HEADER OXIDOREDUCTASE 17-FEB-05 1WYV
TITLE CRYSTAL STRUCTURE OF GLYCINE DECARBOXYLASE (P-PROTEIN) OF THE GLYCINE
TITLE 2 CLEAVAGE SYSTEM, IN INHIBITOR-BOUND FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCINE DEHYDROGENASE (DECARBOXYLATING) SUBUNIT 1;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 SYNONYM: P-PROTEIN OF THE GLYCINE CLEAVAGE SYSTEM SUBUNIT 1;
COMPND 5 EC: 1.4.4.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: GLYCINE DEHYDROGENASE SUBUNIT 2 (P-PROTEIN);
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 SYNONYM: P-PROTEIN OF THE GLYCINE CLEAVAGE SYSTEM SUBUNIT 2;
COMPND 11 EC: 1.4.4.2;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: GCSA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BLR(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 13 ORGANISM_TAXID: 300852;
SOURCE 14 STRAIN: HB8;
SOURCE 15 GENE: GCSB;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BLR(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS ALPHA(2)BETA(2) TETRAMER, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 2 INITIATIVE, RSGI, STRUCTURAL GENOMICS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.NAKAI,N.NAKAGAWA,N.MAOKA,R.MASUI,S.KURAMITSU,N.KAMIYA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 6 03-APR-24 1WYV 1 REMARK
REVDAT 5 13-MAR-24 1WYV 1 REMARK LINK
REVDAT 4 13-JUL-11 1WYV 1 VERSN
REVDAT 3 24-FEB-09 1WYV 1 VERSN
REVDAT 2 21-JUN-05 1WYV 1 JRNL
REVDAT 1 05-APR-05 1WYV 0
JRNL AUTH T.NAKAI,N.NAKAGAWA,N.MAOKA,R.MASUI,S.KURAMITSU,N.KAMIYA
JRNL TITL STRUCTURE OF P-PROTEIN OF THE GLYCINE CLEAVAGE SYSTEM:
JRNL TITL 2 IMPLICATIONS FOR NONKETOTIC HYPERGLYCINEMIA
JRNL REF EMBO J. V. 24 1523 2005
JRNL REFN ISSN 0261-4189
JRNL PMID 15791207
JRNL DOI 10.1038/SJ.EMBOJ.7600632
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 4234196.180
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 165655
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 SET) : 0.188
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8338
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 25756
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1393
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 28132
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 1192
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.85000
REMARK 3 B22 (A**2) : -4.33000
REMARK 3 B33 (A**2) : -3.52000
REMARK 3 B12 (A**2) : 0.00000
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.23
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.150 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.070 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.940 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 36.30
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 : PLP.PARAM
REMARK 3 PARAMETER FILE 5 : AOA.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
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 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WYV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024166.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 166371
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.57800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS 1.1
REMARK 200 STARTING MODEL: P-PROTEIN IN THE HOLO-FORM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, LITHIUM SULFATE, MES, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 67.08650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.14950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.15850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 95.14950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 67.08650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.15850
REMARK 290 SMTRY3 4 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS AN ALPHA(2)BETA(2) TETRAMER. THE
REMARK 300 ASYMMETRIC UNIT CONTAINS TWO SETS OF THE ASSEMBLY (CHAINS A-D AND E-
REMARK 300 H).
