HEADER ISOMERASE 18-MAY-11 3S46
TITLE THE CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM STREPTOCOCCUS
TITLE 2 PNEUMONIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALANINE RACEMASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 5.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 1313;
SOURCE 4 STRAIN: R800;
SOURCE 5 GENE: ALAR, ALR, SP_1698;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET17
KEYWDS ALPHA/BETA BARREL, EXTENDED BETA-STRAND DOMAIN, PYRIDOXAL PHOSPHATE
KEYWDS 2 COFACTOR, ALANINE RACEMASE, CARBAMYLATED LYSINE, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.IM,M.L.SHARPE,U.STRYCH,M.DAVLIEVA,K.L.KRAUSE
REVDAT 1 22-JUN-11 3S46 0
SPRSDE 22-JUN-11 3S46 3MUB
JRNL AUTH H.IM,M.L.SHARPE,U.STRYCH,M.DAVLIEVA,K.L.KRAUSE
JRNL TITL THE CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM STREPTOCOCCUS
JRNL TITL 2 PNEUMONIAE, A TARGET FOR STRUCTURE-BASED DRUG DESIGN.
JRNL REF BMC MICROBIOL. V. 11 116 2011
JRNL REFN ESSN 1471-2180
JRNL PMID 21612658
JRNL DOI 10.1186/1471-2180-11-116
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 63336
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3379
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4412
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE SET COUNT : 236
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5638
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 507
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.27000
REMARK 3 B12 (A**2) : 0.09000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.274
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5758 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7837 ; 1.448 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 732 ; 5.731 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 243 ;38.010 ;24.938
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 953 ;13.905 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;16.374 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 917 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4311 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 3646 ; 0.668 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5874 ; 1.186 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2112 ; 2.035 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1962 ; 3.082 ; 4.500
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 367
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7980 64.3680 -19.1930
REMARK 3 T TENSOR
REMARK 3 T11: 0.1384 T22: 0.2189
REMARK 3 T33: 0.3094 T12: 0.0561
REMARK 3 T13: -0.0476 T23: 0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 1.4797 L22: 0.3420
REMARK 3 L33: 1.2513 L12: 0.1629
REMARK 3 L13: 0.4969 L23: -0.0940
REMARK 3 S TENSOR
REMARK 3 S11: -0.1776 S12: 0.1654 S13: 0.1991
REMARK 3 S21: -0.0308 S22: -0.0144 S23: -0.0338
REMARK 3 S31: -0.2291 S32: 0.1903 S33: 0.1920
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 367
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2140 64.6770 -1.3690
REMARK 3 T TENSOR
REMARK 3 T11: 0.1384 T22: 0.4070
REMARK 3 T33: 0.2788 T12: 0.2197
REMARK 3 T13: -0.0577 T23: -0.1185
REMARK 3 L TENSOR
REMARK 3 L11: 1.7892 L22: 0.4369
REMARK 3 L33: 1.3413 L12: 0.1244
REMARK 3 L13: 0.6816 L23: -0.0277
REMARK 3 S TENSOR
REMARK 3 S11: -0.2014 S12: -0.5622 S13: 0.2217
REMARK 3 S21: 0.0233 S22: -0.0116 S23: 0.0513
REMARK 3 S31: -0.2549 S32: -0.4431 S33: 0.2130
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3S46 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-11.
