 5 AA4 9 VAL A 518 THR A 521 1 O VAL A 519 N VAL A 389
SHEET 6 AA4 9 VAL A 505 GLU A 509 -1 N VAL A 508 O GLY A 520
SHEET 7 AA4 9 ARG A 494 THR A 498 -1 N ARG A 494 O GLU A 509
SHEET 8 AA4 9 ARG A 447 LEU A 455 -1 N VAL A 454 O THR A 498
SHEET 9 AA4 9 GLN A 469 HIS A 476 -1 O HIS A 476 N ARG A 447
SHEET 1 AA5 3 ASN A 413 SER A 414 0
SHEET 2 AA5 3 PRO A 424 THR A 428 1 O ILE A 426 N ASN A 413
SHEET 3 AA5 3 TYR A 478 VAL A 480 -1 O GLU A 479 N ALA A 427
SHEET 1 AA6 7 ASN B 95 THR B 97 0
SHEET 2 AA6 7 VAL B 42 ASP B 48 1 N ASP B 48 O VAL B 96
SHEET 3 AA6 7 VAL B 148 ILE B 153 1 O GLU B 152 N LEU B 47
SHEET 4 AA6 7 LYS B 10 GLY B 16 1 N VAL B 14 O ILE B 153
SHEET 5 AA6 7 VAL B 181 LEU B 188 1 O LEU B 184 N PHE B 13
SHEET 6 AA6 7 ALA B 219 CYS B 224 1 O ILE B 221 N SER B 187
SHEET 7 AA6 7 VAL B 247 PRO B 251 1 O ILE B 248 N LEU B 222
SHEET 1 AA7 2 VAL B 66 VAL B 68 0
SHEET 2 AA7 2 GLU B 74 ASP B 76 -1 O THR B 75 N PHE B 67
SHEET 1 AA8 2 TYR B 191 LEU B 192 0
SHEET 2 AA8 2 GLU B 197 LEU B 198 -1 O GLU B 197 N LEU B 192
SHEET 1 AA9 9 ALA B 333 ALA B 341 0
SHEET 2 AA9 9 GLU B 300 GLY B 308 1 N VAL B 302 O GLU B 336
SHEET 3 AA9 9 GLY B 360 ILE B 363 1 O LEU B 362 N ALA B 305
SHEET 4 AA9 9 VAL B 389 LEU B 392 1 O LEU B 392 N ILE B 363
SHEET 5 AA9 9 VAL B 518 THR B 521 1 O VAL B 519 N VAL B 389
SHEET 6 AA9 9 VAL B 505 GLU B 509 -1 N VAL B 508 O GLY B 520
SHEET 7 AA9 9 ARG B 494 THR B 498 -1 N ARG B 494 O GLU B 509
SHEET 8 AA9 9 ARG B 447 LEU B 455 -1 N VAL B 454 O THR B 498
SHEET 9 AA9 9 GLN B 469 HIS B 476 -1 O HIS B 476 N ARG B 447
SHEET 1 AB1 3 ASN B 413 SER B 414 0
SHEET 2 AB1 3 PRO B 424 THR B 428 1 O ILE B 426 N ASN B 413
SHEET 3 AB1 3 TYR B 478 VAL B 480 -1 O GLU B 479 N ALA B 427
LINK SG CYS A 393 CE ONL A 601 1555 1555 1.77
LINK SG CYS B 393 CE ONL B 601 1555 1555 1.80
LINK OD1 ASP A 78 MG MG A 604 1555 1555 2.74
LINK OD2 ASP A 78 MG MG A 604 1555 1555 2.22
LINK OE1 GLU A 152 MG MG A 604 1555 1555 2.99
LINK OE2 GLU A 152 MG MG A 604 1555 1555 2.66
LINK O3G ACP A 602 MG MG A 604 1555 1555 2.44
LINK O1B ACP A 602 MG MG A 604 1555 1555 2.70
LINK OD2 ASP B 78 MG MG B 604 1555 1555 2.62
LINK OE2 GLU B 152 MG MG B 604 1555 1555 2.67
LINK O1B ACP B 602 MG MG B 604 1555 1555 2.37
CISPEP 1 ILE A 122 PRO A 123 0 9.35
CISPEP 2 ILE B 122 PRO B 123 0 8.62
SITE 1 AC1 10 GLY A 365 GLY A 366 PHE A 367 CYS A 393
SITE 2 AC1 10 GLN A 397 GLU A 416 ARG A 475 HIS A 476
SITE 3 AC1 10 ARG A 477 TYR A 478
SITE 1 AC2 16 SER A 21 LEU A 22 GLY A 23 LYS A 24
SITE 2 AC2 16 GLY A 25 LEU A 26 LYS A 46 ASP A 78
SITE 3 AC2 16 GLU A 152 ARG A 223 ASP A 252 ALA A 253
SITE 4 AC2 16 ILE A 256 ILE A 259 MG A 604 PRO B 194
SITE 1 AC3 11 SER A 20 GLN A 120 ILE A 122 ASP A 159
SITE 2 AC3 11 ILE A 160 GLU A 161 LEU B 198 LYS B 199
SITE 3 AC3 11 THR B 200 LYS B 201 GLN B 204
SITE 1 AC4 4 GLY A 25 ASP A 78 GLU A 152 ACP A 602
SITE 1 AC5 14 PRO A 194 SER B 21 LEU B 22 GLY B 23
SITE 2 AC5 14 LYS B 24 GLY B 25 LEU B 26 LYS B 46
SITE 3 AC5 14 ASP B 78 GLU B 152 ARG B 223 ALA B 253
SITE 4 AC5 14 ILE B 259 MG B 604
SITE 1 AC6 10 LYS A 199 THR A 200 LYS A 201 GLN A 204
SITE 2 AC6 10 SER B 20 GLN B 120 ILE B 122 ASP B 159
SITE 3 AC6 10 ILE B 160 GLU B 161
SITE 1 AC7 4 GLY B 25 ASP B 78 GLU B 152 ACP B 602
SITE 1 AC8 16 GLY B 365 GLY B 366 LEU B 392 LEU B 394
SITE 2 AC8 16 GLY B 395 LEU B 396 GLN B 397 GLU B 416
SITE 3 AC8 16 ARG B 475 HIS B 476 ARG B 477 TYR B 478
SITE 4 AC8 16 THR B 521 GLN B 522 ALA B 523 HIS B 524
CRYST1 121.732 194.724 207.457 90.00 90.00 90.00 I 21 21 21 16
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 0.008215 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005135 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004820 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
