HEADER ISOMERASE 11-DEC-15 5FAC
TITLE ALANINE RACEMASE FROM STREPTOMYCES COELICOLOR A3(2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALANINE RACEMASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 5.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR A3(2);
SOURCE 3 ORGANISM_TAXID: 100226;
SOURCE 4 GENE: ALR, SCO4745, SC6G4.23;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET-15B
KEYWDS ISOMERASE, PLP, ALANINE RACEMASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.TASSONI,N.S.PANNU
REVDAT 4 10-JAN-24 5FAC 1 REMARK
REVDAT 3 01-FEB-17 5FAC 1 JRNL
REVDAT 2 25-JAN-17 5FAC 1 JRNL
REVDAT 1 21-DEC-16 5FAC 0
JRNL AUTH R.TASSONI,L.T.VAN DER AART,M.UBBINK,G.P.VAN WEZEL,N.S.PANNU
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF THE ALANINE
JRNL TITL 2 RACEMASE FROM STREPTOMYCES COELICOLOR A3(2).
JRNL REF BIOCHEM. BIOPHYS. RES. V. 483 122 2017
JRNL REF 2 COMMUN.
JRNL REFN ESSN 1090-2104
JRNL PMID 28042035
JRNL DOI 10.1016/J.BBRC.2016.12.183
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 32860
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1693
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2035
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.3550
REMARK 3 BIN FREE R VALUE SET COUNT : 107
REMARK 3 BIN FREE R VALUE : 0.3650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11337
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 171
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.30000
REMARK 3 B22 (A**2) : 5.96000
REMARK 3 B33 (A**2) : -3.87000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.00000
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): 0.444
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.416
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.747
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11704 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 11087 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15985 ; 1.601 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25387 ; 1.393 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1531 ; 6.423 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 478 ;30.510 ;21.799
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1654 ;15.600 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 132 ;17.845 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1752 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13476 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2648 ; 0.005 ; 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): 6118 ; 3.081 ; 4.365
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6117 ; 3.081 ; 4.365
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7642 ; 4.971 ; 6.542
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7643 ; 4.971 ; 6.542
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5586 ; 3.290 ; 4.725
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5587 ; 3.290 ; 4.725
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8341 ; 5.380 ; 6.937
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 12762 ; 8.397 ;34.998
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 12754 ; 8.398 ;35.013
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 11 390 B 11 390 43936 0.07 0.05
REMARK 3 2 A 9 390 C 9 390 43870 0.08 0.05
REMARK 3 3 A 11 390 D 11 390 44062 0.08 0.05
REMARK 3 4 B 11 390 C 11 390 44208 0.07 0.05
REMARK 3 5 B 11 391 D 11 391 44618 0.07 0.05
REMARK 3 6 C 11 390 D 11 390 44278 0.07 0.05
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 5FAC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972422
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32860