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 41640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -236.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 41710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -242.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 ALA A 438
REMARK 465 MET B 1
REMARK 465 ALA C 438
REMARK 465 MET D 1
REMARK 465 ALA E 438
REMARK 465 MET F 1
REMARK 465 ALA G 438
REMARK 465 MET H 1
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 SER A 129 152.19 137.48
REMARK 500 ASP A 132 -179.03 -170.17
REMARK 500 HIS A 160 122.46 -39.49
REMARK 500 VAL A 239 -31.50 -131.18
REMARK 500 LEU A 258 55.09 -98.34
REMARK 500 HIS A 268 -138.80 -133.27
REMARK 500 THR A 274 -168.52 -162.20
REMARK 500 THR A 290 -159.61 -157.38
REMARK 500 ARG A 312 -114.70 39.69
REMARK 500 THR A 320 -81.76 -118.49
REMARK 500 ASN A 322 -137.14 -111.05
REMARK 500 PHE A 369 -54.56 -134.21
REMARK 500 PHE A 375 -116.60 -96.66
REMARK 500 ALA A 401 75.41 67.61
REMARK 500 PRO B 70 46.50 -69.84
REMARK 500 LYS B 266 -79.75 -115.12
REMARK 500 THR B 269 -0.99 65.69
REMARK 500 PHE B 320 -132.34 62.44
REMARK 500 ASP B 370 63.66 -114.34
REMARK 500 PRO B 372 104.86 -55.98
REMARK 500 MET B 374 -124.46 -97.30
REMARK 500 THR B 419 164.27 74.60
REMARK 500 PRO C 97 73.64 -64.41
REMARK 500 SER C 129 162.60 131.90
REMARK 500 HIS C 160 127.61 -37.85
REMARK 500 HIS C 268 -137.93 -139.51
REMARK 500 THR C 274 -168.15 -162.20
REMARK 500 THR C 290 -163.03 -161.61
REMARK 500 ARG C 312 -105.19 42.23
REMARK 500 THR C 320 -86.56 -111.52
REMARK 500 ASN C 322 -126.52 -107.80
REMARK 500 ALA C 323 46.18 -143.84
REMARK 500 PHE C 369 -67.17 -130.04
REMARK 500 PHE C 375 -112.53 -88.29
REMARK 500 ALA C 401 69.47 69.34
REMARK 500 TYR D 69 78.48 -119.16
REMARK 500 ARG D 156 94.60 -69.00
REMARK 500 LYS D 266 -79.65 -121.60
REMARK 500 THR D 269 -3.99 68.25
REMARK 500 PHE D 320 -139.78 58.73
REMARK 500 MET D 374 -118.42 -95.11
REMARK 500 PRO D 402 -163.45 -78.66
REMARK 500 THR D 419 165.08 69.30
REMARK 500 ASP D 472 61.60 35.28
REMARK 500 PRO E 97 81.05 -65.03
REMARK 500 SER E 129 154.83 134.72
REMARK 500 HIS E 160 125.66 -37.86
REMARK 500 LEU E 258 54.62 -90.26
REMARK 500 PHE E 264 28.95 49.27
REMARK 500 HIS E 268 -135.73 -133.33
REMARK 500
REMARK 500 THIS ENTRY HAS 94 RAMACHANDRAN OUTLIERS.
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 B 1475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AOA B 1476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP D 2475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AOA D 2476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP F 3475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AOA F 3476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP H 4475
