HEADER TRANSFERASE 09-DEC-05 2C94
TITLE LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-
TITLE 2 TRIHYDRO-9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL) 1,1 DIFLUOROPENTANE-1-
TITLE 3 PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 SYNONYM: DMRL SYNTHASE, LUMAZINE SYNTHASE, RIBOFLAVIN SYNTHASE BETA
COMPND 5 CHAIN;
COMPND 6 EC: 2.5.1.9;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PNCO113;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PNCO-MT-LS
KEYWDS TRANSFERASE, RIBOFLAVIN BIOSYNTHESIS, MYCOBACTERIUM TUBERCULOSIS,
KEYWDS 2 LUMAZINE SYNTHASE, INHIBITOR BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR E.MORGUNOVA,B.ILLARIONOV,G.JIN,I.HAASE,M.FISCHER,M.CUSHMAN,A.BACHER,
AUTHOR 2 R.LADENSTEIN
REVDAT 6 13-DEC-23 2C94 1 REMARK LINK
REVDAT 5 24-JUL-19 2C94 1 REMARK
REVDAT 4 10-APR-19 2C94 1 SOURCE
REVDAT 3 13-JUL-11 2C94 1 VERSN
REVDAT 2 24-FEB-09 2C94 1 VERSN
REVDAT 1 13-DEC-06 2C94 0
JRNL AUTH E.MORGUNOVA,B.ILLARIONOV,T.SAMBAIAH,I.HAASE,A.BACHER,
JRNL AUTH 2 M.CUSHMAN,M.FISCHER,R.LADENSTEIN
JRNL TITL STRUCTURAL AND THERMODYNAMIC INSIGHTS INTO THE BINDING MODE
JRNL TITL 2 OF FIVE NOVEL INHIBITORS OF LUMAZINE SYNTHASE FROM
JRNL TITL 3 MYCOBACTERIUM TUBERCULOSIS.
JRNL REF FEBS J. V. 273 4790 2006
JRNL REFN ISSN 1742-464X
JRNL PMID 16984393
JRNL DOI 10.1111/J.1742-4658.2006.05481.X
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 55681
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2972
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3865
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 190
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5269
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 177
REMARK 3 SOLVENT ATOMS : 549
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 25.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.75000
REMARK 3 B22 (A**2) : 0.82000
REMARK 3 B33 (A**2) : -0.85000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.77000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.150
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.372
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5493 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7525 ; 1.415 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 725 ; 4.742 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 200 ;33.660 ;23.750
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 823 ;12.824 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;16.943 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 943 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4020 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2812 ; 0.230 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3789 ; 0.294 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 524 ; 0.126 ; 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): 119 ; 0.233 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 36 ; 0.181 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3609 ; 0.468 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5772 ; 0.919 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1923 ; 1.583 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1753 ; 2.678 ; 4.500
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 : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 15 A 604
REMARK 3 RESIDUE RANGE : A 701 A 701
REMARK 3 ORIGIN FOR THE GROUP (A): 40.7235 -12.5515 13.0227
REMARK 3 T TENSOR
REMARK 3 T11: -0.0609 T22: -0.0406
REMARK 3 T33: -0.0892 T12: 0.0031
REMARK 3 T13: -0.0270 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 1.2692 L22: 0.9775
REMARK 3 L33: 1.4736 L12: 0.0575
REMARK 3 L13: -0.2432 L23: 0.1630
REMARK 3 S TENSOR
REMARK 3 S11: -0.0051 S12: 0.2275 S13: -0.0572
REMARK 3 S21: -0.1459 S22: 0.0072 S23: -0.0184
REMARK 3 S31: 0.0156 S32: -0.0564 S33: -0.0021
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 15 B 604