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 47.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.24900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.1
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 : 1.300
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: 1VFH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PROPANE PH 8.5, 0.2 M
REMARK 280 NABR, 20% (W/V) PEG3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 43.58500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 7650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 -18
REMARK 465 GLY A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 ARG A 7
REMARK 465 MET B -18
REMARK 465 GLY B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLU B 3
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 ALA B 6
REMARK 465 ARG B 7
REMARK 465 ARG B 8
REMARK 465 ASP B 9
REMARK 465 ALA B 10
REMARK 465 MET C -18
REMARK 465 GLY C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLU C 3
REMARK 465 THR C 4
REMARK 465 THR C 5
REMARK 465 ALA C 6
REMARK 465 ARG C 7
REMARK 465 ARG C 8
REMARK 465 MET D -18
REMARK 465 GLY D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLU D 3
REMARK 465 THR D 4
REMARK 465 THR D 5
REMARK 465 ALA D 6
REMARK 465 ARG D 7
REMARK 465 ARG D 8
REMARK 465 ASP D 9
REMARK 465 ALA D 10
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 D 217 O HOH D 501 2.12
REMARK 500 NZ LYS D 46 C4 PLP D 401 2.14
REMARK 500 O GLY D 277 O HOH D 502 2.18
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 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 105 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 111 CG - CD - NE ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG A 217 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 217 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 342 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 199 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG D 111 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG D 166 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG D 328 NE - CZ - NH1 ANGL. DEV. = 3.6 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 ALA A 10 3.86 -63.95
REMARK 500 ARG A 148 -116.09 -98.28
REMARK 500 PHE A 233 -145.92 50.27
REMARK 500 SER A 282 179.23 69.34
REMARK 500 HIS A 285 56.20 35.84
REMARK 500 SER A 312 -5.68 64.88
REMARK 500 ARG B 148 -115.71 -96.68
REMARK 500 PHE B 233 -145.14 49.70
REMARK 500 SER B 282 179.90 68.59
REMARK 500 HIS B 285 56.26 35.61
REMARK 500 SER B 312 -4.61 63.74
REMARK 500 PRO C 103 61.92 -69.91
REMARK 500 ARG C 148 -118.93 -97.84
REMARK 500 PHE C 233 -145.71 49.38
REMARK 500 SER C 282 179.88 69.23
REMARK 500 HIS C 285 56.30 35.66
REMARK 500 SER C 312 -4.11 63.52
REMARK 500 ALA D 72 -68.77 -90.46
REMARK 500 ARG D 148 -114.87 -97.82
REMARK 500 PHE D 233 -145.81 50.65
REMARK 500 SER D 282 -179.69 69.61
REMARK 500 HIS D 285 56.94 34.55
REMARK 500 SER D 312 -4.50 62.93
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 PLP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PLP B 401 and LYS B
REMARK 800 46
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PLP C 401 and LYS C
REMARK 800 46
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PLP D 401 and LYS D
REMARK 800 46
DBREF 5FAC A 1 391 UNP O86786 ALR_STRCO 1 391
DBREF 5FAC B 1 391 UNP O86786 ALR_STRCO 1 391
DBREF 5FAC C 1 391 UNP O86786 ALR_STRCO 1 391
DBREF 5FAC D 1 391 UNP O86786 ALR_STRCO 1 391
SEQADV 5FAC MET A -18 UNP O86786 INITIATING METHIONINE