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AOA H 4476
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WYT RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, IN APO FORM
REMARK 900 RELATED ID: 1WYU RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, IN HOLO FORM
REMARK 900 RELATED ID: TTK003000355.3 RELATED DB: TARGETDB
DBREF 1WYV A 1 438 GB 55771907 BAD70348 1 438
DBREF 1WYV C 1 438 GB 55771907 BAD70348 1 438
DBREF 1WYV E 1 438 GB 55771907 BAD70348 1 438
DBREF 1WYV G 1 438 GB 55771907 BAD70348 1 438
DBREF 1WYV B 1 474 GB 55771908 BAD70349 1 474
DBREF 1WYV D 1 474 GB 55771908 BAD70349 1 474
DBREF 1WYV F 1 474 GB 55771908 BAD70349 1 474
DBREF 1WYV H 1 474 GB 55771908 BAD70349 1 474
SEQRES 1 A 438 MET ASP TYR THR PRO HIS THR GLU GLU GLU ILE ARG GLU
SEQRES 2 A 438 MET LEU ARG ARG VAL GLY ALA ALA SER LEU GLU ASP LEU
SEQRES 3 A 438 PHE ALA HIS LEU PRO LYS GLU ILE LEU SER PRO PRO ILE
SEQRES 4 A 438 ASP LEU PRO GLU PRO LEU PRO GLU TRP LYS VAL LEU GLU
SEQRES 5 A 438 GLU LEU ARG ARG LEU ALA ALA GLN ASN LEU PRO ALA HIS
SEQRES 6 A 438 LYS ALA PHE LEU GLY GLY GLY VAL ARG SER HIS HIS VAL
SEQRES 7 A 438 PRO PRO VAL VAL GLN ALA LEU ALA ALA ARG GLY GLU PHE
SEQRES 8 A 438 LEU THR ALA TYR THR PRO TYR GLN PRO GLU VAL SER GLN
SEQRES 9 A 438 GLY VAL LEU GLN ALA THR PHE GLU TYR GLN THR MET ILE
SEQRES 10 A 438 ALA GLU LEU ALA GLY LEU GLU ILE ALA ASN ALA SER MET
SEQRES 11 A 438 TYR ASP GLY ALA THR ALA LEU ALA GLU GLY VAL LEU LEU
SEQRES 12 A 438 ALA LEU ARG GLU THR GLY ARG MET GLY VAL LEU VAL SER
SEQRES 13 A 438 GLN GLY VAL HIS PRO GLU TYR ARG ALA VAL LEU ARG ALA
SEQRES 14 A 438 TYR LEU GLU ALA VAL GLY ALA LYS LEU LEU THR LEU PRO
SEQRES 15 A 438 LEU GLU GLY GLY ARG THR PRO LEU PRO GLU VAL GLY GLU
SEQRES 16 A 438 GLU VAL GLY ALA VAL VAL VAL GLN ASN PRO ASN PHE LEU
SEQRES 17 A 438 GLY ALA LEU GLU ASP LEU GLY PRO PHE ALA GLU ALA ALA
SEQRES 18 A 438 HIS GLY ALA GLY ALA LEU PHE VAL ALA VAL ALA ASP PRO
SEQRES 19 A 438 LEU SER LEU GLY VAL LEU LYS PRO PRO GLY ALA TYR GLY
SEQRES 20 A 438 ALA ASP ILE ALA VAL GLY ASP GLY GLN SER LEU GLY LEU
SEQRES 21 A 438 PRO MET GLY PHE GLY GLY PRO HIS PHE GLY PHE LEU ALA
SEQRES 22 A 438 THR LYS LYS ALA PHE VAL ARG GLN LEU PRO GLY ARG LEU
SEQRES 23 A 438 VAL SER GLU THR VAL ASP VAL GLU GLY ARG ARG GLY PHE
SEQRES 24 A 438 ILE LEU THR LEU GLN ALA ARG GLU GLN TYR ILE ARG ARG
SEQRES 25 A 438 ALA LYS ALA LYS SER ASN ILE THR THR ASN ALA GLN LEU
SEQRES 26 A 438 THR ALA LEU MET GLY ALA MET TYR LEU ALA ALA LEU GLY
SEQRES 27 A 438 PRO GLU GLY LEU ARG GLU VAL ALA LEU LYS SER VAL GLU
SEQRES 28 A 438 MET ALA HIS LYS LEU HIS ALA LEU LEU LEU GLU VAL PRO
