HEADER ISOMERASE 02-NOV-07 3B8V
TITLE CRYSTAL STRUCTURE OF ESCHERICHIA COLI ALAINE RACEMASE MUTANT E221K
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;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: JM109;
SOURCE 5 GENE: ALR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALPHA/BETA BARREL, CELL SHAPE, CELL WALL BIOGENESIS/DEGRADATION,
KEYWDS 2 ISOMERASE, PEPTIDOGLYCAN SYNTHESIS, PYRIDOXAL PHOSPHATE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.WU,T.HU,L.ZHANG,H.JIANG,X.SHEN
REVDAT 3 13-JUL-11 3B8V 1 VERSN
REVDAT 2 24-FEB-09 3B8V 1 VERSN
REVDAT 1 08-JUL-08 3B8V 0
JRNL AUTH D.WU,T.HU,L.ZHANG,J.CHEN,J.DU,J.DING,H.JIANG,X.SHEN
JRNL TITL RESIDUES ASP164 AND GLU165 AT THE SUBSTRATE ENTRYWAY
JRNL TITL 2 FUNCTION POTENTLY IN SUBSTRATE ORIENTATION OF ALANINE
JRNL TITL 3 RACEMASE FROM E. COLI: ENZYMATIC CHARACTERIZATION WITH
JRNL TITL 4 CRYSTAL STRUCTURE ANALYSIS
JRNL REF PROTEIN SCI. V. 17 1066 2008
JRNL REFN ISSN 0961-8368
JRNL PMID 18434499
JRNL DOI 10.1110/PS.083495908
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 6.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 62214
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.600
REMARK 3 FREE R VALUE TEST SET COUNT : 5943
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10939
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 115
REMARK 3 SOLVENT ATOMS : 489
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.49000
REMARK 3 B22 (A**2) : -2.49000
REMARK 3 B33 (A**2) : 4.98000
REMARK 3 B12 (A**2) : -3.43500
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.961 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.619 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.448 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.175 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 41.54
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NEW_PLP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THIS IS A TWINNED STRUCTURE, THE DETWIN
REMARK 3 FRACTION IS 0.400, AND OPERATOR IS 'H, -H-K, -L'.
REMARK 4
REMARK 4 3B8V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-07.
REMARK 100 THE RCSB ID CODE IS RCSB045224.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
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 : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62549
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 164.399
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.300
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : 0.14100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.80
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
REMARK 200 R SYM FOR SHELL (I) : 0.42500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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 2RJG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 1.6M AMMONIUM SULFATE,
REMARK 280 PH6.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z
REMARK 290 6555 X-Y,X,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 -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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
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 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: 8270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.1 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: 7070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.9 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 -19
REMARK 465 GLY A -18
REMARK 465 SER 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 B -19
REMARK 465 GLY B -18
REMARK 465 SER 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 C -19
REMARK 465 GLY C -18
REMARK 465 SER 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 GLN C 2
REMARK 465 ALA C 335
REMARK 465 GLU C 336
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER 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 GLN D 2
REMARK 465 ALA D 335
REMARK 465 GLU D 336
REMARK 465 MET D 337
REMARK 465 THR D 338
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 CE LYS A 34 C4A PLP A 1001 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 147 CB CYS B 147 SG -0.136