SEQADV 5FAC GLY A -17 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER A -16 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS A -15 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS A -14 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS A -13 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS A -12 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS A -11 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS A -10 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER A -9 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER A -8 UNP O86786 EXPRESSION TAG
SEQADV 5FAC GLY A -7 UNP O86786 EXPRESSION TAG
SEQADV 5FAC LEU A -6 UNP O86786 EXPRESSION TAG
SEQADV 5FAC VAL A -5 UNP O86786 EXPRESSION TAG
SEQADV 5FAC PRO A -4 UNP O86786 EXPRESSION TAG
SEQADV 5FAC ARG A -3 UNP O86786 EXPRESSION TAG
SEQADV 5FAC GLY A -2 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER A -1 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS A 0 UNP O86786 EXPRESSION TAG
SEQADV 5FAC MET B -18 UNP O86786 INITIATING METHIONINE
SEQADV 5FAC GLY B -17 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER B -16 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS B -15 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS B -14 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS B -13 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS B -12 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS B -11 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS B -10 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER B -9 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER B -8 UNP O86786 EXPRESSION TAG
SEQADV 5FAC GLY B -7 UNP O86786 EXPRESSION TAG
SEQADV 5FAC LEU B -6 UNP O86786 EXPRESSION TAG
SEQADV 5FAC VAL B -5 UNP O86786 EXPRESSION TAG
SEQADV 5FAC PRO B -4 UNP O86786 EXPRESSION TAG
SEQADV 5FAC ARG B -3 UNP O86786 EXPRESSION TAG
SEQADV 5FAC GLY B -2 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER B -1 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS B 0 UNP O86786 EXPRESSION TAG
SEQADV 5FAC MET C -18 UNP O86786 INITIATING METHIONINE
SEQADV 5FAC GLY C -17 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER C -16 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS C -15 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS C -14 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS C -13 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS C -12 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS C -11 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS C -10 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER C -9 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER C -8 UNP O86786 EXPRESSION TAG
SEQADV 5FAC GLY C -7 UNP O86786 EXPRESSION TAG
SEQADV 5FAC LEU C -6 UNP O86786 EXPRESSION TAG
SEQADV 5FAC VAL C -5 UNP O86786 EXPRESSION TAG
SEQADV 5FAC PRO C -4 UNP O86786 EXPRESSION TAG
SEQADV 5FAC ARG C -3 UNP O86786 EXPRESSION TAG
SEQADV 5FAC GLY C -2 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER C -1 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS C 0 UNP O86786 EXPRESSION TAG
SEQADV 5FAC MET D -18 UNP O86786 INITIATING METHIONINE
SEQADV 5FAC GLY D -17 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER D -16 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS D -15 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS D -14 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS D -13 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS D -12 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS D -11 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS D -10 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER D -9 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER D -8 UNP O86786 EXPRESSION TAG
SEQADV 5FAC GLY D -7 UNP O86786 EXPRESSION TAG
SEQADV 5FAC LEU D -6 UNP O86786 EXPRESSION TAG
SEQADV 5FAC VAL D -5 UNP O86786 EXPRESSION TAG
SEQADV 5FAC PRO D -4 UNP O86786 EXPRESSION TAG