SEQRES 29 A 438 GLY VAL ARG PRO PHE THR PRO LYS PRO PHE PHE ASN GLU
SEQRES 30 A 438 PHE ALA LEU ALA LEU PRO LYS ASP PRO GLU ALA VAL ARG
SEQRES 31 A 438 ARG ALA LEU ALA GLU ARG GLY PHE HIS GLY ALA THR PRO
SEQRES 32 A 438 VAL PRO ARG GLU TYR GLY GLU ASN LEU ALA LEU PHE ALA
SEQRES 33 A 438 ALA THR GLU LEU HIS GLU GLU GLU ASP LEU LEU ALA LEU
SEQRES 34 A 438 ARG GLU ALA LEU LYS GLU VAL LEU ALA
SEQRES 1 B 474 MET SER PHE PRO LEU ILE PHE GLU ARG SER ARG LYS GLY
SEQRES 2 B 474 ARG ARG GLY LEU LYS LEU VAL LYS ALA VAL PRO LYS ALA
SEQRES 3 B 474 GLU ASP LEU ILE PRO LYS GLU HIS LEU ARG GLU VAL PRO
SEQRES 4 B 474 PRO ARG LEU PRO GLU VAL ASP GLU LEU THR LEU VAL ARG
SEQRES 5 B 474 HIS TYR THR GLY LEU SER ARG ARG GLN VAL GLY VAL ASP
SEQRES 6 B 474 THR THR PHE TYR PRO LEU GLY SER CYS THR MET LYS TYR
SEQRES 7 B 474 ASN PRO LYS LEU HIS GLU GLU ALA ALA ARG LEU PHE ALA
SEQRES 8 B 474 ASP LEU HIS PRO TYR GLN ASP PRO ARG THR ALA GLN GLY
SEQRES 9 B 474 ALA LEU ARG LEU MET TRP GLU LEU GLY GLU TYR LEU LYS
SEQRES 10 B 474 ALA LEU THR GLY MET ASP ALA ILE THR LEU GLU PRO ALA
SEQRES 11 B 474 ALA GLY ALA HIS GLY GLU LEU THR GLY ILE LEU ILE ILE
SEQRES 12 B 474 ARG ALA TYR HIS GLU ASP ARG GLY GLU GLY ARG THR ARG
SEQRES 13 B 474 ARG VAL VAL LEU VAL PRO ASP SER ALA HIS GLY SER ASN
SEQRES 14 B 474 PRO ALA THR ALA SER MET ALA GLY TYR GLN VAL ARG GLU
SEQRES 15 B 474 ILE PRO SER GLY PRO GLU GLY GLU VAL ASP LEU GLU ALA
SEQRES 16 B 474 LEU LYS ARG GLU LEU GLY PRO HIS VAL ALA ALA LEU MET
SEQRES 17 B 474 LEU THR ASN PRO ASN THR LEU GLY LEU PHE GLU ARG ARG
SEQRES 18 B 474 ILE LEU GLU ILE SER ARG LEU CYS LYS GLU ALA GLY VAL
SEQRES 19 B 474 GLN LEU TYR TYR ASP GLY ALA ASN LEU ASN ALA ILE MET
SEQRES 20 B 474 GLY TRP ALA ARG PRO GLY ASP MET GLY PHE ASP VAL VAL
SEQRES 21 B 474 HIS LEU ASN LEU HIS LYS THR PHE THR VAL PRO HIS GLY
SEQRES 22 B 474 GLY GLY GLY PRO GLY SER GLY PRO VAL GLY VAL LYS ALA
SEQRES 23 B 474 HIS LEU ALA PRO TYR LEU PRO VAL PRO LEU VAL GLU ARG
SEQRES 24 B 474 GLY GLU GLU GLY PHE TYR LEU ASP PHE ASP ARG PRO LYS
SEQRES 25 B 474 SER ILE GLY ARG VAL ARG SER PHE TYR GLY ASN PHE LEU
SEQRES 26 B 474 ALA LEU VAL ARG ALA TRP ALA TYR ILE ARG THR LEU GLY
SEQRES 27 B 474 LEU GLU GLY LEU LYS LYS ALA ALA ALA LEU ALA VAL LEU
SEQRES 28 B 474 ASN ALA ARG TYR LEU LYS GLU LEU LEU LYS GLU LYS GLY
SEQRES 29 B 474 TYR ARG VAL PRO TYR ASP GLY PRO SER MET HIS GLU PHE
SEQRES 30 B 474 VAL ALA GLN PRO PRO GLU GLY PHE ARG ALA LEU ASP LEU
SEQRES 31 B 474 ALA LYS GLY LEU LEU GLU LEU GLY PHE HIS PRO PRO THR
SEQRES 32 B 474 VAL TYR PHE PRO LEU ILE VAL LYS GLU ALA LEU MET VAL
SEQRES 33 B 474 GLU PRO THR GLU THR GLU ALA LYS GLU THR LEU GLU ALA