REMARK 3 RESIDUE RANGE : B 701 B 701
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6253 11.0785 12.4399
REMARK 3 T TENSOR
REMARK 3 T11: -0.0077 T22: -0.0232
REMARK 3 T33: -0.0595 T12: 0.0211
REMARK 3 T13: -0.0206 T23: 0.0635
REMARK 3 L TENSOR
REMARK 3 L11: 0.6281 L22: 0.9006
REMARK 3 L33: 1.7624 L12: -0.2234
REMARK 3 L13: -0.1280 L23: -0.1057
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: 0.1619 S13: 0.0994
REMARK 3 S21: -0.1102 S22: -0.0075 S23: -0.0094
REMARK 3 S31: -0.1922 S32: 0.0124 S33: -0.0037
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 15 C 604
REMARK 3 RESIDUE RANGE : C 701 C 701
REMARK 3 ORIGIN FOR THE GROUP (A): 58.4080 19.6935 24.3457
REMARK 3 T TENSOR
REMARK 3 T11: 0.0462 T22: -0.0399
REMARK 3 T33: 0.0221 T12: -0.0576
REMARK 3 T13: -0.0008 T23: 0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 1.4040 L22: 1.1401
REMARK 3 L33: 1.5862 L12: 0.1257
REMARK 3 L13: -0.1889 L23: -0.0894
REMARK 3 S TENSOR
REMARK 3 S11: 0.0334 S12: 0.1607 S13: 0.2458
REMARK 3 S21: -0.1234 S22: -0.0166 S23: -0.1332
REMARK 3 S31: -0.2775 S32: 0.1800 S33: -0.0167
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 15 D 604
REMARK 3 RESIDUE RANGE : D 701 D 701
REMARK 3 ORIGIN FOR THE GROUP (A): 71.0527 1.0727 32.4213
REMARK 3 T TENSOR
REMARK 3 T11: -0.0741 T22: -0.0381
REMARK 3 T33: -0.0188 T12: -0.0457
REMARK 3 T13: 0.0149 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 1.5289 L22: 0.9318
REMARK 3 L33: 1.3551 L12: 0.2007
REMARK 3 L13: 0.1202 L23: -0.1438
REMARK 3 S TENSOR
REMARK 3 S11: 0.0120 S12: 0.1274 S13: 0.0086
REMARK 3 S21: -0.1082 S22: -0.0206 S23: -0.1835
REMARK 3 S31: -0.0508 S32: 0.2225 S33: 0.0086
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 15 E 604
REMARK 3 RESIDUE RANGE : E 701 E 701
REMARK 3 ORIGIN FOR THE GROUP (A): 60.0788 -18.9599 25.3261
REMARK 3 T TENSOR
REMARK 3 T11: -0.0959 T22: -0.0617
REMARK 3 T33: -0.0492 T12: 0.0163
REMARK 3 T13: 0.0071 T23: -0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 1.4309 L22: 1.2841
REMARK 3 L33: 1.4065 L12: -0.1691
REMARK 3 L13: -0.0549 L23: -0.1151
REMARK 3 S TENSOR
REMARK 3 S11: 0.0084 S12: 0.1764 S13: -0.1407
REMARK 3 S21: -0.1344 S22: -0.0047 S23: -0.1054
REMARK 3 S31: 0.0903 S32: 0.1734 S33: -0.0036
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.RESIDUES 1-13 ARE DISORDERED
REMARK 4
REMARK 4 2C94 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1290026696.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.40
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.85
REMARK 200 MONOCHROMATOR : TRIANGULAR MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEACH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58728
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.370
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1W19
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.40
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 65.69200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.62550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 65.69200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.62550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 GLY A 3
REMARK 465 GLY A 4
REMARK 465 ALA A 5
REMARK 465 GLY A 6
REMARK 465 VAL A 7
REMARK 465 PRO A 8
REMARK 465 ASP A 9
REMARK 465 LEU A 10
REMARK 465 PRO A 11
REMARK 465 SER A 12
REMARK 465 LEU A 13
REMARK 465 ASP A 14
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 GLY B 3
REMARK 465 GLY B 4
REMARK 465 ALA B 5
REMARK 465 GLY B 6
REMARK 465 VAL B 7
REMARK 465 PRO B 8
REMARK 465 ASP B 9
REMARK 465 LEU B 10
REMARK 465 PRO B 11
REMARK 465 SER B 12
REMARK 465 LEU B 13
REMARK 465 ASP B 14
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 GLY C 3
REMARK 465 GLY C 4
REMARK 465 ALA C 5
REMARK 465 GLY C 6
REMARK 465 VAL C 7
REMARK 465 PRO C 8
REMARK 465 ASP C 9
REMARK 465 LEU C 10