SEQADV 5FAC ARG D -3 UNP O86786 EXPRESSION TAG
SEQADV 5FAC GLY D -2 UNP O86786 EXPRESSION TAG
SEQADV 5FAC SER D -1 UNP O86786 EXPRESSION TAG
SEQADV 5FAC HIS D 0 UNP O86786 EXPRESSION TAG
SEQRES 1 A 410 MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 410 VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG
SEQRES 3 A 410 ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE
SEQRES 4 A 410 ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG
SEQRES 5 A 410 GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS
SEQRES 6 A 410 ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG
SEQRES 7 A 410 ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA
SEQRES 8 A 410 THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO
SEQRES 9 A 410 GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP
SEQRES 10 A 410 THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG
SEQRES 11 A 410 LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU
SEQRES 12 A 410 VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG
SEQRES 13 A 410 VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY
SEQRES 14 A 410 CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA
SEQRES 15 A 410 ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR
SEQRES 16 A 410 GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY
SEQRES 17 A 410 HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU
SEQRES 18 A 410 MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU
SEQRES 19 A 410 VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU
SEQRES 20 A 410 PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA
SEQRES 21 A 410 MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO
SEQRES 22 A 410 ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA
SEQRES 23 A 410 SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY
SEQRES 24 A 410 VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR
SEQRES 25 A 410 THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE
SEQRES 26 A 410 PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP
SEQRES 27 A 410 GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP
SEQRES 28 A 410 GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO
SEQRES 29 A 410 GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY
SEQRES 30 A 410 GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR
SEQRES 31 A 410 ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL
SEQRES 32 A 410 PRO ARG VAL TYR VAL ASN GLU
SEQRES 1 B 410 MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 B 410 VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG
SEQRES 3 B 410 ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE
SEQRES 4 B 410 ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG
SEQRES 5 B 410 GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS
SEQRES 6 B 410 ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG
SEQRES 7 B 410 ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA
SEQRES 8 B 410 THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO
SEQRES 9 B 410 GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP
SEQRES 10 B 410 THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG
SEQRES 11 B 410 LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU
SEQRES 12 B 410 VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG
SEQRES 13 B 410 VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY
SEQRES 14 B 410 CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA
SEQRES 15 B 410 ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR
SEQRES 16 B 410 GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY
SEQRES 17 B 410 HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU
SEQRES 18 B 410 MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU
