HEADER ISOMERASE 30-NOV-09 3KW3
TITLE CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM BARTONELLA HENSELAE WITH
TITLE 2 COVALENTLY BOUND PYRIDOXAL PHOSPHATE
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: BARTONELLA HENSELAE;
SOURCE 3 ORGANISM_COMMON: ROCHALIMAEA HENSELAE;
SOURCE 4 ORGANISM_TAXID: 38323;
SOURCE 5 GENE: ALR, BH12810;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS NIAID, SSGCID, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS
KEYWDS 2 DISEASE, IODIDE SOAK, ALANINE RACEMASE, LLP, CAT-SCRATCH DISEASE,
KEYWDS 3 ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 6 22-NOV-23 3KW3 1 REMARK
REVDAT 5 06-SEP-23 3KW3 1 SEQADV LINK
REVDAT 4 20-SEP-17 3KW3 1 REMARK
REVDAT 3 20-JUL-11 3KW3 1 JRNL
REVDAT 2 13-JUL-11 3KW3 1 VERSN JRNL
REVDAT 1 22-DEC-09 3KW3 0
JRNL AUTH J.ABENDROTH,A.S.GARDBERG,J.I.ROBINSON,J.S.CHRISTENSEN,
JRNL AUTH 2 B.L.STAKER,P.J.MYLER,L.J.STEWART,T.E.EDWARDS
JRNL TITL SAD PHASING USING IODIDE IONS IN A HIGH-THROUGHPUT
JRNL TITL 2 STRUCTURAL GENOMICS ENVIRONMENT.
JRNL REF J.STRUCT.FUNCT.GENOM. V. 12 83 2011
JRNL REFN ISSN 1345-711X
JRNL PMID 21359836
JRNL DOI 10.1007/S10969-011-9101-7
REMARK 2
REMARK 2 RESOLUTION. 2.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 45875
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 : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2318
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) : 2.04
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2767
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 148
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5407
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 426
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.82000
REMARK 3 B22 (A**2) : -1.01000
REMARK 3 B33 (A**2) : 0.40000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.88000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.216
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.179
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.130
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.904
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
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): 5574 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7598 ; 1.408 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 710 ; 6.391 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 220 ;37.335 ;24.182
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 914 ;15.135 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;16.392 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 876 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4166 ; 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): 3526 ; 0.664 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5695 ; 1.167 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2048 ; 1.954 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1898 ; 3.061 ; 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 : 2