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 11 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 11 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 59 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG A 85 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 129 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 129 NE - CZ - NH1 ANGL. DEV. = -9.9 DEGREES
REMARK 500 ARG A 129 NE - CZ - NH2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ALA A 314 N - CA - C ANGL. DEV. = -17.5 DEGREES
REMARK 500 GLN A 315 N - CA - CB ANGL. DEV. = -11.8 DEGREES
REMARK 500 ARG B 59 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 85 CD - NE - CZ ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG B 85 NE - CZ - NH1 ANGL. DEV. = -9.7 DEGREES
REMARK 500 ARG B 85 NE - CZ - NH2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG B 129 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 GLN B 315 N - CA - CB ANGL. DEV. = -18.8 DEGREES
REMARK 500 ARG C 65 CD - NE - CZ ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG C 65 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG C 65 NE - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG C 85 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG C 85 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG C 129 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG C 223 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG C 223 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ALA C 314 CB - CA - C ANGL. DEV. = -13.7 DEGREES
REMARK 500 GLN C 315 N - CA - CB ANGL. DEV. = -19.6 DEGREES
REMARK 500 ARG C 333 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG D 59 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG D 65 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG D 65 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG D 65 NE - CZ - NH2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 ARG D 85 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG D 85 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG D 129 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG D 223 CD - NE - CZ ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG D 223 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG D 223 NE - CZ - NH2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ALA D 314 N - CA - C ANGL. DEV. = -19.3 DEGREES
REMARK 500 ARG D 333 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG D 333 NE - CZ - NH2 ANGL. DEV. = -3.0 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 3 -147.49 -90.38
REMARK 500 ARG A 129 -73.56 -113.55
REMARK 500 ARG A 162 45.93 -144.73
REMARK 500 ILE A 191 -18.80 -141.96
REMARK 500 ALA A 193 -154.82 -113.20
REMARK 500 PHE A 205 -136.62 47.48
REMARK 500 SER A 239 -157.83 -166.09
REMARK 500 ALA A 243 145.12 -174.82
REMARK 500 ALA A 318 131.34 -29.88
REMARK 500 TRP A 325 144.22 -172.64
REMARK 500 ALA B 3 -153.87 -106.58
REMARK 500 ARG B 129 -72.38 -113.27
REMARK 500 ARG B 162 45.19 -145.42
REMARK 500 ILE B 191 -20.14 -140.43
REMARK 500 ALA B 193 -155.13 -112.73
REMARK 500 PHE B 205 -137.50 47.21
REMARK 500 LYS B 221 63.21 -106.45
REMARK 500 ARG B 223 -8.32 86.24
REMARK 500 SER B 239 -157.92 -164.97
REMARK 500 ALA B 243 144.46 -175.03
REMARK 500 TRP B 325 147.97 -171.85
REMARK 500 GLU B 327 -72.02 -49.78
REMARK 500 LEU B 329 88.40 -158.78
REMARK 500 GLU C 61 -57.01 -9.83
REMARK 500 ARG C 129 -73.02 -111.64
REMARK 500 ARG C 162 44.34 -144.90
REMARK 500 ALA C 193 -154.71 -112.49
REMARK 500 PHE C 205 -137.23 46.49
REMARK 500 SER C 239 -155.62 -165.69
REMARK 500 ALA C 243 144.28 -178.16
REMARK 500 TRP C 325 148.82 -172.19
REMARK 500 LEU C 329 88.81 -159.99
REMARK 500 THR C 338 178.85 -55.48
REMARK 500 LYS C 339 57.76 -104.79
REMARK 500 ALA D 24 62.60 -110.63
REMARK 500 LYS D 73 168.78 -41.84
REMARK 500 ARG D 129 -71.74 -113.41
REMARK 500 ARG D 162 44.43 -145.94
REMARK 500 ILE D 191 -18.87 -140.78
REMARK 500 ALA D 193 -155.27 -114.26
REMARK 500 PHE D 205 -137.19 48.53
REMARK 500 ASP D 222 40.07 -74.83
REMARK 500 ARG D 223 26.69 45.10
REMARK 500 SER D 239 -156.88 -165.77