SEQRES 19 B 410 VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU
SEQRES 20 B 410 PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA
SEQRES 21 B 410 MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO
SEQRES 22 B 410 ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA
SEQRES 23 B 410 SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY
SEQRES 24 B 410 VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR
SEQRES 25 B 410 THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE
SEQRES 26 B 410 PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP
SEQRES 27 B 410 GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP
SEQRES 28 B 410 GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO
SEQRES 29 B 410 GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY
SEQRES 30 B 410 GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR
SEQRES 31 B 410 ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL
SEQRES 32 B 410 PRO ARG VAL TYR VAL ASN GLU
SEQRES 1 C 410 MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 C 410 VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG
SEQRES 3 C 410 ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE
SEQRES 4 C 410 ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG
SEQRES 5 C 410 GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS
SEQRES 6 C 410 ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG
SEQRES 7 C 410 ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA
SEQRES 8 C 410 THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO
SEQRES 9 C 410 GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP
SEQRES 10 C 410 THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG
SEQRES 11 C 410 LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU
SEQRES 12 C 410 VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG
SEQRES 13 C 410 VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY
SEQRES 14 C 410 CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA
SEQRES 15 C 410 ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR
SEQRES 16 C 410 GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY
SEQRES 17 C 410 HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU
SEQRES 18 C 410 MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU
SEQRES 19 C 410 VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU
SEQRES 20 C 410 PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA
SEQRES 21 C 410 MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO
SEQRES 22 C 410 ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA
SEQRES 23 C 410 SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY
SEQRES 24 C 410 VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR
SEQRES 25 C 410 THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE
SEQRES 26 C 410 PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP
SEQRES 27 C 410 GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP
SEQRES 28 C 410 GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO
SEQRES 29 C 410 GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY
SEQRES 30 C 410 GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR
SEQRES 31 C 410 ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL
SEQRES 32 C 410 PRO ARG VAL TYR VAL ASN GLU
SEQRES 1 D 410 MET GLY SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 D 410 VAL PRO ARG GLY SER HIS MET SER GLU THR THR ALA ARG
SEQRES 3 D 410 ARG ASP ALA ASP ALA VAL LEU ARG ALA ARG ALA GLU ILE
SEQRES 4 D 410 ASP LEU ALA ALA LEU ARG ALA ASN VAL ARG ALA LEU ARG
SEQRES 5 D 410 GLU ARG ALA PRO GLY ALA ALA LEU MET ALA VAL VAL LYS
SEQRES 6 D 410 ALA ASP ALA TYR GLY HIS GLY ALA ILE PRO CYS ALA ARG
SEQRES 7 D 410 ALA ALA VAL ALA ALA GLY ALA THR TRP LEU GLY THR ALA