REMARK 465 PRO C 11
REMARK 465 SER C 12
REMARK 465 LEU C 13
REMARK 465 ASP C 14
REMARK 465 MET D 1
REMARK 465 LYS D 2
REMARK 465 GLY D 3
REMARK 465 GLY D 4
REMARK 465 ALA D 5
REMARK 465 GLY D 6
REMARK 465 VAL D 7
REMARK 465 PRO D 8
REMARK 465 ASP D 9
REMARK 465 LEU D 10
REMARK 465 PRO D 11
REMARK 465 SER D 12
REMARK 465 LEU D 13
REMARK 465 ASP D 14
REMARK 465 MET E 1
REMARK 465 LYS E 2
REMARK 465 GLY E 3
REMARK 465 GLY E 4
REMARK 465 ALA E 5
REMARK 465 GLY E 6
REMARK 465 VAL E 7
REMARK 465 PRO E 8
REMARK 465 ASP E 9
REMARK 465 LEU E 10
REMARK 465 PRO E 11
REMARK 465 SER E 12
REMARK 465 LEU E 13
REMARK 465 ASP E 14
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 LEU E 156 CB
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TRP B 27 O HOH B 2008 1.88
REMARK 500 OD1 ASP A 33 NH2 ARG A 55 1.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP E 27 CA TRP E 27 CB 0.225
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TRP A 27 CB - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 TRP A 27 CA - CB - CG ANGL. DEV. = -12.5 DEGREES
REMARK 500 TRP A 27 N - CA - C ANGL. DEV. = -20.4 DEGREES
REMARK 500 HIS A 28 N - CA - CB ANGL. DEV. = 24.9 DEGREES
REMARK 500 ARG B 103 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 103 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 TRP E 27 N - CA - CB ANGL. DEV. = 15.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
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 HIS A 28 57.05 90.09
REMARK 500 HIS B 28 75.97 52.83
REMARK 500 HIS C 28 75.00 64.99
REMARK 500 ASP C 50 114.52 -28.51
REMARK 500 PRO C 88 1.92 -64.89
REMARK 500 HIS D 28 71.82 67.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH E2042 DISTANCE = 6.15 ANGSTROMS
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 K A1162 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 34 O
REMARK 620 2 GLY A 38 N 57.1
REMARK 620 3 ALA A 129 O 77.4 121.7
REMARK 620 4 GLY A 130 O 137.9 163.3 73.9
REMARK 620 5 ASP A 137 OD2 105.3 78.9 80.4 99.7
REMARK 620 6 HOH A2013 O 111.7 61.9 168.4 101.6 90.0
REMARK 620 7 HOH B2022 O 88.3 100.5 113.5 75.9 162.8 74.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1161 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 70 O
REMARK 620 2 HIS A 73 O 81.0
REMARK 620 3 THR A 110 OG1 93.6 101.0
REMARK 620 4 HOH A2047 O 91.7 106.2 152.8
REMARK 620 5 HOH A2050 O 169.3 90.9 94.8 83.8
REMARK 620 6 HOH A2076 O 76.4 157.4 79.3 76.0 111.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1164 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 84 O
REMARK 620 2 ASN A 120 O 84.4
REMARK 620 3 HOH A2089 O 116.4 89.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1163 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 155 O
REMARK 620 2 LEU A 156 O 70.9
REMARK 620 3 LEU A 156 O 136.0 76.3
REMARK 620 4 ARG A 157 O 73.5 68.1 67.5
REMARK 620 5 ARG A 157 O 124.7 67.1 63.4 119.0
REMARK 620 6 HOH A2112 O 117.7 146.4 77.1 82.9 117.3
REMARK 620 7 HOH A2112 O 59.4 82.0 142.8 130.4 80.4 131.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1162 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 34 O
REMARK 620 2 GLY B 38 N 55.4
REMARK 620 3 ALA B 129 O 80.9 124.0
REMARK 620 4 GLY B 130 O 143.5 158.9 75.7
REMARK 620 5 ASP B 137 OD2 107.7 78.2 84.8 97.8
REMARK 620 6 HOH B2016 O 88.1 98.5 114.7 77.0 157.1
REMARK 620 7 HOH B2019 O 110.9 63.2 167.2 96.1 86.7 72.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1161 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 70 O
REMARK 620 2 HIS B 73 O 78.4
REMARK 620 3 THR B 110 OG1 94.7 100.0
REMARK 620 4 HOH B2049 O 93.1 99.7 159.9
REMARK 620 5 HOH B2054 O 167.8 91.4 93.6 81.9
REMARK 620 6 HOH B2077 O 78.7 156.9 78.4 85.0 111.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1164 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 84 O