REMARK 500 ALA D 243 145.21 -174.91
REMARK 500 TRP D 325 146.82 -172.66
REMARK 500 GLU D 327 -72.55 -48.96
REMARK 500 LEU D 329 87.26 -159.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 221 ASP A 222 144.26
REMARK 500 LEU C 60 GLU C 61 140.48
REMARK 500 PRO C 219 LEU C 220 -149.06
REMARK 500 LYS C 221 ASP C 222 -131.02
REMARK 500 LYS D 221 ASP D 222 -134.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 300 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLN A 202 24.5 L L OUTSIDE RANGE
REMARK 500 GLU A 327 24.6 L L OUTSIDE RANGE
REMARK 500 THR B 72 21.7 L L OUTSIDE RANGE
REMARK 500 GLN B 315 47.2 L L OUTSIDE RANGE
REMARK 500 GLN C 202 24.8 L L OUTSIDE RANGE
REMARK 500 LYS C 221 21.8 L L OUTSIDE RANGE
REMARK 500 GLN C 315 46.8 L L OUTSIDE RANGE
REMARK 500 ILE D 8 21.2 L L OUTSIDE RANGE
REMARK 500 ALA D 314 45.1 L L OUTSIDE RANGE
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 A1130 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH B1158 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH C1049 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH D1085 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH D1088 DISTANCE = 5.21 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 360
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 361
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 363
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 363
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP C 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RJG RELATED DB: PDB
REMARK 900 THE WILD-TYPE PROTEIN
REMARK 900 RELATED ID: 2RJH RELATED DB: PDB
REMARK 900 THE WILD-TYPE PROTEIN COMPLEXED WITH D-CYCLOSERINE
REMARK 900 RELATED ID: 3B8T RELATED DB: PDB
REMARK 900 MUTANT P219A
REMARK 900 RELATED ID: 3B8U RELATED DB: PDB
REMARK 900 MUTANT E221A
REMARK 900 RELATED ID: 3B8W RELATED DB: PDB
REMARK 900 MUTANT E221P
DBREF 3B8V A 1 359 UNP P0A6B4 ALR1_ECOLI 1 359
DBREF 3B8V B 1 359 UNP P0A6B4 ALR1_ECOLI 1 359
DBREF 3B8V C 1 359 UNP P0A6B4 ALR1_ECOLI 1 359
DBREF 3B8V D 1 359 UNP P0A6B4 ALR1_ECOLI 1 359
SEQADV 3B8V MET A -19 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY A -18 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER A -17 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER A -16 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS A -15 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS A -14 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS A -13 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS A -12 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS A -11 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS A -10 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER A -9 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER A -8 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY A -7 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V LEU A -6 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V VAL A -5 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V PRO A -4 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V ARG A -3 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY A -2 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER A -1 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS A 0 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V LYS A 221 UNP P0A6B4 GLU 221 ENGINEERED
SEQADV 3B8V MET B -19 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY B -18 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER B -17 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER B -16 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS B -15 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS B -14 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS B -13 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS B -12 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS B -11 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS B -10 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER B -9 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER B -8 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY B -7 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V LEU B -6 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V VAL B -5 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V PRO B -4 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V ARG B -3 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY B -2 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER B -1 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS B 0 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V LYS B 221 UNP P0A6B4 GLU 221 ENGINEERED