SEQRES 8 D 410 THR PRO GLN GLU ALA LEU ALA LEU ARG ALA ALA GLU PRO
SEQRES 9 D 410 GLY LEU PRO ASP ASP VAL ARG ILE MET CYS TRP LEU TRP
SEQRES 10 D 410 THR PRO GLY GLY PRO TRP ARG GLU ALA VAL GLU ALA ARG
SEQRES 11 D 410 LEU ASP VAL SER VAL SER ALA MET TRP ALA MET GLU GLU
SEQRES 12 D 410 VAL THR GLY ALA ALA ARG ALA ALA GLY VAL PRO ALA ARG
SEQRES 13 D 410 VAL GLN LEU KCX ALA ASP THR GLY LEU GLY ARG GLY GLY
SEQRES 14 D 410 CYS GLN PRO GLY ALA ASP TRP GLU ARG LEU VAL GLY ALA
SEQRES 15 D 410 ALA LEU ARG ALA GLU GLU GLU GLY LEU LEU ARG VAL THR
SEQRES 16 D 410 GLY LEU TRP SER HIS PHE ALA CYS ALA ASP GLU PRO GLY
SEQRES 17 D 410 HIS PRO SER ILE ALA ALA GLN LEU THR ARG PHE ARG GLU
SEQRES 18 D 410 MET THR ALA TYR ALA GLU GLN ARG GLY LEU ARG PRO GLU
SEQRES 19 D 410 VAL ARG HIS ILE ALA ASN SER PRO ALA THR LEU THR LEU
SEQRES 20 D 410 PRO ASP ALA HIS PHE ASP LEU VAL ARG PRO GLY ILE ALA
SEQRES 21 D 410 MET TYR GLY VAL SER PRO SER PRO GLU ILE GLY THR PRO
SEQRES 22 D 410 ALA ASP PHE GLY LEU ARG PRO VAL MET THR LEU ALA ALA
SEQRES 23 D 410 SER LEU ALA LEU VAL LYS GLN VAL PRO GLY GLY HIS GLY
SEQRES 24 D 410 VAL SER TYR GLY HIS HIS TYR THR THR PRO GLY GLU THR
SEQRES 25 D 410 THR LEU GLY LEU VAL PRO LEU GLY TYR ALA ASP GLY ILE
SEQRES 26 D 410 PRO ARG HIS ALA SER SER SER GLY PRO VAL LEU VAL ASP
SEQRES 27 D 410 GLY LYS TRP ARG THR VAL ALA GLY ARG ILE ALA MET ASP
SEQRES 28 D 410 GLN PHE VAL VAL ASP LEU GLY GLY ASP ARG PRO GLU PRO
SEQRES 29 D 410 GLY ALA GLU ALA VAL LEU PHE GLY PRO GLY ASP ARG GLY
SEQRES 30 D 410 GLU PRO THR ALA GLU ASP TRP ALA GLN ALA ALA GLY THR
SEQRES 31 D 410 ILE ALA TYR GLU ILE VAL THR ARG ILE GLY SER ARG VAL
SEQRES 32 D 410 PRO ARG VAL TYR VAL ASN GLU
MODRES 5FAC KCX A 141 LYS MODIFIED RESIDUE
MODRES 5FAC KCX B 141 LYS MODIFIED RESIDUE
MODRES 5FAC KCX C 141 LYS MODIFIED RESIDUE
MODRES 5FAC KCX D 141 LYS MODIFIED RESIDUE
HET KCX A 141 12
HET KCX B 141 12
HET KCX C 141 12
HET KCX D 141 12
HET PLP A 401 15
HET CL A 402 1
HET PLP B 401 15
HET CL B 402 1
HET PLP C 401 15
HET CL C 402 1
HET PLP D 401 15
HET CL D 402 1
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM CL CHLORIDE ION
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 1 KCX 4(C7 H14 N2 O4)
FORMUL 5 PLP 4(C8 H10 N O6 P)
FORMUL 6 CL 4(CL 1-)
FORMUL 13 HOH *171(H2 O)
HELIX 1 AA1 ARG A 8 LEU A 14 5 7
HELIX 2 AA2 LEU A 22 ALA A 36 1 15
HELIX 3 AA3 VAL A 45 GLY A 51 1 7
HELIX 4 AA4 GLY A 53 ALA A 64 1 12
HELIX 5 AA5 THR A 73 ALA A 82 1 10
HELIX 6 AA6 PRO A 103 ALA A 110 1 8
HELIX 7 AA7 ALA A 118 GLY A 133 1 16
HELIX 8 AA8 GLY A 154 GLU A 170 1 17
HELIX 9 AA9 HIS A 190 ARG A 210 1 21
HELIX 10 AB1 ASN A 221 LEU A 228 1 8
HELIX 11 AB2 PRO A 229 HIS A 232 5 4
HELIX 12 AB3 GLY A 239 GLY A 244 5 6
HELIX 13 AB4 PRO A 254 GLY A 258 5 5
HELIX 14 AB5 SER A 282 HIS A 286 5 5
HELIX 15 AB6 GLY A 301 GLY A 305 5 5
HELIX 16 AB7 PRO A 307 SER A 311 5 5
HELIX 17 AB8 THR A 361 ALA A 369 1 9
HELIX 18 AB9 ILE A 372 ARG A 379 1 8
HELIX 19 AC1 ASP B 11 LEU B 14 5 4
HELIX 20 AC2 LEU B 22 ALA B 36 1 15
HELIX 21 AC3 VAL B 45 GLY B 51 1 7
HELIX 22 AC4 GLY B 53 ALA B 64 1 12
HELIX 23 AC5 THR B 73 ALA B 82 1 10
HELIX 24 AC6 PRO B 103 ALA B 110 1 8
HELIX 25 AC7 ALA B 118 GLY B 133 1 16
HELIX 26 AC8 GLY B 154 GLU B 170 1 17
HELIX 27 AC9 HIS B 190 ARG B 210 1 21
HELIX 28 AD1 ASN B 221 LEU B 228 1 8
HELIX 29 AD2 PRO B 229 HIS B 232 5 4
HELIX 30 AD3 GLY B 239 GLY B 244 5 6
HELIX 31 AD4 PRO B 254 GLY B 258 5 5
HELIX 32 AD5 SER B 282 HIS B 286 5 5
HELIX 33 AD6 GLY B 301 GLY B 305 5 5
HELIX 34 AD7 PRO B 307 SER B 311 5 5
HELIX 35 AD8 THR B 361 ALA B 369 1 9
HELIX 36 AD9 ILE B 372 ARG B 379 1 8
HELIX 37 AE1 ASP C 9 LEU C 14 5 6
HELIX 38 AE2 LEU C 22 ALA C 36 1 15
HELIX 39 AE3 VAL C 45 GLY C 51 1 7
