HEADER TRANSFERASE 11-MAY-17 5XLW
TITLE MYCOBACTERIUM TUBERCULOSIS PANTOTHENATE KINASE MUTANT F247A/F254A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANTOTHENATE KINASE;
COMPND 3 CHAIN: B, A;
COMPND 4 SYNONYM: PANTOTHENIC ACID KINASE;
COMPND 5 EC: 2.7.1.33;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: COAA, RV1092C, MTV017.45C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VARIANT: DE3;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS HOMODIMER, COA BIOSYNTHESIS, NUCLEOTIDE BINDING, CONCERTED MOVEMENT,
KEYWDS 2 STRUCTURAL TRANSFORMATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PAUL,P.KUMAR,A.SUROLIA,M.VIJAYAN
REVDAT 3 22-NOV-23 5XLW 1 REMARK
REVDAT 2 05-DEC-18 5XLW 1 JRNL
REVDAT 1 16-MAY-18 5XLW 0
JRNL AUTH A.PAUL,P.KUMAR,A.SUROLIA,M.VIJAYAN
JRNL TITL BIOCHEMICAL AND STRUCTURAL STUDIES OF MUTANTS INDICATE
JRNL TITL 2 CONCERTED MOVEMENT OF THE DIMER INTERFACE AND LIGAND-BINDING
JRNL TITL 3 REGION OF MYCOBACTERIUM TUBERCULOSIS PANTOTHENATE KINASE
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 73 635 2017
JRNL REF 2 BIOL COMMUN
JRNL REFN ESSN 2053-230X
JRNL PMID 29095158
JRNL DOI 10.1107/S2053230X17015667
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.DAS,P.KUMAR,V.BHOR,A.SUROLIA,M.VIJAYAN
REMARK 1 TITL EXPRESSION, PURIFICATION, CRYSTALLIZATION AND PRELIMINARY
REMARK 1 TITL 2 X-RAY CRYSTALLOGRAPHIC ANALYSIS OF PANTOTHENATE KINASE FROM
REMARK 1 TITL 3 MYCOBACTERIUM TUBERCULOSIS.
REMARK 1 REF ACTA CRYSTALLOGR. SECT. F V. 61 65 2005
REMARK 1 REF 2 STRUCT. BIOL. CRYST. COMMUN.
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 16508093
REMARK 1 DOI 10.1107/S1744309104028040
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.DAS,P.KUMAR,V.BHOR,A.SUROLIA,M.VIJAYAN
REMARK 1 TITL INVARIANCE AND VARIABILITY IN BACTERIAL PANK: A STUDY BASED
REMARK 1 TITL 2 ON THE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PANK.
REMARK 1 REF ACTA CRYSTALLOGR. D BIOL. V. 62 628 2006
REMARK 1 REF 2 CRYSTALLOGR.
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 16699190
REMARK 1 DOI 10.1107/S0907444906012728
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.CHETNANI,S.DAS,P.KUMAR,A.SUROLIA,M.VIJAYAN
REMARK 1 TITL MYCOBACTERIUM TUBERCULOSIS PANTOTHENATE KINASE: POSSIBLE
REMARK 1 TITL 2 CHANGES IN LOCATION OF LIGANDS DURING ENZYME ACTION.
REMARK 1 REF ACTA CRYSTALLOGR. D BIOL. V. 65 312 2009
REMARK 1 REF 2 CRYSTALLOGR.
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 19307712
REMARK 1 DOI 10.1107/S0907444909002170
REMARK 1 REFERENCE 4
REMARK 1 AUTH B.CHETNANI,P.KUMAR,A.SUROLIA,M.VIJAYAN
REMARK 1 TITL M. TUBERCULOSIS PANTOTHENATE KINASE: DUAL SUBSTRATE
REMARK 1 TITL 2 SPECIFICITY AND UNUSUAL CHANGES IN LIGAND LOCATIONS.