SEQRES 34 B 474 PHE ALA GLU ALA MET GLY ALA LEU LEU LYS LYS PRO LYS
SEQRES 35 B 474 GLU TRP LEU GLU ASN ALA PRO TYR SER THR PRO VAL ARG
SEQRES 36 B 474 ARG LEU ASP GLU LEU ARG ALA ASN LYS HIS PRO LYS LEU
SEQRES 37 B 474 THR TYR PHE ASP GLU GLY
SEQRES 1 C 438 MET ASP TYR THR PRO HIS THR GLU GLU GLU ILE ARG GLU
SEQRES 2 C 438 MET LEU ARG ARG VAL GLY ALA ALA SER LEU GLU ASP LEU
SEQRES 3 C 438 PHE ALA HIS LEU PRO LYS GLU ILE LEU SER PRO PRO ILE
SEQRES 4 C 438 ASP LEU PRO GLU PRO LEU PRO GLU TRP LYS VAL LEU GLU
SEQRES 5 C 438 GLU LEU ARG ARG LEU ALA ALA GLN ASN LEU PRO ALA HIS
SEQRES 6 C 438 LYS ALA PHE LEU GLY GLY GLY VAL ARG SER HIS HIS VAL
SEQRES 7 C 438 PRO PRO VAL VAL GLN ALA LEU ALA ALA ARG GLY GLU PHE
SEQRES 8 C 438 LEU THR ALA TYR THR PRO TYR GLN PRO GLU VAL SER GLN
SEQRES 9 C 438 GLY VAL LEU GLN ALA THR PHE GLU TYR GLN THR MET ILE
SEQRES 10 C 438 ALA GLU LEU ALA GLY LEU GLU ILE ALA ASN ALA SER MET
SEQRES 11 C 438 TYR ASP GLY ALA THR ALA LEU ALA GLU GLY VAL LEU LEU
SEQRES 12 C 438 ALA LEU ARG GLU THR GLY ARG MET GLY VAL LEU VAL SER
SEQRES 13 C 438 GLN GLY VAL HIS PRO GLU TYR ARG ALA VAL LEU ARG ALA
SEQRES 14 C 438 TYR LEU GLU ALA VAL GLY ALA LYS LEU LEU THR LEU PRO
SEQRES 15 C 438 LEU GLU GLY GLY ARG THR PRO LEU PRO GLU VAL GLY GLU
SEQRES 16 C 438 GLU VAL GLY ALA VAL VAL VAL GLN ASN PRO ASN PHE LEU
SEQRES 17 C 438 GLY ALA LEU GLU ASP LEU GLY PRO PHE ALA GLU ALA ALA
SEQRES 18 C 438 HIS GLY ALA GLY ALA LEU PHE VAL ALA VAL ALA ASP PRO
SEQRES 19 C 438 LEU SER LEU GLY VAL LEU LYS PRO PRO GLY ALA TYR GLY
SEQRES 20 C 438 ALA ASP ILE ALA VAL GLY ASP GLY GLN SER LEU GLY LEU
SEQRES 21 C 438 PRO MET GLY PHE GLY GLY PRO HIS PHE GLY PHE LEU ALA
SEQRES 22 C 438 THR LYS LYS ALA PHE VAL ARG GLN LEU PRO GLY ARG LEU
SEQRES 23 C 438 VAL SER GLU THR VAL ASP VAL GLU GLY ARG ARG GLY PHE
SEQRES 24 C 438 ILE LEU THR LEU GLN ALA ARG GLU GLN TYR ILE ARG ARG
SEQRES 25 C 438 ALA LYS ALA LYS SER ASN ILE THR THR ASN ALA GLN LEU
SEQRES 26 C 438 THR ALA LEU MET GLY ALA MET TYR LEU ALA ALA LEU GLY
SEQRES 27 C 438 PRO GLU GLY LEU ARG GLU VAL ALA LEU LYS SER VAL GLU
SEQRES 28 C 438 MET ALA HIS LYS LEU HIS ALA LEU LEU LEU GLU VAL PRO
SEQRES 29 C 438 GLY VAL ARG PRO PHE THR PRO LYS PRO PHE PHE ASN GLU
SEQRES 30 C 438 PHE ALA LEU ALA LEU PRO LYS ASP PRO GLU ALA VAL ARG
SEQRES 31 C 438 ARG ALA LEU ALA GLU ARG GLY PHE HIS GLY ALA THR PRO
SEQRES 32 C 438 VAL PRO ARG GLU TYR GLY GLU ASN LEU ALA LEU PHE ALA
SEQRES 33 C 438 ALA THR GLU LEU HIS GLU GLU GLU ASP LEU LEU ALA LEU
SEQRES 34 C 438 ARG GLU ALA LEU LYS GLU VAL LEU ALA
SEQRES 1 D 474 MET SER PHE PRO LEU ILE PHE GLU ARG SER ARG LYS GLY
SEQRES 2 D 474 ARG ARG GLY LEU LYS LEU VAL LYS ALA VAL PRO LYS ALA