REMARK 100 THE RCSB ID CODE IS RCSB065738.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66748
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 23.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1SFT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M NA CITRATE, 0.1M MES, 10%
REMARK 280 GLYCEROL, PH 7.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 39.36633
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 78.73267
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 78.73267
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 39.36633
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: 6060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 347 NE - CZ - NH2 ANGL. DEV. = -3.1 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 LLP A 40 152.19 -39.14
REMARK 500 GLU A 118 49.78 -92.61
REMARK 500 ARG A 136 -77.77 -101.86
REMARK 500 THR A 168 31.42 -141.49
REMARK 500 ALA A 200 -16.31 -153.64
REMARK 500 PHE A 214 -122.68 -94.75
REMARK 500 SER A 247 -156.29 -151.61
REMARK 500 ASN A 292 -3.14 76.54
REMARK 500 THR A 349 -159.41 -136.74
REMARK 500 GLU B 91 28.45 -73.09
REMARK 500 ASP B 100 65.69 74.04
REMARK 500 ARG B 136 -78.84 -98.60
REMARK 500 ALA B 200 -10.61 -146.01
REMARK 500 PHE B 214 -118.80 -94.36
REMARK 500 SER B 247 -159.96 -150.64
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 A 418 DISTANCE = 5.24 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ A 369
DBREF 3S46 A 1 367 UNP P0A2W8 ALR_STRPN 1 367
DBREF 3S46 B 1 367 UNP P0A2W8 ALR_STRPN 1 367
SEQRES 1 A 367 MET LYS ALA SER PRO HIS ARG PRO THR LYS ALA LEU ILE
SEQRES 2 A 367 HIS LEU GLY ALA ILE ARG GLN ASN ILE GLN GLN MET GLY
SEQRES 3 A 367 ALA HIS ILE PRO GLN GLY THR LEU LYS LEU ALA VAL VAL
SEQRES 4 A 367 LLP ALA ASN ALA TYR GLY HIS GLY ALA VAL ALA VAL ALA
SEQRES 5 A 367 LYS ALA ILE GLN ASP ASP VAL ASP GLY PHE CYS VAL SER
SEQRES 6 A 367 ASN ILE ASP GLU ALA ILE GLU LEU ARG GLN ALA GLY LEU
SEQRES 7 A 367 SER LYS PRO ILE LEU ILE LEU GLY VAL SER GLU ILE GLU
SEQRES 8 A 367 ALA VAL ALA LEU ALA LYS GLU TYR ASP PHE THR LEU THR
SEQRES 9 A 367 VAL ALA GLY LEU GLU TRP ILE GLN ALA LEU LEU ASP LYS
SEQRES 10 A 367 GLU VAL ASP LEU THR GLY LEU THR VAL HIS LEU KCX ILE
SEQRES 11 A 367 ASP SER GLY MET GLY ARG ILE GLY PHE ARG GLU ALA SER
SEQRES 12 A 367 GLU VAL GLU GLN ALA GLN ASP LEU LEU GLN GLN HIS GLY
SEQRES 13 A 367 VAL CYS VAL GLU GLY ILE PHE THR HIS PHE ALA THR ALA
SEQRES 14 A 367 ASP GLU GLU SER ASP ASP TYR PHE ASN ALA GLN LEU GLU