REMARK 620 2 ASN B 120 O 85.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1163 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 155 O
REMARK 620 2 LEU B 156 O 74.3
REMARK 620 3 ARG B 157 O 73.1 70.7
REMARK 620 4 HOH B2107 O 110.9 148.1 80.6
REMARK 620 5 LEU E 156 O 141.9 80.3 72.0 77.7
REMARK 620 6 ARG E 157 O 124.6 71.1 129.7 121.5 70.5
REMARK 620 7 HOH E2113 O 62.3 91.4 135.0 119.3 147.2 76.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C1161 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA C 70 O
REMARK 620 2 HIS C 73 O 78.7
REMARK 620 3 THR C 110 OG1 93.5 100.1
REMARK 620 4 HOH C2012 O 167.7 92.0 96.1
REMARK 620 5 HOH C2032 O 92.6 96.9 162.8 80.3
REMARK 620 6 HOH C2059 O 77.7 156.3 78.6 111.7 87.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C1162 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG C 84 O
REMARK 620 2 ASN C 120 O 86.7
REMARK 620 3 HOH C2040 O 76.7 96.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D1163 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 155 O
REMARK 620 2 LEU C 156 O 69.2
REMARK 620 3 ARG C 157 O 69.4 70.7
REMARK 620 4 HOH C2081 O 112.5 144.3 76.7
REMARK 620 5 GLU D 155 O 152.0 134.8 126.5 58.7
REMARK 620 6 LEU D 156 O 137.3 81.0 72.3 75.4 69.2
REMARK 620 7 ARG D 157 O 124.1 72.4 130.8 122.3 66.1 70.8
REMARK 620 8 HOH D2115 O 56.0 81.6 124.7 130.5 107.2 149.1 79.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D1162 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA D 34 O
REMARK 620 2 ALA D 129 O 78.6
REMARK 620 3 GLY D 130 O 143.2 74.8
REMARK 620 4 ASP D 137 OD2 107.2 83.1 94.3
REMARK 620 5 HOH D2017 O 120.0 161.4 88.0 91.3
REMARK 620 6 HOH D2018 O 85.4 114.7 83.3 160.4 69.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D1161 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA D 70 O
REMARK 620 2 HIS D 73 O 78.2
REMARK 620 3 THR D 110 OG1 92.6 100.2
REMARK 620 4 HOH D2026 O 95.5 98.3 161.0
REMARK 620 5 HOH D2058 O 168.9 95.0 97.2 76.7
REMARK 620 6 HOH D2088 O 79.2 157.1 77.7 86.9 107.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K D1164 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG D 84 O
REMARK 620 2 ASN D 120 O 85.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E1162 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA E 34 O
REMARK 620 2 ALA E 129 O 82.9
REMARK 620 3 GLY E 130 O 148.9 72.0
REMARK 620 4 ASP E 137 OD2 105.5 82.3 89.5
REMARK 620 5 HOH E2019 O 85.2 113.0 87.8 162.7
REMARK 620 6 HOH E2020 O 114.6 161.5 92.8 87.2 75.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E1161 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA E 70 O
REMARK 620 2 HIS E 73 O 80.6
REMARK 620 3 THR E 110 OG1 92.0 100.0
REMARK 620 4 HOH E2026 O 167.4 87.6 94.5
REMARK 620 5 HOH E2055 O 94.5 92.3 166.9 81.4
REMARK 620 6 HOH E2080 O 135.4 138.2 64.9 57.2 102.8
REMARK 620 7 HOH E2081 O 77.6 158.1 79.8 114.2 90.4 61.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E1163 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG E 84 O
REMARK 620 2 ASN E 120 O 87.3
REMARK 620 3 HOH E2063 O 75.0 109.2
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 K A1161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A1164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B1161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B1162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B1163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B1164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C1161
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C1162
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D1161
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D1162
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D1163
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D1164
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E1161
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E1162