SEQADV 3B8V MET C -19 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY C -18 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER C -17 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER C -16 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS C -15 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS C -14 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS C -13 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS C -12 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS C -11 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS C -10 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER C -9 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER C -8 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY C -7 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V LEU C -6 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V VAL C -5 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V PRO C -4 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V ARG C -3 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY C -2 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER C -1 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS C 0 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V LYS C 221 UNP P0A6B4 GLU 221 ENGINEERED
SEQADV 3B8V MET D -19 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY D -18 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER D -17 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER D -16 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS D -15 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS D -14 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS D -13 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS D -12 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS D -11 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS D -10 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER D -9 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER D -8 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY D -7 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V LEU D -6 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V VAL D -5 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V PRO D -4 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V ARG D -3 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V GLY D -2 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V SER D -1 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V HIS D 0 UNP P0A6B4 EXPRESSION TAG
SEQADV 3B8V LYS D 221 UNP P0A6B4 GLU 221 ENGINEERED
SEQRES 1 A 379 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 379 LEU VAL PRO ARG GLY SER HIS MET GLN ALA ALA THR VAL
SEQRES 3 A 379 VAL ILE ASN ARG ARG ALA LEU ARG HIS ASN LEU GLN ARG
SEQRES 4 A 379 LEU ARG GLU LEU ALA PRO ALA SER LYS MET VAL ALA VAL
SEQRES 5 A 379 VAL LYS ALA ASN ALA TYR GLY HIS GLY LEU LEU GLU THR
SEQRES 6 A 379 ALA ARG THR LEU PRO ASP ALA ASP ALA PHE GLY VAL ALA
SEQRES 7 A 379 ARG LEU GLU GLU ALA LEU ARG LEU ARG ALA GLY GLY ILE
SEQRES 8 A 379 THR LYS PRO VAL LEU LEU LEU GLU GLY PHE PHE ASP ALA
SEQRES 9 A 379 ARG ASP LEU PRO THR ILE SER ALA GLN HIS PHE HIS THR
SEQRES 10 A 379 ALA VAL HIS ASN GLU GLU GLN LEU ALA ALA LEU GLU GLU
SEQRES 11 A 379 ALA SER LEU ASP GLU PRO VAL THR VAL TRP MET KCX LEU
SEQRES 12 A 379 ASP THR GLY MET HIS ARG LEU GLY VAL ARG PRO GLU GLN
SEQRES 13 A 379 ALA GLU ALA PHE TYR HIS ARG LEU THR GLN CYS LYS ASN
SEQRES 14 A 379 VAL ARG GLN PRO VAL ASN ILE VAL SER HIS PHE ALA ARG
SEQRES 15 A 379 ALA ASP GLU PRO LYS CYS GLY ALA THR GLU LYS GLN LEU