SEQRES 15 A 367 ARG PHE LYS THR ILE LEU ALA SER MET LYS GLU VAL PRO
SEQRES 16 A 367 GLU LEU VAL HIS ALA SER ASN SER ALA THR THR LEU TRP
SEQRES 17 A 367 HIS VAL GLU THR ILE PHE ASN ALA VAL ARG MET GLY ASP
SEQRES 18 A 367 ALA MET TYR GLY LEU ASN PRO SER GLY ALA VAL LEU ASP
SEQRES 19 A 367 LEU PRO TYR ASP LEU ILE PRO ALA LEU THR LEU GLU SER
SEQRES 20 A 367 ALA LEU VAL HIS VAL LYS THR VAL PRO ALA GLY ALA CYS
SEQRES 21 A 367 MET GLY TYR GLY ALA THR TYR GLN ALA ASP SER GLU GLN
SEQRES 22 A 367 VAL ILE ALA THR VAL PRO ILE GLY TYR ALA ASP GLY TRP
SEQRES 23 A 367 THR ARG ASP MET GLN ASN PHE SER VAL LEU VAL ASP GLY
SEQRES 24 A 367 GLN ALA CYS PRO ILE VAL GLY ARG VAL SER MET ASP GLN
SEQRES 25 A 367 ILE THR ILE ARG LEU PRO LYS LEU TYR PRO LEU GLY THR
SEQRES 26 A 367 LYS VAL THR LEU ILE GLY SER ASN GLY ASP LYS GLU ILE
SEQRES 27 A 367 THR ALA THR GLN VAL ALA THR TYR ARG VAL THR ILE ASN
SEQRES 28 A 367 TYR GLU VAL VAL CYS LEU LEU SER ASP ARG ILE PRO ARG
SEQRES 29 A 367 GLU TYR TYR
SEQRES 1 B 367 MET LYS ALA SER PRO HIS ARG PRO THR LYS ALA LEU ILE
SEQRES 2 B 367 HIS LEU GLY ALA ILE ARG GLN ASN ILE GLN GLN MET GLY
SEQRES 3 B 367 ALA HIS ILE PRO GLN GLY THR LEU LYS LEU ALA VAL VAL
SEQRES 4 B 367 LLP ALA ASN ALA TYR GLY HIS GLY ALA VAL ALA VAL ALA
SEQRES 5 B 367 LYS ALA ILE GLN ASP ASP VAL ASP GLY PHE CYS VAL SER
SEQRES 6 B 367 ASN ILE ASP GLU ALA ILE GLU LEU ARG GLN ALA GLY LEU
SEQRES 7 B 367 SER LYS PRO ILE LEU ILE LEU GLY VAL SER GLU ILE GLU
SEQRES 8 B 367 ALA VAL ALA LEU ALA LYS GLU TYR ASP PHE THR LEU THR
SEQRES 9 B 367 VAL ALA GLY LEU GLU TRP ILE GLN ALA LEU LEU ASP LYS
SEQRES 10 B 367 GLU VAL ASP LEU THR GLY LEU THR VAL HIS LEU KCX ILE
SEQRES 11 B 367 ASP SER GLY MET GLY ARG ILE GLY PHE ARG GLU ALA SER
SEQRES 12 B 367 GLU VAL GLU GLN ALA GLN ASP LEU LEU GLN GLN HIS GLY
SEQRES 13 B 367 VAL CYS VAL GLU GLY ILE PHE THR HIS PHE ALA THR ALA
SEQRES 14 B 367 ASP GLU GLU SER ASP ASP TYR PHE ASN ALA GLN LEU GLU
SEQRES 15 B 367 ARG PHE LYS THR ILE LEU ALA SER MET LYS GLU VAL PRO
SEQRES 16 B 367 GLU LEU VAL HIS ALA SER ASN SER ALA THR THR LEU TRP
SEQRES 17 B 367 HIS VAL GLU THR ILE PHE ASN ALA VAL ARG MET GLY ASP
SEQRES 18 B 367 ALA MET TYR GLY LEU ASN PRO SER GLY ALA VAL LEU ASP
SEQRES 19 B 367 LEU PRO TYR ASP LEU ILE PRO ALA LEU THR LEU GLU SER
SEQRES 20 B 367 ALA LEU VAL HIS VAL LYS THR VAL PRO ALA GLY ALA CYS
SEQRES 21 B 367 MET GLY TYR GLY ALA THR TYR GLN ALA ASP SER GLU GLN
SEQRES 22 B 367 VAL ILE ALA THR VAL PRO ILE GLY TYR ALA ASP GLY TRP
SEQRES 23 B 367 THR ARG ASP MET GLN ASN PHE SER VAL LEU VAL ASP GLY