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 13 A 372
REMARK 3 RESIDUE RANGE : A 373 A 569
REMARK 3 ORIGIN FOR THE GROUP (A): 60.5882 50.4368 34.2100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0483 T22: 0.0587
REMARK 3 T33: 0.0833 T12: -0.0263
REMARK 3 T13: 0.0176 T23: 0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 1.2089 L22: 0.5683
REMARK 3 L33: 1.1781 L12: -0.1464
REMARK 3 L13: 0.6519 L23: -0.2975
REMARK 3 S TENSOR
REMARK 3 S11: -0.0629 S12: 0.1010 S13: 0.1888
REMARK 3 S21: 0.0179 S22: -0.0742 S23: -0.0849
REMARK 3 S31: -0.1672 S32: 0.2235 S33: 0.1371
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 14 B 372
REMARK 3 RESIDUE RANGE : B 373 B 601
REMARK 3 ORIGIN FOR THE GROUP (A): 43.7773 30.1931 24.4218
REMARK 3 T TENSOR
REMARK 3 T11: 0.0646 T22: 0.0135
REMARK 3 T33: 0.0662 T12: 0.0008
REMARK 3 T13: 0.0060 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 0.6745 L22: 0.6478
REMARK 3 L33: 1.4131 L12: 0.0831
REMARK 3 L13: 0.6250 L23: 0.1110
REMARK 3 S TENSOR
REMARK 3 S11: 0.0522 S12: -0.0086 S13: -0.0700
REMARK 3 S21: -0.1067 S22: 0.0357 S23: 0.1005
REMARK 3 S31: 0.1355 S32: -0.0207 S33: -0.0880
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: RESIDUAL ONLY
REMARK 4
REMARK 4 3KW3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056519.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-09; 16-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : ALS; ROTATING ANODE
REMARK 200 BEAMLINE : 5.0.3; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976484; 1.5418
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; RIGAKU SATURN
REMARK 200 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45971
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.040
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.49600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.790
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD, MR
REMARK 200 SOFTWARE USED: PHASER, SHELX, SHELXD
REMARK 200 STARTING MODEL: 2DY3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NATIVE CRYSTAL GROWN IN 0.1 M HEPES PH
REMARK 280 8.0, 33% PEG 3350 AT 42.3 MG/ML, CRYSTAL TRACKING ID 203636D11;
REMARK 280 CRYSTAL USED FOR COMBINED PHASER MR/IODOSAD GROWN IN 0.1 M HEPES
REMARK 280 PH 8.5, 0.2 M MGCL2, 25% PEG 3350 AND SOAKED FOR 1 HOUR IN 0.1 M
REMARK 280 HEPES PH 8.0, 1.0 M KI, 35% PEG 3350, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
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 68.39700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.15800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 68.39700