SEQRES 16 A 379 ALA ILE PHE ASN THR PHE CYS GLU GLY LYS PRO GLY GLN
SEQRES 17 A 379 ARG SER ILE ALA ALA SER GLY GLY ILE LEU LEU TRP PRO
SEQRES 18 A 379 GLN SER HIS PHE ASP TRP VAL ARG PRO GLY ILE ILE LEU
SEQRES 19 A 379 TYR GLY VAL SER PRO LEU LYS ASP ARG SER THR GLY ALA
SEQRES 20 A 379 ASP PHE GLY CYS GLN PRO VAL MET SER LEU THR SER SER
SEQRES 21 A 379 LEU ILE ALA VAL ARG GLU HIS LYS ALA GLY GLU PRO VAL
SEQRES 22 A 379 GLY TYR GLY GLY THR TRP VAL SER GLU ARG ASP THR ARG
SEQRES 23 A 379 LEU GLY VAL VAL ALA MET GLY TYR GLY ASP GLY TYR PRO
SEQRES 24 A 379 ARG ALA ALA PRO SER GLY THR PRO VAL LEU VAL ASN GLY
SEQRES 25 A 379 ARG GLU VAL PRO ILE VAL GLY ARG VAL ALA MET ASP MET
SEQRES 26 A 379 ILE CYS VAL ASP LEU GLY PRO GLN ALA GLN ASP LYS ALA
SEQRES 27 A 379 GLY ASP PRO VAL ILE LEU TRP GLY GLU GLY LEU PRO VAL
SEQRES 28 A 379 GLU ARG ILE ALA GLU MET THR LYS VAL SER ALA TYR GLU
SEQRES 29 A 379 LEU ILE THR ARG LEU THR SER ARG VAL ALA MET LYS TYR
SEQRES 30 A 379 VAL ASP
SEQRES 1 B 379 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 379 LEU VAL PRO ARG GLY SER HIS MET GLN ALA ALA THR VAL
SEQRES 3 B 379 VAL ILE ASN ARG ARG ALA LEU ARG HIS ASN LEU GLN ARG
SEQRES 4 B 379 LEU ARG GLU LEU ALA PRO ALA SER LYS MET VAL ALA VAL
SEQRES 5 B 379 VAL LYS ALA ASN ALA TYR GLY HIS GLY LEU LEU GLU THR
SEQRES 6 B 379 ALA ARG THR LEU PRO ASP ALA ASP ALA PHE GLY VAL ALA
SEQRES 7 B 379 ARG LEU GLU GLU ALA LEU ARG LEU ARG ALA GLY GLY ILE
SEQRES 8 B 379 THR LYS PRO VAL LEU LEU LEU GLU GLY PHE PHE ASP ALA
SEQRES 9 B 379 ARG ASP LEU PRO THR ILE SER ALA GLN HIS PHE HIS THR
SEQRES 10 B 379 ALA VAL HIS ASN GLU GLU GLN LEU ALA ALA LEU GLU GLU
SEQRES 11 B 379 ALA SER LEU ASP GLU PRO VAL THR VAL TRP MET KCX LEU
SEQRES 12 B 379 ASP THR GLY MET HIS ARG LEU GLY VAL ARG PRO GLU GLN
SEQRES 13 B 379 ALA GLU ALA PHE TYR HIS ARG LEU THR GLN CYS LYS ASN
SEQRES 14 B 379 VAL ARG GLN PRO VAL ASN ILE VAL SER HIS PHE ALA ARG
SEQRES 15 B 379 ALA ASP GLU PRO LYS CYS GLY ALA THR GLU LYS GLN LEU
SEQRES 16 B 379 ALA ILE PHE ASN THR PHE CYS GLU GLY LYS PRO GLY GLN
SEQRES 17 B 379 ARG SER ILE ALA ALA SER GLY GLY ILE LEU LEU TRP PRO
SEQRES 18 B 379 GLN SER HIS PHE ASP TRP VAL ARG PRO GLY ILE ILE LEU
SEQRES 19 B 379 TYR GLY VAL SER PRO LEU LYS ASP ARG SER THR GLY ALA
SEQRES 20 B 379 ASP PHE GLY CYS GLN PRO VAL MET SER LEU THR SER SER
SEQRES 21 B 379 LEU ILE ALA VAL ARG GLU HIS LYS ALA GLY GLU PRO VAL
SEQRES 22 B 379 GLY TYR GLY GLY THR TRP VAL SER GLU ARG ASP THR ARG
SEQRES 23 B 379 LEU GLY VAL VAL ALA MET GLY TYR GLY ASP GLY TYR PRO
SEQRES 24 B 379 ARG ALA ALA PRO SER GLY THR PRO VAL LEU VAL ASN GLY
SEQRES 25 B 379 ARG GLU VAL PRO ILE VAL GLY ARG VAL ALA MET ASP MET
SEQRES 26 B 379 ILE CYS VAL ASP LEU GLY PRO GLN ALA GLN ASP LYS ALA
SEQRES 27 B 379 GLY ASP PRO VAL ILE LEU TRP GLY GLU GLY LEU PRO VAL
SEQRES 28 B 379 GLU ARG ILE ALA GLU MET THR LYS VAL SER ALA TYR GLU
SEQRES 29 B 379 LEU ILE THR ARG LEU THR SER ARG VAL ALA MET LYS TYR
SEQRES 30 B 379 VAL ASP
SEQRES 1 C 379 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 379 LEU VAL PRO ARG GLY SER HIS MET GLN ALA ALA THR VAL
SEQRES 3 C 379 VAL ILE ASN ARG ARG ALA LEU ARG HIS ASN LEU GLN ARG
SEQRES 4 C 379 LEU ARG GLU LEU ALA PRO ALA SER LYS MET VAL ALA VAL
SEQRES 5 C 379 VAL LYS ALA ASN ALA TYR GLY HIS GLY LEU LEU GLU THR
SEQRES 6 C 379 ALA ARG THR LEU PRO ASP ALA ASP ALA PHE GLY VAL ALA
SEQRES 7 C 379 ARG LEU GLU GLU ALA LEU ARG LEU ARG ALA GLY GLY ILE
SEQRES 8 C 379 THR LYS PRO VAL LEU LEU LEU GLU GLY PHE PHE ASP ALA
SEQRES 9 C 379 ARG ASP LEU PRO THR ILE SER ALA GLN HIS PHE HIS THR
SEQRES 10 C 379 ALA VAL HIS ASN GLU GLU GLN LEU ALA ALA LEU GLU GLU
SEQRES 11 C 379 ALA SER LEU ASP GLU PRO VAL THR VAL TRP MET KCX LEU
SEQRES 12 C 379 ASP THR GLY MET HIS ARG LEU GLY VAL ARG PRO GLU GLN
SEQRES 13 C 379 ALA GLU ALA PHE TYR HIS ARG LEU THR GLN CYS LYS ASN
SEQRES 14 C 379 VAL ARG GLN PRO VAL ASN ILE VAL SER HIS PHE ALA ARG
SEQRES 15 C 379 ALA ASP GLU PRO LYS CYS GLY ALA THR GLU LYS GLN LEU
SEQRES 16 C 379 ALA ILE PHE ASN THR PHE CYS GLU GLY LYS PRO GLY GLN
SEQRES 17 C 379 ARG SER ILE ALA ALA SER GLY GLY ILE LEU LEU TRP PRO