SEQRES 3 D 474 GLU ASP LEU ILE PRO LYS GLU HIS LEU ARG GLU VAL PRO
SEQRES 4 D 474 PRO ARG LEU PRO GLU VAL ASP GLU LEU THR LEU VAL ARG
SEQRES 5 D 474 HIS TYR THR GLY LEU SER ARG ARG GLN VAL GLY VAL ASP
SEQRES 6 D 474 THR THR PHE TYR PRO LEU GLY SER CYS THR MET LYS TYR
SEQRES 7 D 474 ASN PRO LYS LEU HIS GLU GLU ALA ALA ARG LEU PHE ALA
SEQRES 8 D 474 ASP LEU HIS PRO TYR GLN ASP PRO ARG THR ALA GLN GLY
SEQRES 9 D 474 ALA LEU ARG LEU MET TRP GLU LEU GLY GLU TYR LEU LYS
SEQRES 10 D 474 ALA LEU THR GLY MET ASP ALA ILE THR LEU GLU PRO ALA
SEQRES 11 D 474 ALA GLY ALA HIS GLY GLU LEU THR GLY ILE LEU ILE ILE
SEQRES 12 D 474 ARG ALA TYR HIS GLU ASP ARG GLY GLU GLY ARG THR ARG
SEQRES 13 D 474 ARG VAL VAL LEU VAL PRO ASP SER ALA HIS GLY SER ASN
SEQRES 14 D 474 PRO ALA THR ALA SER MET ALA GLY TYR GLN VAL ARG GLU
SEQRES 15 D 474 ILE PRO SER GLY PRO GLU GLY GLU VAL ASP LEU GLU ALA
SEQRES 16 D 474 LEU LYS ARG GLU LEU GLY PRO HIS VAL ALA ALA LEU MET
SEQRES 17 D 474 LEU THR ASN PRO ASN THR LEU GLY LEU PHE GLU ARG ARG
SEQRES 18 D 474 ILE LEU GLU ILE SER ARG LEU CYS LYS GLU ALA GLY VAL
SEQRES 19 D 474 GLN LEU TYR TYR ASP GLY ALA ASN LEU ASN ALA ILE MET
SEQRES 20 D 474 GLY TRP ALA ARG PRO GLY ASP MET GLY PHE ASP VAL VAL
SEQRES 21 D 474 HIS LEU ASN LEU HIS LYS THR PHE THR VAL PRO HIS GLY
SEQRES 22 D 474 GLY GLY GLY PRO GLY SER GLY PRO VAL GLY VAL LYS ALA
SEQRES 23 D 474 HIS LEU ALA PRO TYR LEU PRO VAL PRO LEU VAL GLU ARG
SEQRES 24 D 474 GLY GLU GLU GLY PHE TYR LEU ASP PHE ASP ARG PRO LYS
SEQRES 25 D 474 SER ILE GLY ARG VAL ARG SER PHE TYR GLY ASN PHE LEU
SEQRES 26 D 474 ALA LEU VAL ARG ALA TRP ALA TYR ILE ARG THR LEU GLY
SEQRES 27 D 474 LEU GLU GLY LEU LYS LYS ALA ALA ALA LEU ALA VAL LEU
SEQRES 28 D 474 ASN ALA ARG TYR LEU LYS GLU LEU LEU LYS GLU LYS GLY
SEQRES 29 D 474 TYR ARG VAL PRO TYR ASP GLY PRO SER MET HIS GLU PHE
SEQRES 30 D 474 VAL ALA GLN PRO PRO GLU GLY PHE ARG ALA LEU ASP LEU
SEQRES 31 D 474 ALA LYS GLY LEU LEU GLU LEU GLY PHE HIS PRO PRO THR
SEQRES 32 D 474 VAL TYR PHE PRO LEU ILE VAL LYS GLU ALA LEU MET VAL
SEQRES 33 D 474 GLU PRO THR GLU THR GLU ALA LYS GLU THR LEU GLU ALA
SEQRES 34 D 474 PHE ALA GLU ALA MET GLY ALA LEU LEU LYS LYS PRO LYS
SEQRES 35 D 474 GLU TRP LEU GLU ASN ALA PRO TYR SER THR PRO VAL ARG
SEQRES 36 D 474 ARG LEU ASP GLU LEU ARG ALA ASN LYS HIS PRO LYS LEU
SEQRES 37 D 474 THR TYR PHE ASP GLU GLY
SEQRES 1 E 438 MET ASP TYR THR PRO HIS THR GLU GLU GLU ILE ARG GLU
SEQRES 2 E 438 MET LEU ARG ARG VAL GLY ALA ALA SER LEU GLU ASP LEU
SEQRES 3 E 438 PHE ALA HIS LEU PRO LYS GLU ILE LEU SER PRO PRO ILE
SEQRES 4 E 438 ASP LEU PRO GLU PRO LEU PRO GLU TRP LYS VAL LEU GLU
SEQRES 5 E 438 GLU LEU ARG ARG LEU ALA ALA GLN ASN LEU PRO ALA HIS