REMARK 1 REF J. MOL. BIOL. V. 400 171 2010
REMARK 1 REFN ESSN 1089-8638
REMARK 1 PMID 20451532
REMARK 1 DOI 10.1016/J.JMB.2010.04.064
REMARK 1 REFERENCE 5
REMARK 1 AUTH B.CHETNANI,P.KUMAR,K.V.ABHINAV,M.CHHIBBER,A.SUROLIA,
REMARK 1 AUTH 2 M.VIJAYAN
REMARK 1 TITL LOCATION AND CONFORMATION OF PANTOTHENATE AND ITS
REMARK 1 TITL 2 DERIVATIVES IN MYCOBACTERIUM TUBERCULOSIS PANTOTHENATE
REMARK 1 TITL 3 KINASE: INSIGHTS INTO ENZYME ACTION.
REMARK 1 REF ACTA CRYSTALLOGR. D BIOL. V. 67 774 2011
REMARK 1 REF 2 CRYSTALLOGR.
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 21904030
REMARK 1 DOI 10.1107/S0907444911024462
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 46901
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2500
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) : 2.26
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.32
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3444
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 211
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4652
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 123
REMARK 3 SOLVENT ATOMS : 178
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.70000
REMARK 3 B22 (A**2) : -0.70000
REMARK 3 B33 (A**2) : 2.28000
REMARK 3 B12 (A**2) : -0.35000
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): 0.188
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.171
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.133
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.504
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4871 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4713 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6595 ; 2.045 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10747 ; 1.007 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 594 ; 6.634 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 220 ;32.445 ;22.455
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 754 ;19.252 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;18.123 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 748 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5413 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1140 ; 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): 2373 ; 3.962 ; 3.924
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2372 ; 3.957 ; 3.923
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2962 ; 5.815 ; 5.868
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2963 ; 5.815 ; 5.868
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2498 ; 4.858 ; 4.485
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2482 ; 4.856 ; 4.485
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3608 ; 7.312 ; 6.486
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5592 ; 9.693 ;32.095
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5592 ; 9.692 ;32.094
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5XLW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1300003740.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95372