SEQRES 18 C 379 GLN SER HIS PHE ASP TRP VAL ARG PRO GLY ILE ILE LEU
SEQRES 19 C 379 TYR GLY VAL SER PRO LEU LYS ASP ARG SER THR GLY ALA
SEQRES 20 C 379 ASP PHE GLY CYS GLN PRO VAL MET SER LEU THR SER SER
SEQRES 21 C 379 LEU ILE ALA VAL ARG GLU HIS LYS ALA GLY GLU PRO VAL
SEQRES 22 C 379 GLY TYR GLY GLY THR TRP VAL SER GLU ARG ASP THR ARG
SEQRES 23 C 379 LEU GLY VAL VAL ALA MET GLY TYR GLY ASP GLY TYR PRO
SEQRES 24 C 379 ARG ALA ALA PRO SER GLY THR PRO VAL LEU VAL ASN GLY
SEQRES 25 C 379 ARG GLU VAL PRO ILE VAL GLY ARG VAL ALA MET ASP MET
SEQRES 26 C 379 ILE CYS VAL ASP LEU GLY PRO GLN ALA GLN ASP LYS ALA
SEQRES 27 C 379 GLY ASP PRO VAL ILE LEU TRP GLY GLU GLY LEU PRO VAL
SEQRES 28 C 379 GLU ARG ILE ALA GLU MET THR LYS VAL SER ALA TYR GLU
SEQRES 29 C 379 LEU ILE THR ARG LEU THR SER ARG VAL ALA MET LYS TYR
SEQRES 30 C 379 VAL ASP
SEQRES 1 D 379 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 379 LEU VAL PRO ARG GLY SER HIS MET GLN ALA ALA THR VAL
SEQRES 3 D 379 VAL ILE ASN ARG ARG ALA LEU ARG HIS ASN LEU GLN ARG
SEQRES 4 D 379 LEU ARG GLU LEU ALA PRO ALA SER LYS MET VAL ALA VAL
SEQRES 5 D 379 VAL LYS ALA ASN ALA TYR GLY HIS GLY LEU LEU GLU THR
SEQRES 6 D 379 ALA ARG THR LEU PRO ASP ALA ASP ALA PHE GLY VAL ALA
SEQRES 7 D 379 ARG LEU GLU GLU ALA LEU ARG LEU ARG ALA GLY GLY ILE
SEQRES 8 D 379 THR LYS PRO VAL LEU LEU LEU GLU GLY PHE PHE ASP ALA
SEQRES 9 D 379 ARG ASP LEU PRO THR ILE SER ALA GLN HIS PHE HIS THR
SEQRES 10 D 379 ALA VAL HIS ASN GLU GLU GLN LEU ALA ALA LEU GLU GLU
SEQRES 11 D 379 ALA SER LEU ASP GLU PRO VAL THR VAL TRP MET KCX LEU
SEQRES 12 D 379 ASP THR GLY MET HIS ARG LEU GLY VAL ARG PRO GLU GLN
SEQRES 13 D 379 ALA GLU ALA PHE TYR HIS ARG LEU THR GLN CYS LYS ASN
SEQRES 14 D 379 VAL ARG GLN PRO VAL ASN ILE VAL SER HIS PHE ALA ARG
SEQRES 15 D 379 ALA ASP GLU PRO LYS CYS GLY ALA THR GLU LYS GLN LEU
SEQRES 16 D 379 ALA ILE PHE ASN THR PHE CYS GLU GLY LYS PRO GLY GLN
SEQRES 17 D 379 ARG SER ILE ALA ALA SER GLY GLY ILE LEU LEU TRP PRO
SEQRES 18 D 379 GLN SER HIS PHE ASP TRP VAL ARG PRO GLY ILE ILE LEU
SEQRES 19 D 379 TYR GLY VAL SER PRO LEU LYS ASP ARG SER THR GLY ALA
SEQRES 20 D 379 ASP PHE GLY CYS GLN PRO VAL MET SER LEU THR SER SER
SEQRES 21 D 379 LEU ILE ALA VAL ARG GLU HIS LYS ALA GLY GLU PRO VAL
SEQRES 22 D 379 GLY TYR GLY GLY THR TRP VAL SER GLU ARG ASP THR ARG
SEQRES 23 D 379 LEU GLY VAL VAL ALA MET GLY TYR GLY ASP GLY TYR PRO
SEQRES 24 D 379 ARG ALA ALA PRO SER GLY THR PRO VAL LEU VAL ASN GLY
SEQRES 25 D 379 ARG GLU VAL PRO ILE VAL GLY ARG VAL ALA MET ASP MET
SEQRES 26 D 379 ILE CYS VAL ASP LEU GLY PRO GLN ALA GLN ASP LYS ALA
SEQRES 27 D 379 GLY ASP PRO VAL ILE LEU TRP GLY GLU GLY LEU PRO VAL
SEQRES 28 D 379 GLU ARG ILE ALA GLU MET THR LYS VAL SER ALA TYR GLU
SEQRES 29 D 379 LEU ILE THR ARG LEU THR SER ARG VAL ALA MET LYS TYR
SEQRES 30 D 379 VAL ASP
MODRES 3B8V KCX A 122 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3B8V KCX B 122 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3B8V KCX C 122 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 3B8V KCX D 122 LYS LYSINE NZ-CARBOXYLIC ACID
HET KCX A 122 12
HET KCX B 122 12
HET KCX C 122 12
HET KCX D 122 12
HET SO4 A 360 5
HET SO4 A 361 5
HET SO4 A 362 5
HET SO4 A 363 5
HET SO4 B 360 5
HET SO4 B 361 5
HET SO4 B 362 5
HET SO4 B 363 5
HET SO4 C 360 5
HET SO4 C 361 5
HET SO4 C 362 5
HET PLP A1001 15
HET PLP B1001 15
HET PLP C1001 15
HET PLP D1001 15
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM SO4 SULFATE ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 1 KCX 4(C7 H14 N2 O4)
FORMUL 5 SO4 11(O4 S 2-)
FORMUL 16 PLP 4(C8 H10 N O6 P)
FORMUL 20 HOH *489(H2 O)
HELIX 1 1 ARG A 10 ALA A 24 1 15
HELIX 2 2 VAL A 33 GLY A 39 1 7
HELIX 3 3 GLY A 41 LEU A 49 1 9
HELIX 4 4 ARG A 59 GLY A 69 1 11
HELIX 5 5 ASP A 83 ARG A 85 5 3
HELIX 6 6 ASP A 86 GLN A 93 1 8
HELIX 7 7 ASN A 101 ALA A 111 1 11
HELIX 8 8 ARG A 133 THR A 145 1 13
HELIX 9 9 GLY A 169 GLU A 183 1 15
HELIX 10 10 ALA A 193 TRP A 200 1 8
HELIX 11 11 PRO A 201 HIS A 204 5 4
HELIX 12 12 GLY A 211 GLY A 216 5 6
HELIX 13 13 THR A 225 GLY A 230 5 6
HELIX 14 14 GLY A 254 THR A 258 5 5
HELIX 15 15 PRO A 330 LYS A 339 1 10