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.15800
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 LYS A 3
REMARK 465 SER A 4
REMARK 465 ALA A 5
REMARK 465 LYS A 6
REMARK 465 ASP A 7
REMARK 465 THR A 8
REMARK 465 ALA A 9
REMARK 465 ASN A 10
REMARK 465 PRO A 11
REMARK 465 LEU A 12
REMARK 465 ASP A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 ILE A 264
REMARK 465 PRO A 265
REMARK 465 VAL A 266
REMARK 465 GLY A 267
REMARK 465 TYR A 268
REMARK 465 ARG A 269
REMARK 465 GLU A 270
REMARK 465 SER A 271
REMARK 465 PHE A 272
REMARK 465 MET A 273
REMARK 465 THR A 274
REMARK 465 ARG A 275
REMARK 465 ARG A 276
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 LYS B 3
REMARK 465 SER B 4
REMARK 465 ALA B 5
REMARK 465 LYS B 6
REMARK 465 ASP B 7
REMARK 465 THR B 8
REMARK 465 ALA B 9
REMARK 465 ASN B 10
REMARK 465 PRO B 11
REMARK 465 LEU B 12
REMARK 465 PHE B 13
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 GLN A 80 CG CD OE1 NE2
REMARK 470 LYS A 82 CG CD CE NZ
REMARK 470 LYS A 100 CG CD CE NZ
REMARK 470 GLN A 107 CG CD OE1 NE2
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 PHE A 259 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 260 CG1 CG2 CD1
REMARK 470 LYS A 307 CG CD CE NZ
REMARK 470 LYS A 328 CG CD CE NZ
REMARK 470 LYS A 365 CG CD CE NZ
REMARK 470 GLN B 64 CG CD OE1 NE2
REMARK 470 GLU B 76 CG CD OE1 OE2
REMARK 470 GLU B 87 CG CD OE1 OE2
REMARK 470 LYS B 152 CG CD CE NZ
REMARK 470 GLN B 155 CG CD OE1 NE2
REMARK 470 LYS B 159 CG CD CE NZ
REMARK 470 GLU B 180 CG CD OE1 OE2
REMARK 470 LYS B 189 CG CD CE NZ
REMARK 470 ARG B 196 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 239 CG CD CE NZ
REMARK 470 LYS B 328 CG CD CE NZ
REMARK 470 LYS B 365 CG CD CE NZ
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 OH TYR A 371 O HOH A 548 2.12
REMARK 500 OD2 ASP A 141 O HOH A 425 2.14
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 PRO A 86 -173.25 -67.52
REMARK 500 ASN A 143 -18.03 154.01
REMARK 500 ARG A 146 -74.92 -123.80
REMARK 500 PHE A 208 -37.63 -137.16
REMARK 500 PHE A 222 -128.75 45.88
REMARK 500 LEU A 224 124.64 -171.48
REMARK 500 ASN A 297 19.08 57.83
REMARK 500 LYS A 298 -43.84 -141.99
REMARK 500 ALA B 38 136.70 -38.44
REMARK 500 ASN B 88 47.70 -81.15
REMARK 500 ASN B 143 24.12 -153.69
REMARK 500 HIS B 184 135.66 -35.89
REMARK 500 CYS B 204 147.24 -174.48
REMARK 500 PHE B 208 -42.62 -140.87
REMARK 500 PHE B 222 -125.13 45.85
REMARK 500 SER B 284 45.06 -78.07
REMARK 500 LYS B 298 -44.88 -144.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BAHEA.00339.A RELATED DB: TARGETDB
DBREF 3KW3 A 1 372 UNP Q6G2F2 Q6G2F2_BARHE 1 372
DBREF 3KW3 B 1 372 UNP Q6G2F2 Q6G2F2_BARHE 1 372
SEQADV 3KW3 GLY A -3 UNP Q6G2F2 EXPRESSION TAG
SEQADV 3KW3 PRO A -2 UNP Q6G2F2 EXPRESSION TAG