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49403
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260
REMARK 200 RESOLUTION RANGE LOW (A) : 43.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.49800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
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: 2GEU
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% PEG 400, 2.0 M AMMONIUM SULPHATE,
REMARK 280 100MM HEPES SODIUM SALT, PH 7.5, MICROBATCH, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.48000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.96000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 84.96000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.48000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 LEU B 4
REMARK 465 SER B 5
REMARK 465 GLU B 6
REMARK 465 ARG B 243
REMARK 465 THR B 244
REMARK 465 THR B 245
REMARK 465 ALA B 246
REMARK 465 ALA B 247
REMARK 465 ALA B 248
REMARK 465 ASP B 249
REMARK 465 PRO B 250
REMARK 465 GLU B 251
REMARK 465 SER B 252
REMARK 465 HIS B 253
REMARK 465 ALA B 254
REMARK 465 HIS B 255
REMARK 465 HIS B 256
REMARK 465 TYR B 257
REMARK 465 ALA B 258
REMARK 465 ALA B 259
REMARK 465 PHE B 260
REMARK 465 SER B 261
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 LEU A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
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 ARG B 16 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 19 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 22 CG CD NE CZ NH1 NH2
REMARK 470 THR B 25 OG1 CG2
REMARK 470 GLU B 32 CG CD OE1 OE2
REMARK 470 ARG B 38 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 76 CG CD OE1 OE2
REMARK 470 GLN B 82 CG CD OE1 NE2
REMARK 470 ARG B 155 NE CZ NH1 NH2
REMARK 470 ARG B 160 NE CZ NH1 NH2
REMARK 470 THR B 208 OG1 CG2
REMARK 470 THR B 211 OG1 CG2
REMARK 470 LEU B 212 CG CD1 CD2
REMARK 470 LEU B 240 CG CD1 CD2
REMARK 470 MET B 242 CG SD CE
REMARK 470 ASP B 262 CG OD1 OD2
REMARK 470 GLN B 264 CG CD OE1 NE2
REMARK 470 ARG B 270 CZ NH1 NH2
REMARK 470 ARG A 16 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 22 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 51 CG CD OE1 OE2
REMARK 470 ARG A 58 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 82 CG CD OE1 NE2
REMARK 470 ARG A 156 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 160 CG CD NE CZ NH1 NH2
REMARK 470 THR A 211 OG1 CG2
REMARK 470 LEU A 212 CG CD1 CD2
REMARK 470 GLU A 229 CG CD OE1 OE2
REMARK 470 GLU A 251 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG A 310 O HOH A 501 2.11
REMARK 500 OH TYR A 10 O HOH A 502 2.14
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 ASP B 14 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 LEU A 222 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ASP A 299 CB - CA - C ANGL. DEV. = -15.2 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 THR B 25 129.83 67.99
REMARK 500 LEU B 27 71.67 54.60