SEQRES 24 B 367 GLN ALA CYS PRO ILE VAL GLY ARG VAL SER MET ASP GLN
SEQRES 25 B 367 ILE THR ILE ARG LEU PRO LYS LEU TYR PRO LEU GLY THR
SEQRES 26 B 367 LYS VAL THR LEU ILE GLY SER ASN GLY ASP LYS GLU ILE
SEQRES 27 B 367 THR ALA THR GLN VAL ALA THR TYR ARG VAL THR ILE ASN
SEQRES 28 B 367 TYR GLU VAL VAL CYS LEU LEU SER ASP ARG ILE PRO ARG
SEQRES 29 B 367 GLU TYR TYR
MODRES 3S46 LLP A 40 LYS
MODRES 3S46 KCX A 129 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3S46 LLP B 40 LYS
MODRES 3S46 KCX B 129 LYS LYSINE NZ-CARBOXYLIC ACID
HET LLP A 40 24
HET KCX A 129 12
HET LLP B 40 24
HET KCX B 129 12
HET BEZ A 369 9
HETNAM LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-
HETNAM 2 LLP PYRIDIN-4-YLMETHANE)
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM BEZ BENZOIC ACID
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL 1 LLP 2(C14 H24 N3 O7 P)
FORMUL 1 KCX 2(C7 H14 N2 O4)
FORMUL 3 BEZ C7 H6 O2
FORMUL 4 HOH *507(H2 O)
HELIX 1 1 LEU A 15 HIS A 28 1 14
HELIX 2 2 VAL A 39 GLY A 45 1 7
HELIX 3 3 GLY A 47 GLN A 56 1 10
HELIX 4 4 ASP A 57 VAL A 59 5 3
HELIX 5 5 ASN A 66 ALA A 76 1 11
HELIX 6 6 GLU A 89 GLU A 91 5 3
HELIX 7 7 ALA A 92 TYR A 99 1 8
HELIX 8 8 GLY A 107 LYS A 117 1 11
HELIX 9 9 GLU A 141 HIS A 155 1 15
HELIX 10 10 ASP A 174 SER A 190 1 17
HELIX 11 11 ASN A 202 HIS A 209 1 8
HELIX 12 12 VAL A 210 ILE A 213 5 4
HELIX 13 13 GLY A 220 GLY A 225 5 6
HELIX 14 14 GLY A 262 THR A 266 5 5
HELIX 15 15 GLY A 281 GLY A 285 5 5
HELIX 16 16 THR A 287 GLN A 291 5 5
HELIX 17 17 THR A 339 VAL A 348 1 10
HELIX 18 18 ILE A 350 LEU A 357 1 8
HELIX 19 19 LEU B 15 HIS B 28 1 14
HELIX 20 20 VAL B 39 GLY B 45 1 7
HELIX 21 21 GLY B 47 GLN B 56 1 10
HELIX 22 22 ASP B 57 VAL B 59 5 3
HELIX 23 23 ASN B 66 GLY B 77 1 12
HELIX 24 24 GLU B 89 GLU B 91 5 3
HELIX 25 25 ALA B 92 ASP B 100 1 9
HELIX 26 26 GLY B 107 LYS B 117 1 11
HELIX 27 27 GLU B 141 HIS B 155 1 15
HELIX 28 28 ASP B 174 MET B 191 1 18
HELIX 29 29 ASN B 202 HIS B 209 1 8
HELIX 30 30 VAL B 210 ILE B 213 5 4
HELIX 31 31 GLY B 262 THR B 266 5 5
HELIX 32 32 GLY B 281 GLY B 285 5 5
HELIX 33 33 THR B 287 GLN B 291 5 5
HELIX 34 34 THR B 339 VAL B 348 1 10
HELIX 35 35 ILE B 350 LEU B 357 1 8
SHEET 1 A 5 LYS A 336 ILE A 338 0
SHEET 2 A 5 LYS A 326 ASN A 333 -1 N GLY A 331 O ILE A 338
SHEET 3 A 5 LEU A 243 ALA A 248 -1 N LEU A 245 O LEU A 329
SHEET 4 A 5 LYS A 10 HIS A 14 -1 N LYS A 10 O GLU A 246
SHEET 5 A 5 ARG A 364 TYR A 367 1 O TYR A 367 N ILE A 13
SHEET 1 B 9 LEU A 34 VAL A 38 0