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E1163
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSF A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSF B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSF C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSF D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSF E 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1W19 RELATED DB: PDB
REMARK 900 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-
REMARK 900 TRIHYDRO- 9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL) PROPANE 1-PHOSPHATE
REMARK 900 RELATED ID: 1W29 RELATED DB: PDB
REMARK 900 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-
REMARK 900 TRIHYDRO- 9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL) BUTANE 1-PHOSPHATE
REMARK 900 RELATED ID: 2C92 RELATED DB: PDB
REMARK 900 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-
REMARK 900 TRIHYDRO- 9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL) PENTANE 1 PHOSPHATE
REMARK 900 RELATED ID: 2C97 RELATED DB: PDB
REMARK 900 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 4-(6-
REMARK 900 CHLORO-2,4- DIOXO-1,2,3,4-TETRAHYDROPYRIMIDIN-5-YL) BUTYL PHOSPHATE
REMARK 900 RELATED ID: 2C9B RELATED DB: PDB
REMARK 900 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-
REMARK 900 TRIHYDRO- 9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL)
REMARK 900 RELATED ID: 2C9D RELATED DB: PDB
REMARK 900 LUMAZINE SYNTHASE FROM MYCOBACTERIUM TUBERCULOSIS BOUND TO 3-(1,3,7-
REMARK 900 TRIHYDRO- 9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL) HEXANE 1-PHOSPHATE
DBREF 2C94 A 1 160 UNP P66034 RISB_MYCTU 1 160
DBREF 2C94 B 1 160 UNP P66034 RISB_MYCTU 1 160
DBREF 2C94 C 1 160 UNP P66034 RISB_MYCTU 1 160
DBREF 2C94 D 1 160 UNP P66034 RISB_MYCTU 1 160
DBREF 2C94 E 1 160 UNP P66034 RISB_MYCTU 1 160
SEQRES 1 A 160 MET LYS GLY GLY ALA GLY VAL PRO ASP LEU PRO SER LEU
SEQRES 2 A 160 ASP ALA SER GLY VAL ARG LEU ALA ILE VAL ALA SER SER
SEQRES 3 A 160 TRP HIS GLY LYS ILE CYS ASP ALA LEU LEU ASP GLY ALA
SEQRES 4 A 160 ARG LYS VAL ALA ALA GLY CYS GLY LEU ASP ASP PRO THR
SEQRES 5 A 160 VAL VAL ARG VAL LEU GLY ALA ILE GLU ILE PRO VAL VAL
SEQRES 6 A 160 ALA GLN GLU LEU ALA ARG ASN HIS ASP ALA VAL VAL ALA
SEQRES 7 A 160 LEU GLY VAL VAL ILE ARG GLY GLN THR PRO HIS PHE ASP
SEQRES 8 A 160 TYR VAL CYS ASP ALA VAL THR GLN GLY LEU THR ARG VAL
SEQRES 9 A 160 SER LEU ASP SER SER THR PRO ILE ALA ASN GLY VAL LEU
SEQRES 10 A 160 THR THR ASN THR GLU GLU GLN ALA LEU ASP ARG ALA GLY
SEQRES 11 A 160 LEU PRO THR SER ALA GLU ASP LYS GLY ALA GLN ALA THR
SEQRES 12 A 160 VAL ALA ALA LEU ALA THR ALA LEU THR LEU ARG GLU LEU
SEQRES 13 A 160 ARG ALA HIS SER
SEQRES 1 B 160 MET LYS GLY GLY ALA GLY VAL PRO ASP LEU PRO SER LEU
SEQRES 2 B 160 ASP ALA SER GLY VAL ARG LEU ALA ILE VAL ALA SER SER
SEQRES 3 B 160 TRP HIS GLY LYS ILE CYS ASP ALA LEU LEU ASP GLY ALA
SEQRES 4 B 160 ARG LYS VAL ALA ALA GLY CYS GLY LEU ASP ASP PRO THR
SEQRES 5 B 160 VAL VAL ARG VAL LEU GLY ALA ILE GLU ILE PRO VAL VAL
SEQRES 6 B 160 ALA GLN GLU LEU ALA ARG ASN HIS ASP ALA VAL VAL ALA
SEQRES 7 B 160 LEU GLY VAL VAL ILE ARG GLY GLN THR PRO HIS PHE ASP
SEQRES 8 B 160 TYR VAL CYS ASP ALA VAL THR GLN GLY LEU THR ARG VAL
SEQRES 9 B 160 SER LEU ASP SER SER THR PRO ILE ALA ASN GLY VAL LEU
SEQRES 10 B 160 THR THR ASN THR GLU GLU GLN ALA LEU ASP ARG ALA GLY
SEQRES 11 B 160 LEU PRO THR SER ALA GLU ASP LYS GLY ALA GLN ALA THR
SEQRES 12 B 160 VAL ALA ALA LEU ALA THR ALA LEU THR LEU ARG GLU LEU
SEQRES 13 B 160 ARG ALA HIS SER
SEQRES 1 C 160 MET LYS GLY GLY ALA GLY VAL PRO ASP LEU PRO SER LEU
SEQRES 2 C 160 ASP ALA SER GLY VAL ARG LEU ALA ILE VAL ALA SER SER
SEQRES 3 C 160 TRP HIS GLY LYS ILE CYS ASP ALA LEU LEU ASP GLY ALA
SEQRES 4 C 160 ARG LYS VAL ALA ALA GLY CYS GLY LEU ASP ASP PRO THR
SEQRES 5 C 160 VAL VAL ARG VAL LEU GLY ALA ILE GLU ILE PRO VAL VAL