REMARK 500 ASP B 45 134.08 -38.55
REMARK 500 THR B 211 -79.55 160.92
REMARK 500 ILE B 276 -61.86 -121.64
REMARK 500 ARG A 22 -95.66 -66.09
REMARK 500 MET A 23 -146.22 103.80
REMARK 500 SER A 24 -28.12 -160.97
REMARK 500 THR A 25 76.76 55.96
REMARK 500 PRO A 26 -83.80 -72.07
REMARK 500 THR A 30 155.55 -35.63
REMARK 500 HIS A 120 72.98 -150.68
REMARK 500 HIS A 194 62.03 38.59
REMARK 500 PRO A 210 -142.98 -70.85
REMARK 500 THR A 211 -83.66 -24.75
REMARK 500 ALA A 248 -25.39 163.61
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 EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 411
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5XLV RELATED DB: PDB
DBREF 5XLW B 1 312 UNP P9WPA7 COAA_MYCTU 1 312
DBREF 5XLW A 1 312 UNP P9WPA7 COAA_MYCTU 1 312
SEQADV 5XLW ALA B 247 UNP P9WPA7 PHE 247 ENGINEERED MUTATION
SEQADV 5XLW ALA B 254 UNP P9WPA7 PHE 254 ENGINEERED MUTATION
SEQADV 5XLW ALA A 247 UNP P9WPA7 PHE 247 ENGINEERED MUTATION
SEQADV 5XLW ALA A 254 UNP P9WPA7 PHE 254 ENGINEERED MUTATION
SEQRES 1 B 312 MET SER ARG LEU SER GLU PRO SER PRO TYR VAL GLU PHE
SEQRES 2 B 312 ASP ARG ARG GLN TRP ARG ALA LEU ARG MET SER THR PRO
SEQRES 3 B 312 LEU ALA LEU THR GLU GLU GLU LEU VAL GLY LEU ARG GLY
SEQRES 4 B 312 LEU GLY GLU GLN ILE ASP LEU LEU GLU VAL GLU GLU VAL
SEQRES 5 B 312 TYR LEU PRO LEU ALA ARG LEU ILE HIS LEU GLN VAL ALA
SEQRES 6 B 312 ALA ARG GLN ARG LEU PHE ALA ALA THR ALA GLU PHE LEU
SEQRES 7 B 312 GLY GLU PRO GLN GLN ASN PRO ASP ARG PRO VAL PRO PHE
SEQRES 8 B 312 ILE ILE GLY VAL ALA GLY SER VAL ALA VAL GLY LYS SER
SEQRES 9 B 312 THR THR ALA ARG VAL LEU GLN ALA LEU LEU ALA ARG TRP
SEQRES 10 B 312 ASP HIS HIS PRO ARG VAL ASP LEU VAL THR THR ASP GLY
SEQRES 11 B 312 PHE LEU TYR PRO ASN ALA GLU LEU GLN ARG ARG ASN LEU
SEQRES 12 B 312 MET HIS ARG LYS GLY PHE PRO GLU SER TYR ASN ARG ARG
SEQRES 13 B 312 ALA LEU MET ARG PHE VAL THR SER VAL LYS SER GLY SER
SEQRES 14 B 312 ASP TYR ALA CYS ALA PRO VAL TYR SER HIS LEU HIS TYR
SEQRES 15 B 312 ASP ILE ILE PRO GLY ALA GLU GLN VAL VAL ARG HIS PRO
SEQRES 16 B 312 ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN THR
SEQRES 17 B 312 GLY PRO THR LEU MET VAL SER ASP LEU PHE ASP PHE SER
SEQRES 18 B 312 LEU TYR VAL ASP ALA ARG ILE GLU ASP ILE GLU GLN TRP
SEQRES 19 B 312 TYR VAL SER ARG PHE LEU ALA MET ARG THR THR ALA ALA
SEQRES 20 B 312 ALA ASP PRO GLU SER HIS ALA HIS HIS TYR ALA ALA PHE
SEQRES 21 B 312 SER ASP SER GLN ALA VAL VAL ALA ALA ARG GLU ILE TRP
SEQRES 22 B 312 ARG THR ILE ASN ARG PRO ASN LEU VAL GLU ASN ILE LEU
SEQRES 23 B 312 PRO THR ARG PRO ARG ALA THR LEU VAL LEU ARG LYS ASP
SEQRES 24 B 312 ALA ASP HIS SER ILE ASN ARG LEU ARG LEU ARG LYS LEU
SEQRES 1 A 312 MET SER ARG LEU SER GLU PRO SER PRO TYR VAL GLU PHE
SEQRES 2 A 312 ASP ARG ARG GLN TRP ARG ALA LEU ARG MET SER THR PRO
SEQRES 3 A 312 LEU ALA LEU THR GLU GLU GLU LEU VAL GLY LEU ARG GLY
SEQRES 4 A 312 LEU GLY GLU GLN ILE ASP LEU LEU GLU VAL GLU GLU VAL
SEQRES 5 A 312 TYR LEU PRO LEU ALA ARG LEU ILE HIS LEU GLN VAL ALA