SEQADV 3KW3 GLY A -1 UNP Q6G2F2 EXPRESSION TAG
SEQADV 3KW3 SER A 0 UNP Q6G2F2 EXPRESSION TAG
SEQADV 3KW3 GLY B -3 UNP Q6G2F2 EXPRESSION TAG
SEQADV 3KW3 PRO B -2 UNP Q6G2F2 EXPRESSION TAG
SEQADV 3KW3 GLY B -1 UNP Q6G2F2 EXPRESSION TAG
SEQADV 3KW3 SER B 0 UNP Q6G2F2 EXPRESSION TAG
SEQRES 1 A 376 GLY PRO GLY SER MET ASN LYS SER ALA LYS ASP THR ALA
SEQRES 2 A 376 ASN PRO LEU PHE PRO ALA THR ALA ILE ALA THR ILE ASP
SEQRES 3 A 376 VAL ARG ALA ILE VAL ALA ASN TYR ARG THR LEU ALA GLN
SEQRES 4 A 376 HIS VAL ALA PRO THR GLU CYS SER ALA VAL VAL LLP ALA
SEQRES 5 A 376 ASN ALA TYR GLY LEU GLY ALA HIS LYS ILE ALA PRO ALA
SEQRES 6 A 376 LEU TYR GLN ALA GLY CYS ARG THR PHE PHE VAL ALA GLN
SEQRES 7 A 376 ILE GLU GLU ALA LEU GLN LEU LYS ALA VAL LEU PRO GLU
SEQRES 8 A 376 ASN VAL MET ILE ALA LEU LEU ASN GLY PHE PRO HIS LYS
SEQRES 9 A 376 ALA GLU GLU PHE VAL ALA GLN SER GLY ILE ILE PRO LEU
SEQRES 10 A 376 LEU ASN SER TRP SER THR ILE GLU ASP TRP GLN THR LEU
SEQRES 11 A 376 CYS GLN LYS LYS ASN LYS LYS PHE PRO ALA ILE ILE GLN
SEQRES 12 A 376 VAL ASP THR ASN MET SER ARG LEU GLY LEU ASP LYS LYS
SEQRES 13 A 376 GLU LEU GLN LYS LEU ILE LYS ASN PRO THR ILE PHE GLU
SEQRES 14 A 376 LYS ALA GLU ILE LYS TYR ILE LEU SER HIS LEU ALA ASN
SEQRES 15 A 376 GLY GLU ASP ALA SER HIS SER SER ASN ASN LYS GLN LEU
SEQRES 16 A 376 ALA ALA PHE LYS ARG VAL LEU ALA GLN LEU PRO THR CYS
SEQRES 17 A 376 LYS VAL SER PHE ALA ASN SER GLY GLY ILE PHE LEU GLY
SEQRES 18 A 376 SER ASP PHE TYR PHE ASP LEU VAL ARG PRO GLY ILE ALA
SEQRES 19 A 376 LEU TYR GLY VAL ASP PRO HIS GLY LYS HIS PRO THR PRO
SEQRES 20 A 376 LEU LYS ALA VAL VAL LYS VAL GLU ALA GLN VAL LEU GLN
SEQRES 21 A 376 SER ARG PHE ILE ASP ALA GLY ILE PRO VAL GLY TYR ARG
SEQRES 22 A 376 GLU SER PHE MET THR ARG ARG PRO SER THR LEU ALA THR
SEQRES 23 A 376 ILE SER ILE GLY TYR ALA ASP GLY TRP PRO ARG ILE LEU
SEQRES 24 A 376 SER ASN LYS GLY THR VAL TYR PHE ASN GLY HIS LYS LEU
SEQRES 25 A 376 PRO ILE VAL GLY HIS ILE SER MET ASP SER ILE ILE VAL
SEQRES 26 A 376 ASP ALA THR ASP LEU ASP LYS LYS PRO GLN ARG GLY ASP
SEQRES 27 A 376 TRP VAL GLU LEU ILE GLY PRO HIS GLN PRO LEU GLU LYS
SEQRES 28 A 376 VAL SER THR ASP THR ASN THR ILE PRO HIS GLU ILE LEU
SEQRES 29 A 376 THR SER LEU GLY LYS ARG TYR LYS ARG ILE TYR ILE
SEQRES 1 B 376 GLY PRO GLY SER MET ASN LYS SER ALA LYS ASP THR ALA
SEQRES 2 B 376 ASN PRO LEU PHE PRO ALA THR ALA ILE ALA THR ILE ASP
SEQRES 3 B 376 VAL ARG ALA ILE VAL ALA ASN TYR ARG THR LEU ALA GLN
SEQRES 4 B 376 HIS VAL ALA PRO THR GLU CYS SER ALA VAL VAL LLP ALA
SEQRES 5 B 376 ASN ALA TYR GLY LEU GLY ALA HIS LYS ILE ALA PRO ALA
SEQRES 6 B 376 LEU TYR GLN ALA GLY CYS ARG THR PHE PHE VAL ALA GLN
SEQRES 7 B 376 ILE GLU GLU ALA LEU GLN LEU LYS ALA VAL LEU PRO GLU
SEQRES 8 B 376 ASN VAL MET ILE ALA LEU LEU ASN GLY PHE PRO HIS LYS