HELIX 40 AE4 GLY C 53 ALA C 64 1 12
HELIX 41 AE5 THR C 73 ALA C 82 1 10
HELIX 42 AE6 PRO C 103 ALA C 110 1 8
HELIX 43 AE7 ALA C 118 GLY C 133 1 16
HELIX 44 AE8 GLY C 154 GLU C 170 1 17
HELIX 45 AE9 HIS C 190 ARG C 210 1 21
HELIX 46 AF1 ASN C 221 LEU C 228 1 8
HELIX 47 AF2 PRO C 229 HIS C 232 5 4
HELIX 48 AF3 GLY C 239 GLY C 244 5 6
HELIX 49 AF4 PRO C 254 GLY C 258 5 5
HELIX 50 AF5 SER C 282 HIS C 286 5 5
HELIX 51 AF6 GLY C 301 GLY C 305 5 5
HELIX 52 AF7 PRO C 307 SER C 311 5 5
HELIX 53 AF8 THR C 361 ALA C 369 1 9
HELIX 54 AF9 ILE C 372 ARG C 379 1 8
HELIX 55 AG1 ASP D 11 LEU D 14 5 4
HELIX 56 AG2 ASP D 21 ALA D 36 1 16
HELIX 57 AG3 VAL D 45 GLY D 51 1 7
HELIX 58 AG4 GLY D 53 ALA D 64 1 12
HELIX 59 AG5 THR D 73 ALA D 82 1 10
HELIX 60 AG6 PRO D 103 ALA D 110 1 8
HELIX 61 AG7 ALA D 118 GLY D 133 1 16
HELIX 62 AG8 GLY D 154 GLU D 170 1 17
HELIX 63 AG9 HIS D 190 ARG D 210 1 21
HELIX 64 AH1 ASN D 221 LEU D 228 1 8
HELIX 65 AH2 PRO D 229 HIS D 232 5 4
HELIX 66 AH3 GLY D 239 GLY D 244 5 6
HELIX 67 AH4 PRO D 254 GLY D 258 5 5
HELIX 68 AH5 SER D 282 HIS D 286 5 5
HELIX 69 AH6 GLY D 301 GLY D 305 5 5
HELIX 70 AH7 PRO D 307 SER D 311 5 5
HELIX 71 AH8 THR D 361 ALA D 369 1 9
HELIX 72 AH9 ILE D 372 ARG D 379 1 8
SHEET 1 AA1 6 LYS A 321 THR A 324 0
SHEET 2 AA1 6 PRO A 315 VAL A 318 -1 N VAL A 316 O ARG A 323
SHEET 3 AA1 6 GLU A 348 PHE A 352 -1 O VAL A 350 N LEU A 317
SHEET 4 AA1 6 MET A 263 SER A 268 -1 N ALA A 267 O ALA A 349
SHEET 5 AA1 6 ALA A 16 ASP A 21 -1 N GLU A 19 O THR A 264
SHEET 6 AA1 6 ARG A 386 VAL A 389 1 O VAL A 387 N ILE A 20
SHEET 1 AA2 8 VAL A 216 HIS A 218 0
SHEET 2 AA2 8 LEU A 173 TRP A 179 1 N THR A 176 O VAL A 216
SHEET 3 AA2 8 ALA A 136 KCX A 141 1 N ALA A 136 O ARG A 174
SHEET 4 AA2 8 ASP A 113 VAL A 116 1 N VAL A 114 O GLN A 139
SHEET 5 AA2 8 ARG A 92 CYS A 95 1 N ILE A 93 O ASP A 113
SHEET 6 AA2 8 TRP A 68 THR A 71 1 N LEU A 69 O ARG A 92
SHEET 7 AA2 8 ALA A 40 VAL A 44 1 N ALA A 43 O TRP A 68
SHEET 8 AA2 8 LEU A 235 VAL A 236 1 O VAL A 236 N MET A 42
SHEET 1 AA3 3 LEU A 271 VAL A 275 0
SHEET 2 AA3 3 THR A 293 VAL A 298 -1 O LEU A 295 N LYS A 273
SHEET 3 AA3 3 PHE A 334 ASP A 337 -1 O PHE A 334 N VAL A 298
SHEET 1 AA4 2 GLY A 280 VAL A 281 0
SHEET 2 AA4 2 TYR A 287 THR A 288 -1 O TYR A 287 N VAL A 281
SHEET 1 AA5 6 LYS B 321 THR B 324 0
SHEET 2 AA5 6 PRO B 315 VAL B 318 -1 N VAL B 316 O ARG B 323
SHEET 3 AA5 6 GLU B 348 PHE B 352 -1 O VAL B 350 N LEU B 317
SHEET 4 AA5 6 MET B 263 SER B 268 -1 N ALA B 267 O ALA B 349
SHEET 5 AA5 6 ALA B 16 ASP B 21 -1 N GLU B 19 O THR B 264
SHEET 6 AA5 6 ARG B 386 VAL B 389 1 O VAL B 387 N ILE B 20
SHEET 1 AA6 8 VAL B 216 HIS B 218 0
SHEET 2 AA6 8 LEU B 173 TRP B 179 1 N LEU B 178 O VAL B 216
SHEET 3 AA6 8 ALA B 136 KCX B 141 1 N ALA B 136 O ARG B 174
SHEET 4 AA6 8 ASP B 113 VAL B 116 1 N VAL B 114 O GLN B 139
SHEET 5 AA6 8 ARG B 92 CYS B 95 1 N ILE B 93 O ASP B 113
SHEET 6 AA6 8 TRP B 68 THR B 71 1 N LEU B 69 O ARG B 92
SHEET 7 AA6 8 ALA B 40 VAL B 44 1 N ALA B 43 O TRP B 68
SHEET 8 AA6 8 LEU B 235 VAL B 236 1 O VAL B 236 N MET B 42
SHEET 1 AA7 3 LEU B 271 VAL B 275 0
SHEET 2 AA7 3 THR B 293 VAL B 298 -1 O LEU B 295 N LYS B 273
SHEET 3 AA7 3 PHE B 334 ASP B 337 -1 O PHE B 334 N VAL B 298
SHEET 1 AA8 2 GLY B 280 VAL B 281 0
SHEET 2 AA8 2 TYR B 287 THR B 288 -1 O TYR B 287 N VAL B 281
SHEET 1 AA9 6 LYS C 321 THR C 324 0
SHEET 2 AA9 6 PRO C 315 VAL C 318 -1 N VAL C 316 O ARG C 323
SHEET 3 AA9 6 GLU C 348 PHE C 352 -1 O VAL C 350 N LEU C 317
SHEET 4 AA9 6 MET C 263 SER C 268 -1 N ALA C 267 O ALA C 349
SHEET 5 AA9 6 ALA C 16 ASP C 21 -1 N GLU C 19 O THR C 264
SHEET 6 AA9 6 ARG C 386 VAL C 389 1 O VAL C 387 N ILE C 20
SHEET 1 AB1 8 VAL C 216 HIS C 218 0
SHEET 2 AB1 8 LEU C 173 TRP C 179 1 N THR C 176 O VAL C 216