SEQRES 6 A 312 ALA ARG GLN ARG LEU PHE ALA ALA THR ALA GLU PHE LEU
SEQRES 7 A 312 GLY GLU PRO GLN GLN ASN PRO ASP ARG PRO VAL PRO PHE
SEQRES 8 A 312 ILE ILE GLY VAL ALA GLY SER VAL ALA VAL GLY LYS SER
SEQRES 9 A 312 THR THR ALA ARG VAL LEU GLN ALA LEU LEU ALA ARG TRP
SEQRES 10 A 312 ASP HIS HIS PRO ARG VAL ASP LEU VAL THR THR ASP GLY
SEQRES 11 A 312 PHE LEU TYR PRO ASN ALA GLU LEU GLN ARG ARG ASN LEU
SEQRES 12 A 312 MET HIS ARG LYS GLY PHE PRO GLU SER TYR ASN ARG ARG
SEQRES 13 A 312 ALA LEU MET ARG PHE VAL THR SER VAL LYS SER GLY SER
SEQRES 14 A 312 ASP TYR ALA CYS ALA PRO VAL TYR SER HIS LEU HIS TYR
SEQRES 15 A 312 ASP ILE ILE PRO GLY ALA GLU GLN VAL VAL ARG HIS PRO
SEQRES 16 A 312 ASP ILE LEU ILE LEU GLU GLY LEU ASN VAL LEU GLN THR
SEQRES 17 A 312 GLY PRO THR LEU MET VAL SER ASP LEU PHE ASP PHE SER
SEQRES 18 A 312 LEU TYR VAL ASP ALA ARG ILE GLU ASP ILE GLU GLN TRP
SEQRES 19 A 312 TYR VAL SER ARG PHE LEU ALA MET ARG THR THR ALA ALA
SEQRES 20 A 312 ALA ASP PRO GLU SER HIS ALA HIS HIS TYR ALA ALA PHE
SEQRES 21 A 312 SER ASP SER GLN ALA VAL VAL ALA ALA ARG GLU ILE TRP
SEQRES 22 A 312 ARG THR ILE ASN ARG PRO ASN LEU VAL GLU ASN ILE LEU
SEQRES 23 A 312 PRO THR ARG PRO ARG ALA THR LEU VAL LEU ARG LYS ASP
SEQRES 24 A 312 ALA ASP HIS SER ILE ASN ARG LEU ARG LEU ARG LYS LEU
HET EDO B 401 4
HET EDO B 402 4
HET EDO B 403 4
HET EDO B 404 4
HET EDO B 405 4
HET EDO B 406 4
HET EDO B 407 4
HET EDO B 408 4
HET EDO B 409 4
HET EDO B 410 4
HET EDO B 411 4
HET EDO B 412 4
HET 1PE B 413 16
HET SO4 B 414 5
HET SO4 B 415 5
HET PEG A 401 7
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 4
HET EDO A 409 4
HET SO4 A 410 5
HET SO4 A 411 5
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 EDO 20(C2 H6 O2)
FORMUL 15 1PE C10 H22 O6
FORMUL 16 SO4 4(O4 S 2-)
FORMUL 18 PEG C4 H10 O3
FORMUL 29 HOH *178(H2 O)
HELIX 1 AA1 ARG B 15 ALA B 20 1 6
HELIX 2 AA2 THR B 30 LEU B 40 1 11
HELIX 3 AA3 ASP B 45 VAL B 52 1 8
HELIX 4 AA4 VAL B 52 GLY B 79 1 28
HELIX 5 AA5 GLY B 102 ALA B 115 1 14
HELIX 6 AA6 ASP B 129 LEU B 132 5 4
HELIX 7 AA7 PRO B 134 ARG B 141 1 8
HELIX 8 AA8 LEU B 143 LYS B 147 5 5
HELIX 9 AA9 PHE B 149 TYR B 153 5 5
HELIX 10 AB1 ASN B 154 SER B 167 1 14
HELIX 11 AB2 MET B 213 PHE B 218 5 6
HELIX 12 AB3 ARG B 227 MET B 242 1 16
HELIX 13 AB4 SER B 263 ILE B 276 1 14
HELIX 14 AB5 ILE B 276 ILE B 285 1 10
HELIX 15 AB6 LEU B 286 ALA B 292 5 7
HELIX 16 AB7 ARG A 15 ALA A 20 1 6
HELIX 17 AB8 THR A 30 ARG A 38 1 9
HELIX 18 AB9 GLY A 39 GLY A 41 5 3
HELIX 19 AC1 ASP A 45 VAL A 52 1 8
HELIX 20 AC2 VAL A 52 GLY A 79 1 28
HELIX 21 AC3 GLY A 102 ARG A 116 1 15
HELIX 22 AC4 ASP A 129 LEU A 132 5 4
HELIX 23 AC5 PRO A 134 ARG A 141 1 8
HELIX 24 AC6 LEU A 143 LYS A 147 5 5
HELIX 25 AC7 PHE A 149 TYR A 153 5 5
HELIX 26 AC8 ASN A 154 SER A 167 1 14
HELIX 27 AC9 MET A 213 PHE A 218 5 6
HELIX 28 AD1 ARG A 227 ALA A 247 1 21
HELIX 29 AD2 HIS A 255 PHE A 260 5 6
HELIX 30 AD3 SER A 261 ILE A 276 1 16
HELIX 31 AD4 ILE A 276 ILE A 285 1 10
HELIX 32 AD5 LEU A 286 ALA A 292 5 7