HELIX 16 16 SER A 341 ARG A 348 1 8
HELIX 17 17 ARG B 10 ALA B 24 1 15
HELIX 18 18 VAL B 33 GLY B 39 1 7
HELIX 19 19 GLY B 41 LEU B 49 1 9
HELIX 20 20 ARG B 59 GLY B 69 1 11
HELIX 21 21 ASP B 83 ARG B 85 5 3
HELIX 22 22 ASP B 86 GLN B 93 1 8
HELIX 23 23 ASN B 101 ALA B 111 1 11
HELIX 24 24 ARG B 133 GLN B 146 1 14
HELIX 25 25 GLY B 169 GLU B 183 1 15
HELIX 26 26 ALA B 193 TRP B 200 1 8
HELIX 27 27 PRO B 201 HIS B 204 5 4
HELIX 28 28 GLY B 211 GLY B 216 5 6
HELIX 29 29 THR B 225 GLY B 230 5 6
HELIX 30 30 GLY B 254 THR B 258 5 5
HELIX 31 31 PRO B 330 LYS B 339 1 10
HELIX 32 32 SER B 341 ARG B 348 1 8
HELIX 33 33 ARG C 10 ALA C 24 1 15
HELIX 34 34 VAL C 33 HIS C 40 1 8
HELIX 35 35 GLY C 41 THR C 48 1 8
HELIX 36 36 ARG C 59 GLY C 69 1 11
HELIX 37 37 ASP C 83 ARG C 85 5 3
HELIX 38 38 ASP C 86 GLN C 93 1 8
HELIX 39 39 ASN C 101 ALA C 111 1 11
HELIX 40 40 ARG C 133 GLN C 146 1 14
HELIX 41 41 GLY C 169 GLU C 183 1 15
HELIX 42 42 ALA C 193 TRP C 200 1 8
HELIX 43 43 PRO C 201 HIS C 204 5 4
HELIX 44 44 GLY C 211 GLY C 216 5 6
HELIX 45 45 THR C 225 PHE C 229 5 5
HELIX 46 46 GLY C 254 THR C 258 5 5
HELIX 47 47 SER C 341 ARG C 348 1 8
HELIX 48 48 ARG D 10 ALA D 24 1 15
HELIX 49 49 VAL D 33 HIS D 40 1 8
HELIX 50 50 GLY D 41 LEU D 49 1 9
HELIX 51 51 ARG D 59 GLY D 69 1 11
HELIX 52 52 ASP D 83 ARG D 85 5 3
HELIX 53 53 ASP D 86 GLN D 93 1 8
HELIX 54 54 ASN D 101 ALA D 111 1 11
HELIX 55 55 ARG D 133 THR D 145 1 13
HELIX 56 56 GLY D 169 GLU D 183 1 15
HELIX 57 57 ALA D 193 TRP D 200 1 8
HELIX 58 58 PRO D 201 HIS D 204 5 4
HELIX 59 59 GLY D 211 GLY D 216 5 6
HELIX 60 60 THR D 225 GLY D 230 5 6
HELIX 61 61 GLY D 254 THR D 258 5 5
HELIX 62 62 SER D 341 ARG D 348 1 8
SHEET 1 A 6 ARG A 293 PRO A 296 0
SHEET 2 A 6 PRO A 287 VAL A 290 -1 N VAL A 288 O VAL A 295
SHEET 3 A 6 PRO A 321 TRP A 325 -1 O ILE A 323 N LEU A 289
SHEET 4 A 6 MET A 235 HIS A 247 -1 N LEU A 237 O LEU A 324
SHEET 5 A 6 THR A 265 VAL A 270 -1 O VAL A 269 N ILE A 242
SHEET 6 A 6 ILE A 306 ASP A 309 -1 O ILE A 306 N VAL A 270
SHEET 1 B 6 ARG A 293 PRO A 296 0
SHEET 2 B 6 PRO A 287 VAL A 290 -1 N VAL A 288 O VAL A 295
SHEET 3 B 6 PRO A 321 TRP A 325 -1 O ILE A 323 N LEU A 289
SHEET 4 B 6 MET A 235 HIS A 247 -1 N LEU A 237 O LEU A 324
SHEET 5 B 6 THR A 5 ASN A 9 -1 N THR A 5 O THR A 238
SHEET 6 B 6 ALA A 354 VAL A 358 1 O LYS A 356 N VAL A 6
SHEET 1 C 8 ARG A 189 SER A 190 0
SHEET 2 C 8 ASN A 155 VAL A 157 1 N ILE A 156 O SER A 190
SHEET 3 C 8 VAL A 119 KCX A 122 1 N MET A 121 O ASN A 155
SHEET 4 C 8 PHE A 95 VAL A 99 1 N THR A 97 O TRP A 120
SHEET 5 C 8 VAL A 75 LEU A 77 1 N LEU A 77 O HIS A 96
SHEET 6 C 8 ALA A 54 VAL A 57 1 N PHE A 55 O LEU A 76
SHEET 7 C 8 LYS A 28 VAL A 32 1 N ALA A 31 O GLY A 56
SHEET 8 C 8 TRP A 207 VAL A 208 1 O VAL A 208 N LYS A 28
SHEET 1 D 2 PRO A 252 VAL A 253 0
SHEET 2 D 2 TRP A 259 VAL A 260 -1 O TRP A 259 N VAL A 253
SHEET 1 E 6 ARG B 293 PRO B 296 0
SHEET 2 E 6 PRO B 287 VAL B 290 -1 N VAL B 290 O ARG B 293
SHEET 3 E 6 PRO B 321 TRP B 325 -1 O ILE B 323 N LEU B 289
SHEET 4 E 6 MET B 235 HIS B 247 -1 N LEU B 237 O LEU B 324
SHEET 5 E 6 THR B 265 VAL B 270 -1 O VAL B 269 N ILE B 242
SHEET 6 E 6 ILE B 306 ASP B 309 -1 O ILE B 306 N VAL B 270
SHEET 1 F 6 ARG B 293 PRO B 296 0
SHEET 2 F 6 PRO B 287 VAL B 290 -1 N VAL B 290 O ARG B 293
SHEET 3 F 6 PRO B 321 TRP B 325 -1 O ILE B 323 N LEU B 289
SHEET 4 F 6 MET B 235 HIS B 247 -1 N LEU B 237 O LEU B 324
SHEET 5 F 6 THR B 5 ASN B 9 -1 N THR B 5 O THR B 238
SHEET 6 F 6 ALA B 354 VAL B 358 1 O LYS B 356 N ILE B 8
SHEET 1 G 8 ARG B 189 SER B 190 0
SHEET 2 G 8 ASN B 155 VAL B 157 1 N ILE B 156 O SER B 190
SHEET 3 G 8 VAL B 119 KCX B 122 1 N MET B 121 O ASN B 155
SHEET 4 G 8 PHE B 95 VAL B 99 1 N THR B 97 O TRP B 120
SHEET 5 G 8 VAL B 75 LEU B 77 1 N LEU B 77 O HIS B 96
SHEET 6 G 8 ALA B 54 VAL B 57 1 N PHE B 55 O LEU B 76
SHEET 7 G 8 LYS B 28 VAL B 32 1 N ALA B 31 O GLY B 56
SHEET 8 G 8 TRP B 207 VAL B 208 1 O VAL B 208 N LYS B 28
SHEET 1 H 2 PRO B 252 VAL B 253 0
SHEET 2 H 2 TRP B 259 VAL B 260 -1 O TRP B 259 N VAL B 253
SHEET 1 I 6 ARG C 293 PRO C 296 0
SHEET 2 I 6 PRO C 287 VAL C 290 -1 N VAL C 290 O ARG C 293