SEQRES 6 C 160 ALA GLN GLU LEU ALA ARG ASN HIS ASP ALA VAL VAL ALA
SEQRES 7 C 160 LEU GLY VAL VAL ILE ARG GLY GLN THR PRO HIS PHE ASP
SEQRES 8 C 160 TYR VAL CYS ASP ALA VAL THR GLN GLY LEU THR ARG VAL
SEQRES 9 C 160 SER LEU ASP SER SER THR PRO ILE ALA ASN GLY VAL LEU
SEQRES 10 C 160 THR THR ASN THR GLU GLU GLN ALA LEU ASP ARG ALA GLY
SEQRES 11 C 160 LEU PRO THR SER ALA GLU ASP LYS GLY ALA GLN ALA THR
SEQRES 12 C 160 VAL ALA ALA LEU ALA THR ALA LEU THR LEU ARG GLU LEU
SEQRES 13 C 160 ARG ALA HIS SER
SEQRES 1 D 160 MET LYS GLY GLY ALA GLY VAL PRO ASP LEU PRO SER LEU
SEQRES 2 D 160 ASP ALA SER GLY VAL ARG LEU ALA ILE VAL ALA SER SER
SEQRES 3 D 160 TRP HIS GLY LYS ILE CYS ASP ALA LEU LEU ASP GLY ALA
SEQRES 4 D 160 ARG LYS VAL ALA ALA GLY CYS GLY LEU ASP ASP PRO THR
SEQRES 5 D 160 VAL VAL ARG VAL LEU GLY ALA ILE GLU ILE PRO VAL VAL
SEQRES 6 D 160 ALA GLN GLU LEU ALA ARG ASN HIS ASP ALA VAL VAL ALA
SEQRES 7 D 160 LEU GLY VAL VAL ILE ARG GLY GLN THR PRO HIS PHE ASP
SEQRES 8 D 160 TYR VAL CYS ASP ALA VAL THR GLN GLY LEU THR ARG VAL
SEQRES 9 D 160 SER LEU ASP SER SER THR PRO ILE ALA ASN GLY VAL LEU
SEQRES 10 D 160 THR THR ASN THR GLU GLU GLN ALA LEU ASP ARG ALA GLY
SEQRES 11 D 160 LEU PRO THR SER ALA GLU ASP LYS GLY ALA GLN ALA THR
SEQRES 12 D 160 VAL ALA ALA LEU ALA THR ALA LEU THR LEU ARG GLU LEU
SEQRES 13 D 160 ARG ALA HIS SER
SEQRES 1 E 160 MET LYS GLY GLY ALA GLY VAL PRO ASP LEU PRO SER LEU
SEQRES 2 E 160 ASP ALA SER GLY VAL ARG LEU ALA ILE VAL ALA SER SER
SEQRES 3 E 160 TRP HIS GLY LYS ILE CYS ASP ALA LEU LEU ASP GLY ALA
SEQRES 4 E 160 ARG LYS VAL ALA ALA GLY CYS GLY LEU ASP ASP PRO THR
SEQRES 5 E 160 VAL VAL ARG VAL LEU GLY ALA ILE GLU ILE PRO VAL VAL
SEQRES 6 E 160 ALA GLN GLU LEU ALA ARG ASN HIS ASP ALA VAL VAL ALA
SEQRES 7 E 160 LEU GLY VAL VAL ILE ARG GLY GLN THR PRO HIS PHE ASP
SEQRES 8 E 160 TYR VAL CYS ASP ALA VAL THR GLN GLY LEU THR ARG VAL
SEQRES 9 E 160 SER LEU ASP SER SER THR PRO ILE ALA ASN GLY VAL LEU
SEQRES 10 E 160 THR THR ASN THR GLU GLU GLN ALA LEU ASP ARG ALA GLY
SEQRES 11 E 160 LEU PRO THR SER ALA GLU ASP LYS GLY ALA GLN ALA THR
SEQRES 12 E 160 VAL ALA ALA LEU ALA THR ALA LEU THR LEU ARG GLU LEU
SEQRES 13 E 160 ARG ALA HIS SER
HET TSF A 701 32
HET K A1161 1
HET K A1162 1
HET K A1163 1
HET K A1164 1
HET TSF B 701 32
HET K B1161 1
HET K B1162 1
HET K B1163 1
HET K B1164 1
HET TSF C 701 32
HET K C1161 1
HET K C1162 1
HET TSF D 701 32
HET K D1161 1
HET K D1162 1
HET K D1163 1
HET K D1164 1
HET TSF E 701 32
HET K E1161 1
HET K E1162 1
HET K E1163 1
HETNAM TSF 3-(1,3,7-TRIHYDRO-9-D-RIBITYL-2,6,8-PURINETRIONE-7-YL)
HETNAM 2 TSF 1,1 DIFLUOROPENTANE-1-PHOSPHATE
HETNAM K POTASSIUM ION
FORMUL 6 TSF 5(C15 H23 F2 N4 O10 P)
FORMUL 7 K 17(K 1+)
FORMUL 28 HOH *549(H2 O)
HELIX 1 1 HIS A 28 CYS A 46 1 19
HELIX 2 2 GLY A 58 ILE A 60 5 3
HELIX 3 3 GLU A 61 ARG A 71 1 11
HELIX 4 4 PRO A 88 SER A 109 1 22
HELIX 5 5 THR A 121 ASP A 127 1 7
HELIX 6 6 ASP A 137 ARG A 157 1 21
HELIX 7 7 HIS B 28 CYS B 46 1 19
HELIX 8 8 GLY B 58 ILE B 60 5 3
HELIX 9 9 GLU B 61 ARG B 71 1 11
HELIX 10 10 PRO B 88 SER B 109 1 22
HELIX 11 11 THR B 121 ASP B 127 1 7
HELIX 12 12 ASP B 137 ARG B 157 1 21
HELIX 13 13 HIS C 28 CYS C 46 1 19
HELIX 14 14 GLY C 58 ILE C 60 5 3
HELIX 15 15 GLU C 61 ARG C 71 1 11
HELIX 16 16 PRO C 88 SER C 109 1 22
HELIX 17 17 THR C 121 ASP C 127 1 7
HELIX 18 18 ASP C 137 ARG C 157 1 21
HELIX 19 19 HIS D 28 CYS D 46 1 19
HELIX 20 20 GLY D 58 ILE D 60 5 3
HELIX 21 21 GLU D 61 ARG D 71 1 11
HELIX 22 22 PRO D 88 SER D 109 1 22
HELIX 23 23 THR D 121 ASP D 127 1 7
HELIX 24 24 ASP D 137 ARG D 157 1 21
HELIX 25 25 HIS E 28 CYS E 46 1 19
HELIX 26 26 GLY E 58 ILE E 60 5 3
HELIX 27 27 GLU E 61 ARG E 71 1 11
HELIX 28 28 PRO E 88 SER E 109 1 22
HELIX 29 29 THR E 121 ASP E 127 1 7
HELIX 30 30 ASP E 137 ARG E 157 1 21
SHEET 1 AA 4 THR A 52 VAL A 56 0
SHEET 2 AA 4 LEU A 20 SER A 25 1 O LEU A 20 N THR A 52
SHEET 3 AA 4 ALA A 75 ILE A 83 1 O ALA A 75 N ALA A 21