SEQRES 9 B 376 ALA GLU GLU PHE VAL ALA GLN SER GLY ILE ILE PRO LEU
SEQRES 10 B 376 LEU ASN SER TRP SER THR ILE GLU ASP TRP GLN THR LEU
SEQRES 11 B 376 CYS GLN LYS LYS ASN LYS LYS PHE PRO ALA ILE ILE GLN
SEQRES 12 B 376 VAL ASP THR ASN MET SER ARG LEU GLY LEU ASP LYS LYS
SEQRES 13 B 376 GLU LEU GLN LYS LEU ILE LYS ASN PRO THR ILE PHE GLU
SEQRES 14 B 376 LYS ALA GLU ILE LYS TYR ILE LEU SER HIS LEU ALA ASN
SEQRES 15 B 376 GLY GLU ASP ALA SER HIS SER SER ASN ASN LYS GLN LEU
SEQRES 16 B 376 ALA ALA PHE LYS ARG VAL LEU ALA GLN LEU PRO THR CYS
SEQRES 17 B 376 LYS VAL SER PHE ALA ASN SER GLY GLY ILE PHE LEU GLY
SEQRES 18 B 376 SER ASP PHE TYR PHE ASP LEU VAL ARG PRO GLY ILE ALA
SEQRES 19 B 376 LEU TYR GLY VAL ASP PRO HIS GLY LYS HIS PRO THR PRO
SEQRES 20 B 376 LEU LYS ALA VAL VAL LYS VAL GLU ALA GLN VAL LEU GLN
SEQRES 21 B 376 SER ARG PHE ILE ASP ALA GLY ILE PRO VAL GLY TYR ARG
SEQRES 22 B 376 GLU SER PHE MET THR ARG ARG PRO SER THR LEU ALA THR
SEQRES 23 B 376 ILE SER ILE GLY TYR ALA ASP GLY TRP PRO ARG ILE LEU
SEQRES 24 B 376 SER ASN LYS GLY THR VAL TYR PHE ASN GLY HIS LYS LEU
SEQRES 25 B 376 PRO ILE VAL GLY HIS ILE SER MET ASP SER ILE ILE VAL
SEQRES 26 B 376 ASP ALA THR ASP LEU ASP LYS LYS PRO GLN ARG GLY ASP
SEQRES 27 B 376 TRP VAL GLU LEU ILE GLY PRO HIS GLN PRO LEU GLU LYS
SEQRES 28 B 376 VAL SER THR ASP THR ASN THR ILE PRO HIS GLU ILE LEU
SEQRES 29 B 376 THR SER LEU GLY LYS ARG TYR LYS ARG ILE TYR ILE
MODRES 3KW3 LLP A 47 LYS
MODRES 3KW3 LLP B 47 LYS
HET LLP A 47 24
HET LLP B 47 24
HETNAM LLP (2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-
HETNAM 2 LLP (PHOSPHONOOXYMETHYL)PYRIDIN-4-
HETNAM 3 LLP YL]METHYLIDENEAMINO]HEXANOIC ACID
HETSYN LLP N'-PYRIDOXYL-LYSINE-5'-MONOPHOSPHATE
FORMUL 1 LLP 2(C14 H22 N3 O7 P)
FORMUL 3 HOH *426(H2 O)
HELIX 1 1 VAL A 23 ALA A 38 1 16
HELIX 2 2 VAL A 46 GLY A 52 1 7
HELIX 3 3 GLY A 54 ALA A 65 1 12
HELIX 4 4 GLN A 74 LEU A 85 1 12
HELIX 5 5 ALA A 101 SER A 108 1 8
HELIX 6 6 SER A 116 ASN A 131 1 16
HELIX 7 7 ASP A 150 ASN A 160 1 11
HELIX 8 8 THR A 162 ALA A 167 1 6
HELIX 9 9 SER A 185 ALA A 199 1 15
HELIX 10 10 ASN A 210 PHE A 215 1 6
HELIX 11 11 LEU A 216 TYR A 221 5 6
HELIX 12 12 GLY A 228 GLY A 233 5 6
HELIX 13 13 GLY A 286 GLY A 290 5 5
HELIX 14 14 PRO A 292 SER A 296 5 5
HELIX 15 15 PRO A 344 ASN A 353 1 10
HELIX 16 16 ILE A 355 SER A 362 1 8
HELIX 17 17 VAL B 23 ALA B 38 1 16
HELIX 18 18 VAL B 46 GLY B 52 1 7
HELIX 19 19 GLY B 54 ALA B 65 1 12
HELIX 20 20 GLN B 74 LEU B 85 1 12
HELIX 21 21 ALA B 101 SER B 108 1 8
HELIX 22 22 SER B 116 ASN B 131 1 16
HELIX 23 23 ASP B 150 ASN B 160 1 11
HELIX 24 24 THR B 162 ALA B 167 1 6
HELIX 25 25 SER B 185 GLN B 200 1 16
HELIX 26 26 ASN B 210 PHE B 215 1 6
HELIX 27 27 LEU B 216 TYR B 221 5 6
HELIX 28 28 GLY B 228 GLY B 233 5 6
HELIX 29 29 GLY B 267 SER B 271 5 5