SHEET 3 I 6 PRO C 321 TRP C 325 -1 O ILE C 323 N LEU C 289
SHEET 4 I 6 MET C 235 HIS C 247 -1 N LEU C 237 O LEU C 324
SHEET 5 I 6 THR C 265 VAL C 270 -1 O VAL C 269 N ILE C 242
SHEET 6 I 6 ILE C 306 ASP C 309 -1 O ILE C 306 N VAL C 270
SHEET 1 J 6 ARG C 293 PRO C 296 0
SHEET 2 J 6 PRO C 287 VAL C 290 -1 N VAL C 290 O ARG C 293
SHEET 3 J 6 PRO C 321 TRP C 325 -1 O ILE C 323 N LEU C 289
SHEET 4 J 6 MET C 235 HIS C 247 -1 N LEU C 237 O LEU C 324
SHEET 5 J 6 THR C 5 ASN C 9 -1 N THR C 5 O THR C 238
SHEET 6 J 6 ALA C 354 VAL C 358 1 O LYS C 356 N ILE C 8
SHEET 1 K 8 ARG C 189 SER C 190 0
SHEET 2 K 8 ASN C 155 VAL C 157 1 N ILE C 156 O SER C 190
SHEET 3 K 8 VAL C 119 KCX C 122 1 N MET C 121 O ASN C 155
SHEET 4 K 8 PHE C 95 VAL C 99 1 N THR C 97 O TRP C 120
SHEET 5 K 8 VAL C 75 LEU C 77 1 N LEU C 77 O HIS C 96
SHEET 6 K 8 ALA C 54 VAL C 57 1 N PHE C 55 O LEU C 76
SHEET 7 K 8 LYS C 28 VAL C 32 1 N ALA C 31 O ALA C 54
SHEET 8 K 8 TRP C 207 VAL C 208 1 O VAL C 208 N LYS C 28
SHEET 1 L 2 PRO C 252 VAL C 253 0
SHEET 2 L 2 TRP C 259 VAL C 260 -1 O TRP C 259 N VAL C 253
SHEET 1 M 6 ARG D 293 PRO D 296 0
SHEET 2 M 6 PRO D 287 VAL D 290 -1 N VAL D 290 O ARG D 293
SHEET 3 M 6 PRO D 321 TRP D 325 -1 O ILE D 323 N LEU D 289
SHEET 4 M 6 MET D 235 HIS D 247 -1 N LEU D 237 O LEU D 324
SHEET 5 M 6 THR D 265 VAL D 270 -1 O VAL D 269 N ILE D 242
SHEET 6 M 6 ILE D 306 ASP D 309 -1 O ILE D 306 N VAL D 270
SHEET 1 N 6 ARG D 293 PRO D 296 0
SHEET 2 N 6 PRO D 287 VAL D 290 -1 N VAL D 290 O ARG D 293
SHEET 3 N 6 PRO D 321 TRP D 325 -1 O ILE D 323 N LEU D 289
SHEET 4 N 6 MET D 235 HIS D 247 -1 N LEU D 237 O LEU D 324
SHEET 5 N 6 THR D 5 ASN D 9 -1 N THR D 5 O THR D 238
SHEET 6 N 6 ALA D 354 VAL D 358 1 O LYS D 356 N VAL D 6
SHEET 1 O 8 ARG D 189 SER D 190 0
SHEET 2 O 8 ASN D 155 VAL D 157 1 N ILE D 156 O SER D 190
SHEET 3 O 8 VAL D 119 KCX D 122 1 N MET D 121 O ASN D 155
SHEET 4 O 8 PHE D 95 VAL D 99 1 N THR D 97 O TRP D 120
SHEET 5 O 8 VAL D 75 LEU D 77 1 N LEU D 77 O HIS D 96
SHEET 6 O 8 ALA D 54 VAL D 57 1 N PHE D 55 O LEU D 76
SHEET 7 O 8 LYS D 28 VAL D 32 1 N ALA D 31 O GLY D 56
SHEET 8 O 8 TRP D 207 VAL D 208 1 O VAL D 208 N LYS D 28
SHEET 1 P 2 PRO D 252 VAL D 253 0
SHEET 2 P 2 TRP D 259 VAL D 260 -1 O TRP D 259 N VAL D 253
LINK C4A PLP A1001 NZ LYS A 34 1555 1555 1.27
LINK C4A PLP B1001 NZ LYS B 34 1555 1555 1.29
LINK C4A PLP C1001 NZ LYS C 34 1555 1555 1.29
LINK C4A PLP D1001 NZ LYS D 34 1555 1555 1.30
LINK C MET A 121 N KCX A 122 1555 1555 1.33
LINK C KCX A 122 N LEU A 123 1555 1555 1.33
LINK C MET B 121 N KCX B 122 1555 1555 1.33
LINK C KCX B 122 N LEU B 123 1555 1555 1.32
LINK C MET C 121 N KCX C 122 1555 1555 1.33
LINK C KCX C 122 N LEU C 123 1555 1555 1.32
LINK C MET D 121 N KCX D 122 1555 1555 1.33
LINK C KCX D 122 N LEU D 123 1555 1555 1.33
CISPEP 1 GLN A 152 PRO A 153 0 -0.20
CISPEP 2 GLN B 152 PRO B 153 0 0.00
CISPEP 3 GLN C 152 PRO C 153 0 0.13
CISPEP 4 GLN D 152 PRO D 153 0 0.12
SITE 1 AC1 4 TYR A 255 TYR A 274 ARG A 280 TYR B 343
SITE 1 AC2 2 ARG A 19 ARG B 266
SITE 1 AC3 1 ARG A 162
SITE 1 AC4 4 TYR A 343 TYR B 255 TYR B 274 ARG B 280
SITE 1 AC5 2 ARG A 266 ARG B 19
SITE 1 AC6 3 TYR C 255 TYR C 274 ALA C 302
SITE 1 AC7 3 ARG C 19 ARG D 266 ALA D 314
SITE 1 AC8 2 ARG C 162 CYS C 168
SITE 1 AC9 3 ARG A 280 ARG A 300 LYS B 221
SITE 1 BC1 3 LYS A 221 ARG B 280 ARG B 300
SITE 1 BC2 9 LYS A 34 TYR A 38 HIS A 159 ALA A 193
SITE 2 BC2 9 SER A 194 ARG A 209 GLY A 211 ILE A 212
SITE 3 BC2 9 TYR A 343
SITE 1 BC3 9 LYS B 34 TYR B 38 HIS B 159 ALA B 193
SITE 2 BC3 9 SER B 194 ARG B 209 GLY B 211 ILE B 212
SITE 3 BC3 9 TYR B 343
SITE 1 BC4 10 LYS C 34 TYR C 38 LEU C 78 HIS C 159
SITE 2 BC4 10 ALA C 193 SER C 194 ARG C 209 GLY C 211
SITE 3 BC4 10 ILE C 212 TYR C 343
SITE 1 BC5 9 LYS D 34 TYR D 38 HIS D 159 ALA D 193
SITE 2 BC5 9 SER D 194 ARG D 209 GLY D 211 ILE D 212
SITE 3 BC5 9 TYR D 343
CRYST1 148.181 148.181 163.689 90.00 90.00 120.00 P 6 24
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 0.006749 0.003896 0.000000 0.00000
SCALE2 0.000000 0.007793 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006109 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