SHEET 1 AA1 7 TYR B 10 ASP B 14 0
SHEET 2 AA1 7 ILE B 304 ARG B 310 -1 O LEU B 309 N VAL B 11
SHEET 3 AA1 7 LEU B 294 LYS B 298 -1 N ARG B 297 O ARG B 306
SHEET 4 AA1 7 PHE B 220 ASP B 225 1 N ASP B 225 O LEU B 296
SHEET 5 AA1 7 PHE B 91 GLY B 97 1 N ALA B 96 O VAL B 224
SHEET 6 AA1 7 ILE B 197 GLU B 201 1 O LEU B 198 N PHE B 91
SHEET 7 AA1 7 VAL B 123 THR B 127 1 N VAL B 126 O ILE B 199
SHEET 1 AA2 2 ALA B 172 ALA B 174 0
SHEET 2 AA2 2 GLN B 190 VAL B 192 -1 O VAL B 192 N ALA B 172
SHEET 1 AA3 2 TYR B 177 SER B 178 0
SHEET 2 AA3 2 ASP B 183 ILE B 184 -1 O ASP B 183 N SER B 178
SHEET 1 AA4 7 TYR A 10 ASP A 14 0
SHEET 2 AA4 7 ILE A 304 ARG A 310 -1 O LEU A 309 N VAL A 11
SHEET 3 AA4 7 LEU A 294 LYS A 298 -1 N VAL A 295 O ARG A 308
SHEET 4 AA4 7 PHE A 220 ASP A 225 1 N ASP A 225 O LEU A 296
SHEET 5 AA4 7 PHE A 91 ALA A 96 1 N ALA A 96 O VAL A 224
SHEET 6 AA4 7 ILE A 197 GLU A 201 1 O LEU A 200 N ILE A 93
SHEET 7 AA4 7 VAL A 123 THR A 127 1 N ASP A 124 O ILE A 199
SHEET 1 AA5 2 ALA A 172 SER A 178 0
SHEET 2 AA5 2 ASP A 183 VAL A 192 -1 O ASP A 183 N SER A 178
SITE 1 AC1 4 SER B 164 TYR B 171 ALA B 172 CYS B 173
SITE 1 AC2 7 LEU B 138 GLN B 139 ASN B 142 LEU B 143
SITE 2 AC2 7 MET B 144 HIS B 145 HOH B 502
SITE 1 AC3 5 ASN B 204 LEU B 212 MET B 213 VAL B 214
SITE 2 AC3 5 HOH B 571
SITE 1 AC4 3 SER B 169 ASP B 170 TYR B 171
SITE 1 AC5 9 VAL B 126 THR B 127 GLY B 130 PRO B 175
SITE 2 AC5 9 VAL B 176 TYR B 177 GLN B 190 HOH B 510
SITE 3 AC5 9 HOH B 527
SITE 1 AC6 5 SER B 215 PHE B 220 SER B 221 ARG B 291
SITE 2 AC6 5 THR B 293
SITE 1 AC7 5 ALA B 157 CYS B 173 PRO B 175 EDO B 411
SITE 2 AC7 5 HOH B 553
SITE 1 AC8 4 ARG B 289 ARG B 306 ARG B 308 HOH B 528
SITE 1 AC9 5 ASP A 249 TYR B 177 HIS B 179 LEU B 180
SITE 2 AC9 5 HOH B 516
SITE 1 AD1 4 VAL B 99 ARG B 238 1PE B 413 HOH B 519
SITE 1 AD2 3 ARG B 160 EDO B 407 EDO B 412
SITE 1 AD3 2 ASN B 154 EDO B 411
SITE 1 AD4 8 ASP B 129 LYS B 147 HIS B 179 TYR B 182
SITE 2 AD4 8 TYR B 235 ASN B 277 EDO B 410 HOH B 519
SITE 1 AD5 9 SER B 98 ALA B 100 VAL B 101 GLY B 102
SITE 2 AD5 9 LYS B 103 SER B 104 ARG B 238 HOH B 547
SITE 3 AD5 9 HOH B 550
SITE 1 AD6 3 PRO B 85 ASP B 86 ARG B 87
SITE 1 AD7 1 ASN A 277
SITE 1 AD8 5 SER A 215 PHE A 220 SER A 221 ARG A 291
SITE 2 AD8 5 THR A 293
SITE 1 AD9 3 ARG A 289 ARG A 306 HOH A 509
SITE 1 AE1 3 THR A 105 LYS A 298 HIS A 302
SITE 1 AE2 1 GLN A 17
SITE 1 AE3 4 TYR A 10 ARG A 289 PRO A 290 HOH A 507
SITE 1 AE4 4 ASN A 142 GLN A 207 THR A 208 HOH A 523
SITE 1 AE5 2 PRO A 7 LYS A 311
SITE 1 AE6 1 SER A 104
SITE 1 AE7 3 PRO A 85 ASP A 86 ARG A 87
SITE 1 AE8 10 SER A 98 VAL A 99 ALA A 100 VAL A 101
SITE 2 AE8 10 GLY A 102 LYS A 103 SER A 104 ARG A 238
SITE 3 AE8 10 HOH A 531 HOH A 540
CRYST1 119.330 119.330 127.440 90.00 90.00 120.00 P 31 2 1 12
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 0.008380 0.004838 0.000000 0.00000
SCALE2 0.000000 0.009677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007847 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