SHEET 4 AA 4 ILE A 112 THR A 119 1 O ALA A 113 N ALA A 78
SHEET 1 BA 4 THR B 52 VAL B 56 0
SHEET 2 BA 4 LEU B 20 SER B 25 1 O LEU B 20 N THR B 52
SHEET 3 BA 4 ALA B 75 ILE B 83 1 O ALA B 75 N ALA B 21
SHEET 4 BA 4 ILE B 112 THR B 119 1 O ALA B 113 N ALA B 78
SHEET 1 CA 4 THR C 52 VAL C 56 0
SHEET 2 CA 4 LEU C 20 SER C 25 1 O LEU C 20 N THR C 52
SHEET 3 CA 4 ALA C 75 ILE C 83 1 O ALA C 75 N ALA C 21
SHEET 4 CA 4 ILE C 112 THR C 119 1 O ALA C 113 N ALA C 78
SHEET 1 DA 4 THR D 52 VAL D 56 0
SHEET 2 DA 4 LEU D 20 SER D 25 1 O LEU D 20 N THR D 52
SHEET 3 DA 4 ALA D 75 ILE D 83 1 O ALA D 75 N ALA D 21
SHEET 4 DA 4 ILE D 112 THR D 119 1 O ALA D 113 N ALA D 78
SHEET 1 EA 4 THR E 52 VAL E 56 0
SHEET 2 EA 4 LEU E 20 SER E 25 1 O LEU E 20 N THR E 52
SHEET 3 EA 4 ALA E 75 ILE E 83 1 O ALA E 75 N ALA E 21
SHEET 4 EA 4 ILE E 112 THR E 119 1 O ALA E 113 N ALA E 78
LINK O ALA A 34 K K A1162 1555 1555 2.58
LINK N GLY A 38 K K A1162 1555 1555 3.61
LINK O ALA A 70 K K A1161 1555 1555 2.62
LINK O HIS A 73 K K A1161 1555 1555 2.66
LINK O ARG A 84 K K A1164 1555 1555 2.76
LINK OG1 THR A 110 K K A1161 1555 1555 2.76
LINK O ASN A 120 K K A1164 1555 1555 2.73
LINK O ALA A 129 K K A1162 1555 1555 3.19
LINK O GLY A 130 K K A1162 1555 1555 2.82
LINK OD2 ASP A 137 K K A1162 1555 1555 2.78
LINK O GLU A 155 K K A1163 1555 1555 3.57
LINK O LEU A 156 K K A1163 1555 1555 3.04
LINK O LEU A 156 K K A1163 2656 1555 3.21
LINK O ARG A 157 K K A1163 1555 1555 2.91
LINK O ARG A 157 K K A1163 2656 1555 3.13
LINK K K A1161 O HOH A2047 1555 1555 2.68
LINK K K A1161 O HOH A2050 1555 1555 2.92
LINK K K A1161 O HOH A2076 1555 1555 2.83
LINK K K A1162 O HOH A2013 1555 1555 2.68
LINK K K A1162 O HOH B2022 1555 4545 2.70
LINK K K A1163 O HOH A2112 1555 1555 2.68
LINK K K A1163 O HOH A2112 1555 2656 2.57
LINK K K A1164 O HOH A2089 1555 1555 3.70
LINK O ALA B 34 K K B1162 1555 1555 2.77
LINK N GLY B 38 K K B1162 1555 1555 3.67
LINK O ALA B 70 K K B1161 1555 1555 2.65
LINK O HIS B 73 K K B1161 1555 1555 2.73
LINK O ARG B 84 K K B1164 1555 1555 2.72
LINK OG1 THR B 110 K K B1161 1555 1555 2.74
LINK O ASN B 120 K K B1164 1555 1555 2.76
LINK O ALA B 129 K K B1162 1555 1555 2.96
LINK O GLY B 130 K K B1162 1555 1555 2.90
LINK OD2 ASP B 137 K K B1162 1555 1555 2.77
LINK O GLU B 155 K K B1163 1555 1555 3.38
LINK O LEU B 156 K K B1163 1555 1555 2.89
LINK O ARG B 157 K K B1163 1555 1555 2.88
LINK K K B1161 O HOH B2049 1555 1555 2.91
LINK K K B1161 O HOH B2054 1555 1555 2.67
LINK K K B1161 O HOH B2077 1555 1555 2.83
LINK K K B1162 O HOH B2016 1555 1555 2.60
LINK K K B1162 O HOH B2019 1555 1555 2.70
LINK K K B1163 O HOH B2107 1555 1555 2.66
LINK K K B1163 O LEU E 156 1555 2656 2.81
LINK K K B1163 O ARG E 157 1555 2656 3.09
LINK K K B1163 O HOH E2113 1555 2656 2.58
LINK O ALA C 70 K K C1161 1555 1555 2.66
LINK O HIS C 73 K K C1161 1555 1555 2.71
LINK O ARG C 84 K K C1162 1555 1555 2.69
LINK OG1 THR C 110 K K C1161 1555 1555 2.75
LINK O ASN C 120 K K C1162 1555 1555 2.75
LINK O GLU C 155 K K D1163 2656 1555 3.70
LINK O LEU C 156 K K D1163 2656 1555 2.92
LINK O ARG C 157 K K D1163 2656 1555 2.91
LINK K K C1161 O HOH C2012 1555 1555 2.65
LINK K K C1161 O HOH C2032 1555 1555 2.74
LINK K K C1161 O HOH C2059 1555 1555 2.77
LINK K K C1162 O HOH C2040 1555 1555 2.78
LINK O HOH C2081 K K D1163 2656 1555 2.83
LINK O ALA D 34 K K D1162 1555 1555 2.68
LINK O ALA D 70 K K D1161 1555 1555 2.68
LINK O HIS D 73 K K D1161 1555 1555 2.67
LINK O ARG D 84 K K D1164 1555 1555 2.71
LINK OG1 THR D 110 K K D1161 1555 1555 2.76
LINK O ASN D 120 K K D1164 1555 1555 2.78
LINK O ALA D 129 K K D1162 1555 1555 2.97
LINK O GLY D 130 K K D1162 1555 1555 2.71
LINK OD2 ASP D 137 K K D1162 1555 1555 2.78
LINK O GLU D 155 K K D1163 1555 1555 3.71
LINK O LEU D 156 K K D1163 1555 1555 2.77
LINK O ARG D 157 K K D1163 1555 1555 3.06
LINK K K D1161 O HOH D2026 1555 1555 2.74