HELIX 30 30 GLY B 286 GLY B 290 5 5
HELIX 31 31 PRO B 292 SER B 296 5 5
HELIX 32 32 PRO B 344 ASN B 353 1 10
HELIX 33 33 ILE B 355 SER B 362 1 8
SHEET 1 A 4 ILE A 319 ASP A 322 0
SHEET 2 A 4 THR A 279 ILE A 283 -1 N ALA A 281 O VAL A 321
SHEET 3 A 4 VAL A 248 PHE A 259 -1 N LEU A 255 O THR A 282
SHEET 4 A 4 TRP A 335 ILE A 339 -1 O LEU A 338 N VAL A 250
SHEET 1 B 5 ILE A 319 ASP A 322 0
SHEET 2 B 5 THR A 279 ILE A 283 -1 N ALA A 281 O VAL A 321
SHEET 3 B 5 VAL A 248 PHE A 259 -1 N LEU A 255 O THR A 282
SHEET 4 B 5 ALA A 17 ASP A 22 -1 N ILE A 18 O GLU A 251
SHEET 5 B 5 LYS A 368 ILE A 372 1 O ILE A 370 N ILE A 21
SHEET 1 C 2 GLU A 41 CYS A 42 0
SHEET 2 C 2 LEU A 224 VAL A 225 1 O VAL A 225 N GLU A 41
SHEET 1 D 7 ALA A 44 VAL A 45 0
SHEET 2 D 7 THR A 69 VAL A 72 1 O THR A 69 N ALA A 44
SHEET 3 D 7 MET A 90 LEU A 93 1 O MET A 90 N PHE A 70
SHEET 4 D 7 ILE A 111 LEU A 114 1 O ILE A 111 N ILE A 91
SHEET 5 D 7 PRO A 135 GLN A 139 1 O ILE A 137 N LEU A 114
SHEET 6 D 7 GLU A 168 LEU A 173 1 O LEU A 173 N ILE A 138
SHEET 7 D 7 VAL A 206 SER A 207 1 O SER A 207 N ILE A 172
SHEET 1 E 2 THR A 300 PHE A 303 0
SHEET 2 E 2 HIS A 306 PRO A 309 -1 O LEU A 308 N VAL A 301
SHEET 1 F 4 ILE B 319 ASP B 322 0
SHEET 2 F 4 SER B 278 ILE B 283 -1 N ILE B 283 O ILE B 319
SHEET 3 F 4 VAL B 248 ILE B 260 -1 N LEU B 255 O THR B 282
SHEET 4 F 4 TRP B 335 ILE B 339 -1 O LEU B 338 N VAL B 250
SHEET 1 G 5 ILE B 319 ASP B 322 0
SHEET 2 G 5 SER B 278 ILE B 283 -1 N ILE B 283 O ILE B 319
SHEET 3 G 5 VAL B 248 ILE B 260 -1 N LEU B 255 O THR B 282
SHEET 4 G 5 ALA B 17 ASP B 22 -1 N THR B 20 O LYS B 249
SHEET 5 G 5 LYS B 368 ILE B 372 1 O ILE B 370 N ILE B 21
SHEET 1 H 2 GLU B 41 CYS B 42 0
SHEET 2 H 2 LEU B 224 VAL B 225 1 O VAL B 225 N GLU B 41
SHEET 1 I 7 ALA B 44 VAL B 45 0
SHEET 2 I 7 THR B 69 VAL B 72 1 O PHE B 71 N ALA B 44
SHEET 3 I 7 MET B 90 LEU B 93 1 O ALA B 92 N PHE B 70
SHEET 4 I 7 ILE B 111 LEU B 114 1 O ILE B 111 N LEU B 93
SHEET 5 I 7 PRO B 135 GLN B 139 1 O ILE B 137 N LEU B 114
SHEET 6 I 7 GLU B 168 LEU B 173 1 O LEU B 173 N ILE B 138
SHEET 7 I 7 VAL B 206 SER B 207 1 O SER B 207 N ILE B 172
SHEET 1 J 2 PRO B 265 VAL B 266 0
SHEET 2 J 2 PHE B 272 MET B 273 -1 O PHE B 272 N VAL B 266
SHEET 1 K 2 THR B 300 PHE B 303 0
SHEET 2 K 2 HIS B 306 PRO B 309 -1 O LEU B 308 N VAL B 301
LINK C LLP A 47 N ALA A 48 1555 1555 1.34
LINK C LLP B 47 N ALA B 48 1555 1555 1.32
CISPEP 1 ALA A 38 PRO A 39 0 5.51
CISPEP 2 HIS A 240 PRO A 241 0 0.73
CISPEP 3 ALA B 38 PRO B 39 0 4.01
CISPEP 4 HIS B 240 PRO B 241 0 10.96
CRYST1 136.794 54.316 107.476 90.00 112.39 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007310 0.000000 0.003011 0.00000
SCALE2 0.000000 0.018411 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010063 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