SHEET 2 B 9 GLY A 61 VAL A 64 1 O GLY A 61 N ALA A 37
SHEET 3 B 9 ILE A 82 VAL A 87 1 O LEU A 85 N VAL A 64
SHEET 4 B 9 THR A 102 VAL A 105 1 O THR A 102 N ILE A 84
SHEET 5 B 9 THR A 125 ILE A 130 1 O HIS A 127 N VAL A 105
SHEET 6 B 9 CYS A 158 THR A 164 1 O PHE A 163 N ILE A 130
SHEET 7 B 9 LEU A 197 SER A 201 1 O LEU A 197 N GLU A 160
SHEET 8 B 9 ALA A 216 MET A 219 1 O ARG A 218 N SER A 201
SHEET 9 B 9 LEU A 34 VAL A 38 1 N VAL A 38 O MET A 219
SHEET 1 C 3 HIS A 251 VAL A 255 0
SHEET 2 C 3 GLN A 273 VAL A 278 -1 O GLN A 273 N VAL A 255
SHEET 3 C 3 ILE A 313 LEU A 317 -1 O ILE A 315 N ALA A 276
SHEET 1 D 2 CYS A 260 MET A 261 0
SHEET 2 D 2 TYR A 267 GLN A 268 -1 O TYR A 267 N MET A 261
SHEET 1 E 2 SER A 294 VAL A 297 0
SHEET 2 E 2 GLN A 300 PRO A 303 -1 O CYS A 302 N VAL A 295
SHEET 1 F 5 LYS B 336 ILE B 338 0
SHEET 2 F 5 LYS B 326 ASN B 333 -1 N ASN B 333 O LYS B 336
SHEET 3 F 5 LEU B 243 ALA B 248 -1 N SER B 247 O VAL B 327
SHEET 4 F 5 LYS B 10 HIS B 14 -1 N LYS B 10 O GLU B 246
SHEET 5 F 5 ARG B 364 TYR B 367 1 O GLU B 365 N ILE B 13
SHEET 1 G 9 LEU B 34 VAL B 38 0
SHEET 2 G 9 GLY B 61 VAL B 64 1 O CYS B 63 N ALA B 37
SHEET 3 G 9 ILE B 82 ILE B 84 1 O LEU B 83 N PHE B 62
SHEET 4 G 9 THR B 102 VAL B 105 1 O THR B 102 N ILE B 82
SHEET 5 G 9 THR B 125 KCX B 129 1 O KCX B 129 N VAL B 105
SHEET 6 G 9 CYS B 158 PHE B 163 1 O GLY B 161 N LEU B 128
SHEET 7 G 9 LEU B 197 SER B 201 1 O LEU B 197 N ILE B 162
SHEET 8 G 9 ALA B 216 MET B 219 1 O ARG B 218 N SER B 201
SHEET 9 G 9 LEU B 34 VAL B 38 1 N LEU B 36 O VAL B 217
SHEET 1 H 3 HIS B 251 VAL B 255 0
SHEET 2 H 3 GLN B 273 VAL B 278 -1 O THR B 277 N HIS B 251
SHEET 3 H 3 ILE B 313 LEU B 317 -1 O ILE B 315 N ALA B 276
SHEET 1 I 2 CYS B 260 MET B 261 0
SHEET 2 I 2 TYR B 267 GLN B 268 -1 O TYR B 267 N MET B 261
SHEET 1 J 2 SER B 294 VAL B 297 0
SHEET 2 J 2 GLN B 300 PRO B 303 -1 O CYS B 302 N VAL B 295
LINK C LLP A 40 N ALA A 41 1555 1555 1.55
LINK C LEU A 128 N KCX A 129 1555 1555 1.34
LINK C KCX A 129 N ILE A 130 1555 1555 1.33
LINK C LLP B 40 N ALA B 41 1555 1555 1.34
LINK C LEU B 128 N KCX B 129 1555 1555 1.33
LINK C KCX B 129 N ILE B 130 1555 1555 1.33
SITE 1 AC1 9 HIS A 28 ILE A 29 PRO A 30 GLU B 141
SITE 2 AC1 9 ALA B 142 ARG B 183 THR B 186 HOH B 393
SITE 3 AC1 9 HOH B 453
CRYST1 119.973 119.973 118.099 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 0.008335 0.004812 0.000000 0.00000
SCALE2 0.000000 0.009625 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008467 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