SEQRES 6 E 438 LYS ALA PHE LEU GLY GLY GLY VAL ARG SER HIS HIS VAL
SEQRES 7 E 438 PRO PRO VAL VAL GLN ALA LEU ALA ALA ARG GLY GLU PHE
SEQRES 8 E 438 LEU THR ALA TYR THR PRO TYR GLN PRO GLU VAL SER GLN
SEQRES 9 E 438 GLY VAL LEU GLN ALA THR PHE GLU TYR GLN THR MET ILE
SEQRES 10 E 438 ALA GLU LEU ALA GLY LEU GLU ILE ALA ASN ALA SER MET
SEQRES 11 E 438 TYR ASP GLY ALA THR ALA LEU ALA GLU GLY VAL LEU LEU
SEQRES 12 E 438 ALA LEU ARG GLU THR GLY ARG MET GLY VAL LEU VAL SER
SEQRES 13 E 438 GLN GLY VAL HIS PRO GLU TYR ARG ALA VAL LEU ARG ALA
SEQRES 14 E 438 TYR LEU GLU ALA VAL GLY ALA LYS LEU LEU THR LEU PRO
SEQRES 15 E 438 LEU GLU GLY GLY ARG THR PRO LEU PRO GLU VAL GLY GLU
SEQRES 16 E 438 GLU VAL GLY ALA VAL VAL VAL GLN ASN PRO ASN PHE LEU
SEQRES 17 E 438 GLY ALA LEU GLU ASP LEU GLY PRO PHE ALA GLU ALA ALA
SEQRES 18 E 438 HIS GLY ALA GLY ALA LEU PHE VAL ALA VAL ALA ASP PRO
SEQRES 19 E 438 LEU SER LEU GLY VAL LEU LYS PRO PRO GLY ALA TYR GLY
SEQRES 20 E 438 ALA ASP ILE ALA VAL GLY ASP GLY GLN SER LEU GLY LEU
SEQRES 21 E 438 PRO MET GLY PHE GLY GLY PRO HIS PHE GLY PHE LEU ALA
SEQRES 22 E 438 THR LYS LYS ALA PHE VAL ARG GLN LEU PRO GLY ARG LEU
SEQRES 23 E 438 VAL SER GLU THR VAL ASP VAL GLU GLY ARG ARG GLY PHE
SEQRES 24 E 438 ILE LEU THR LEU GLN ALA ARG GLU GLN TYR ILE ARG ARG
SEQRES 25 E 438 ALA LYS ALA LYS SER ASN ILE THR THR ASN ALA GLN LEU
SEQRES 26 E 438 THR ALA LEU MET GLY ALA MET TYR LEU ALA ALA LEU GLY
SEQRES 27 E 438 PRO GLU GLY LEU ARG GLU VAL ALA LEU LYS SER VAL GLU
SEQRES 28 E 438 MET ALA HIS LYS LEU HIS ALA LEU LEU LEU GLU VAL PRO
SEQRES 29 E 438 GLY VAL ARG PRO PHE THR PRO LYS PRO PHE PHE ASN GLU
SEQRES 30 E 438 PHE ALA LEU ALA LEU PRO LYS ASP PRO GLU ALA VAL ARG
SEQRES 31 E 438 ARG ALA LEU ALA GLU ARG GLY PHE HIS GLY ALA THR PRO
SEQRES 32 E 438 VAL PRO ARG GLU TYR GLY GLU ASN LEU ALA LEU PHE ALA
SEQRES 33 E 438 ALA THR GLU LEU HIS GLU GLU GLU ASP LEU LEU ALA LEU
SEQRES 34 E 438 ARG GLU ALA LEU LYS GLU VAL LEU ALA
SEQRES 1 F 474 MET SER PHE PRO LEU ILE PHE GLU ARG SER ARG LYS GLY
SEQRES 2 F 474 ARG ARG GLY LEU LYS LEU VAL LYS ALA VAL PRO LYS ALA
SEQRES 3 F 474 GLU ASP LEU ILE PRO LYS GLU HIS LEU ARG GLU VAL PRO
SEQRES 4 F 474 PRO ARG LEU PRO GLU VAL ASP GLU LEU THR LEU VAL ARG
SEQRES 5 F 474 HIS TYR THR GLY LEU SER ARG ARG GLN VAL GLY VAL ASP
SEQRES 6 F 474 THR THR PHE TYR PRO LEU GLY SER CYS THR MET LYS TYR
SEQRES 7 F 474 ASN PRO LYS LEU HIS GLU GLU ALA ALA ARG LEU PHE ALA
SEQRES 8 F 474 ASP LEU HIS PRO TYR GLN ASP PRO ARG THR ALA GLN GLY
SEQRES 9 F 474 ALA LEU ARG LEU MET TRP GLU LEU GLY GLU TYR LEU LYS
SEQRES 10 F 474 ALA LEU THR GLY MET ASP ALA ILE THR LEU GLU PRO ALA
SEQRES 11 F 474 ALA GLY ALA HIS GLY GLU LEU THR GLY ILE LEU ILE ILE