LINK K K D1161 O HOH D2058 1555 1555 2.75
LINK K K D1161 O HOH D2088 1555 1555 2.87
LINK K K D1162 O HOH D2017 1555 1555 2.70
LINK K K D1162 O HOH D2018 1555 1555 3.22
LINK K K D1163 O HOH D2115 1555 1555 2.78
LINK O ALA E 34 K K E1162 1555 1555 2.69
LINK O ALA E 70 K K E1161 1555 1555 2.63
LINK O HIS E 73 K K E1161 1555 1555 2.70
LINK O ARG E 84 K K E1163 1555 1555 2.66
LINK OG1 THR E 110 K K E1161 1555 1555 2.76
LINK O ASN E 120 K K E1163 1555 1555 2.65
LINK O ALA E 129 K K E1162 1555 1555 2.96
LINK O GLY E 130 K K E1162 1555 1555 3.03
LINK OD2 ASP E 137 K K E1162 1555 1555 2.82
LINK K K E1161 O HOH E2026 1555 1555 2.67
LINK K K E1161 O HOH E2055 1555 1555 2.77
LINK K K E1161 O HOH E2080 1555 1555 3.29
LINK K K E1161 O HOH E2081 1555 1555 2.77
LINK K K E1162 O HOH E2019 1555 1555 3.16
LINK K K E1162 O HOH E2020 1555 1555 2.56
LINK K K E1163 O HOH E2063 1555 1555 2.81
CISPEP 1 HIS E 159 SER E 160 0 -5.54
SITE 1 AC1 6 ALA A 70 HIS A 73 THR A 110 HOH A2047
SITE 2 AC1 6 HOH A2050 HOH A2076
SITE 1 AC2 7 ALA A 34 GLY A 38 ALA A 129 GLY A 130
SITE 2 AC2 7 ASP A 137 HOH A2013 HOH B2022
SITE 1 AC3 4 GLU A 155 LEU A 156 ARG A 157 HOH A2112
SITE 1 AC4 2 ARG A 84 ASN A 120
SITE 1 AC5 6 ALA B 70 HIS B 73 THR B 110 HOH B2049
SITE 2 AC5 6 HOH B2054 HOH B2077
SITE 1 AC6 7 ALA B 34 GLY B 38 ALA B 129 GLY B 130
SITE 2 AC6 7 ASP B 137 HOH B2016 HOH B2019
SITE 1 AC7 7 GLU B 155 LEU B 156 ARG B 157 HOH B2107
SITE 2 AC7 7 LEU E 156 ARG E 157 HOH E2113
SITE 1 AC8 2 ARG B 84 ASN B 120
SITE 1 AC9 6 ALA C 70 HIS C 73 THR C 110 HOH C2012
SITE 2 AC9 6 HOH C2032 HOH C2059
SITE 1 BC1 3 ARG C 84 ASN C 120 HOH C2040
SITE 1 BC2 6 ALA D 70 HIS D 73 THR D 110 HOH D2026
SITE 2 BC2 6 HOH D2058 HOH D2088
SITE 1 BC3 5 ALA D 34 ALA D 129 GLY D 130 ASP D 137
SITE 2 BC3 5 HOH D2017
SITE 1 BC4 7 GLU C 155 LEU C 156 ARG C 157 HOH C2081
SITE 2 BC4 7 LEU D 156 ARG D 157 HOH D2115
SITE 1 BC5 2 ARG D 84 ASN D 120
SITE 1 BC6 6 ALA E 70 HIS E 73 THR E 110 HOH E2026
SITE 2 BC6 6 HOH E2055 HOH E2081
SITE 1 BC7 5 ALA E 34 ALA E 129 GLY E 130 ASP E 137
SITE 2 BC7 5 HOH E2020
SITE 1 BC8 3 ARG E 84 ASN E 120 HOH E2063
SITE 1 BC9 23 SER A 25 TRP A 27 HIS A 28 GLY A 58
SITE 2 BC9 23 ALA A 59 ILE A 60 GLU A 61 VAL A 81
SITE 3 BC9 23 VAL A 82 ILE A 83 GLY A 85 GLN A 86
SITE 4 BC9 23 THR A 87 HIS A 89 HOH A2055 HOH A2114
SITE 5 BC9 23 HOH A2115 HOH A2116 HOH A2117 ALA B 113
SITE 6 BC9 23 ASN B 114 ARG B 128 LYS B 138
SITE 1 CC1 22 SER B 25 TRP B 27 HIS B 28 GLY B 58
SITE 2 CC1 22 ALA B 59 ILE B 60 GLU B 61 VAL B 81
SITE 3 CC1 22 VAL B 82 ILE B 83 GLY B 85 GLN B 86
SITE 4 CC1 22 THR B 87 HIS B 89 HOH B2007 HOH B2109
SITE 5 CC1 22 HOH B2110 ALA C 113 ASN C 114 ARG C 128
SITE 6 CC1 22 LYS C 138 HOH C2073
SITE 1 CC2 22 TRP C 27 HIS C 28 GLY C 58 ALA C 59
SITE 2 CC2 22 ILE C 60 GLU C 61 VAL C 81 VAL C 82
SITE 3 CC2 22 ILE C 83 GLY C 85 GLN C 86 THR C 87
SITE 4 CC2 22 HIS C 89 HOH C2005 HOH C2082 HOH C2083
SITE 5 CC2 22 HOH C2084 HOH C2085 ALA D 113 ASN D 114
SITE 6 CC2 22 ARG D 128 LYS D 138
SITE 1 CC3 22 TRP D 27 HIS D 28 GLY D 58 ALA D 59
SITE 2 CC3 22 ILE D 60 GLU D 61 VAL D 81 VAL D 82
SITE 3 CC3 22 ILE D 83 GLY D 85 GLN D 86 THR D 87
SITE 4 CC3 22 HIS D 89 HOH D2047 HOH D2064 HOH D2118
SITE 5 CC3 22 HOH D2119 HOH D2120 ALA E 113 ASN E 114
SITE 6 CC3 22 ARG E 128 LYS E 138
SITE 1 CC4 21 ALA A 113 ASN A 114 ARG A 128 SER E 25
SITE 2 CC4 21 TRP E 27 HIS E 28 GLY E 58 ALA E 59
SITE 3 CC4 21 ILE E 60 GLU E 61 VAL E 81 VAL E 82
SITE 4 CC4 21 ILE E 83 ARG E 84 GLY E 85 GLN E 86
SITE 5 CC4 21 THR E 87 HOH E2114 HOH E2115 HOH E2116
SITE 6 CC4 21 HOH E2117
CRYST1 131.384 81.251 85.883 90.00 120.25 90.00 C 1 2 1 20
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 0.007611 0.000000 0.004439 0.00000
SCALE2 0.000000 0.012308 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013479 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