SHEET 3 AB1 8 ALA C 136 KCX C 141 1 N ALA C 136 O ARG C 174
SHEET 4 AB1 8 ASP C 113 VAL C 116 1 N VAL C 114 O GLN C 139
SHEET 5 AB1 8 ARG C 92 CYS C 95 1 N ILE C 93 O ASP C 113
SHEET 6 AB1 8 TRP C 68 THR C 71 1 N LEU C 69 O ARG C 92
SHEET 7 AB1 8 ALA C 40 VAL C 44 1 N ALA C 43 O TRP C 68
SHEET 8 AB1 8 LEU C 235 VAL C 236 1 O VAL C 236 N MET C 42
SHEET 1 AB2 3 LEU C 271 VAL C 275 0
SHEET 2 AB2 3 THR C 293 VAL C 298 -1 O LEU C 295 N LYS C 273
SHEET 3 AB2 3 PHE C 334 ASP C 337 -1 O PHE C 334 N VAL C 298
SHEET 1 AB3 2 GLY C 280 VAL C 281 0
SHEET 2 AB3 2 TYR C 287 THR C 288 -1 O TYR C 287 N VAL C 281
SHEET 1 AB4 6 LYS D 321 THR D 324 0
SHEET 2 AB4 6 PRO D 315 VAL D 318 -1 N VAL D 316 O ARG D 323
SHEET 3 AB4 6 GLU D 348 PHE D 352 -1 O VAL D 350 N LEU D 317
SHEET 4 AB4 6 MET D 263 SER D 268 -1 N ALA D 267 O ALA D 349
SHEET 5 AB4 6 ALA D 16 ILE D 20 -1 N GLU D 19 O THR D 264
SHEET 6 AB4 6 ARG D 386 TYR D 388 1 O VAL D 387 N ILE D 20
SHEET 1 AB5 8 VAL D 216 HIS D 218 0
SHEET 2 AB5 8 LEU D 173 TRP D 179 1 N LEU D 178 O VAL D 216
SHEET 3 AB5 8 ALA D 136 KCX D 141 1 N ALA D 136 O ARG D 174
SHEET 4 AB5 8 ASP D 113 VAL D 116 1 N VAL D 114 O GLN D 139
SHEET 5 AB5 8 ARG D 92 CYS D 95 1 N ILE D 93 O ASP D 113
SHEET 6 AB5 8 TRP D 68 THR D 71 1 N LEU D 69 O ARG D 92
SHEET 7 AB5 8 ALA D 40 VAL D 44 1 N ALA D 43 O TRP D 68
SHEET 8 AB5 8 LEU D 235 VAL D 236 1 O VAL D 236 N MET D 42
SHEET 1 AB6 3 LEU D 271 VAL D 275 0
SHEET 2 AB6 3 THR D 293 VAL D 298 -1 O LEU D 295 N LYS D 273
SHEET 3 AB6 3 PHE D 334 ASP D 337 -1 O PHE D 334 N VAL D 298
SHEET 1 AB7 2 GLY D 280 VAL D 281 0
SHEET 2 AB7 2 TYR D 287 THR D 288 -1 O TYR D 287 N VAL D 281
LINK NZ LYS A 46 C4A PLP A 401 1555 1555 1.30
LINK C LEU A 140 N KCX A 141 1555 1555 1.33
LINK C KCX A 141 N ALA A 142 1555 1555 1.33
LINK NZ LYS B 46 C4A PLP B 401 1555 1555 1.27
LINK C LEU B 140 N KCX B 141 1555 1555 1.33
LINK C KCX B 141 N ALA B 142 1555 1555 1.32
LINK NZ LYS C 46 C4A PLP C 401 1555 1555 1.29
LINK C LEU C 140 N KCX C 141 1555 1555 1.33
LINK C KCX C 141 N ALA C 142 1555 1555 1.33
LINK NZ LYS D 46 C4A PLP D 401 1555 1555 1.29
LINK C LEU D 140 N KCX D 141 1555 1555 1.32
LINK C KCX D 141 N ALA D 142 1555 1555 1.30
CISPEP 1 GLU A 84 PRO A 85 0 -0.85
CISPEP 2 GLU B 84 PRO B 85 0 -2.70
CISPEP 3 GLU C 84 PRO C 85 0 -0.03
CISPEP 4 GLU D 84 PRO D 85 0 3.09
SITE 1 AC1 11 LYS A 46 TYR A 50 TRP A 96 TRP A 179
SITE 2 AC1 11 HIS A 181 SER A 222 ARG A 237 PRO A 238
SITE 3 AC1 11 GLY A 239 ILE A 240 TYR A 374
SITE 1 AC2 4 KCX A 141 ASP A 143 LEU A 146 GLY A 150
SITE 1 AC3 4 KCX B 141 ASP B 143 LEU B 146 GLY B 149
SITE 1 AC4 3 KCX C 141 ASP C 143 GLY C 149
SITE 1 AC5 4 KCX D 141 ASP D 143 LEU D 146 GLY D 149
SITE 1 AC6 19 MET A 331 ASP A 332 HOH A 505 VAL B 44
SITE 2 AC6 19 VAL B 45 ALA B 47 ASP B 48 ALA B 49
SITE 3 AC6 19 TYR B 50 GLY B 70 ALA B 72 TRP B 96
SITE 4 AC6 19 TRP B 179 ASN B 221 SER B 222 ARG B 237
SITE 5 AC6 19 GLY B 239 ILE B 240 TYR B 374
SITE 1 AC7 18 VAL C 44 VAL C 45 ALA C 47 ASP C 48
SITE 2 AC7 18 ALA C 49 TYR C 50 GLY C 70 ALA C 72
SITE 3 AC7 18 TRP C 96 TRP C 179 ASN C 221 SER C 222
SITE 4 AC7 18 PRO C 223 ARG C 237 GLY C 239 ILE C 240
SITE 5 AC7 18 TYR C 374 ASP D 332
SITE 1 AC8 19 MET C 331 ASP C 332 VAL D 44 VAL D 45
SITE 2 AC8 19 ALA D 47 ASP D 48 ALA D 49 TYR D 50
SITE 3 AC8 19 GLY D 70 ALA D 72 TRP D 96 KCX D 141
SITE 4 AC8 19 TRP D 179 ASN D 221 SER D 222 ARG D 237
SITE 5 AC8 19 GLY D 239 ILE D 240 TYR D 374
CRYST1 78.960 87.170 109.626 90.00 102.26 90.00 P 1 21 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 0.012665 0.000000 0.002753 0.00000
SCALE2 0.000000 0.011472 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009335 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