SEQRES 12 F 474 ARG ALA TYR HIS GLU ASP ARG GLY GLU GLY ARG THR ARG
SEQRES 13 F 474 ARG VAL VAL LEU VAL PRO ASP SER ALA HIS GLY SER ASN
SEQRES 14 F 474 PRO ALA THR ALA SER MET ALA GLY TYR GLN VAL ARG GLU
SEQRES 15 F 474 ILE PRO SER GLY PRO GLU GLY GLU VAL ASP LEU GLU ALA
SEQRES 16 F 474 LEU LYS ARG GLU LEU GLY PRO HIS VAL ALA ALA LEU MET
SEQRES 17 F 474 LEU THR ASN PRO ASN THR LEU GLY LEU PHE GLU ARG ARG
SEQRES 18 F 474 ILE LEU GLU ILE SER ARG LEU CYS LYS GLU ALA GLY VAL
SEQRES 19 F 474 GLN LEU TYR TYR ASP GLY ALA ASN LEU ASN ALA ILE MET
SEQRES 20 F 474 GLY TRP ALA ARG PRO GLY ASP MET GLY PHE ASP VAL VAL
SEQRES 21 F 474 HIS LEU ASN LEU HIS LYS THR PHE THR VAL PRO HIS GLY
SEQRES 22 F 474 GLY GLY GLY PRO GLY SER GLY PRO VAL GLY VAL LYS ALA
SEQRES 23 F 474 HIS LEU ALA PRO TYR LEU PRO VAL PRO LEU VAL GLU ARG
SEQRES 24 F 474 GLY GLU GLU GLY PHE TYR LEU ASP PHE ASP ARG PRO LYS
SEQRES 25 F 474 SER ILE GLY ARG VAL ARG SER PHE TYR GLY ASN PHE LEU
SEQRES 26 F 474 ALA LEU VAL ARG ALA TRP ALA TYR ILE ARG THR LEU GLY
SEQRES 27 F 474 LEU GLU GLY LEU LYS LYS ALA ALA ALA LEU ALA VAL LEU
SEQRES 28 F 474 ASN ALA ARG TYR LEU LYS GLU LEU LEU LYS GLU LYS GLY
SEQRES 29 F 474 TYR ARG VAL PRO TYR ASP GLY PRO SER MET HIS GLU PHE
SEQRES 30 F 474 VAL ALA GLN PRO PRO GLU GLY PHE ARG ALA LEU ASP LEU
SEQRES 31 F 474 ALA LYS GLY LEU LEU GLU LEU GLY PHE HIS PRO PRO THR
SEQRES 32 F 474 VAL TYR PHE PRO LEU ILE VAL LYS GLU ALA LEU MET VAL
SEQRES 33 F 474 GLU PRO THR GLU THR GLU ALA LYS GLU THR LEU GLU ALA
SEQRES 34 F 474 PHE ALA GLU ALA MET GLY ALA LEU LEU LYS LYS PRO LYS
SEQRES 35 F 474 GLU TRP LEU GLU ASN ALA PRO TYR SER THR PRO VAL ARG
SEQRES 36 F 474 ARG LEU ASP GLU LEU ARG ALA ASN LYS HIS PRO LYS LEU
SEQRES 37 F 474 THR TYR PHE ASP GLU GLY
SEQRES 1 G 438 MET ASP TYR THR PRO HIS THR GLU GLU GLU ILE ARG GLU
SEQRES 2 G 438 MET LEU ARG ARG VAL GLY ALA ALA SER LEU GLU ASP LEU
SEQRES 3 G 438 PHE ALA HIS LEU PRO LYS GLU ILE LEU SER PRO PRO ILE
SEQRES 4 G 438 ASP LEU PRO GLU PRO LEU PRO GLU TRP LYS VAL LEU GLU
SEQRES 5 G 438 GLU LEU ARG ARG LEU ALA ALA GLN ASN LEU PRO ALA HIS
SEQRES 6 G 438 LYS ALA PHE LEU GLY GLY GLY VAL ARG SER HIS HIS VAL
SEQRES 7 G 438 PRO PRO VAL VAL GLN ALA LEU ALA ALA ARG GLY GLU PHE
SEQRES 8 G 438 LEU THR ALA TYR THR PRO TYR GLN PRO GLU VAL SER GLN
SEQRES 9 G 438 GLY VAL LEU GLN ALA THR PHE GLU TYR GLN THR MET ILE
SEQRES 10 G 438 ALA GLU LEU ALA GLY LEU GLU ILE ALA ASN ALA SER MET
SEQRES 11 G 438 TYR ASP GLY ALA THR ALA LEU ALA GLU GLY VAL LEU LEU
SEQRES 12 G 438 ALA LEU ARG GLU THR GLY ARG MET GLY VAL LEU VAL SER
SEQRES 13 G 438 GLN GLY VAL HIS PRO GLU TYR ARG ALA VAL LEU ARG ALA
SEQRES 14 G 438 TYR LEU GLU ALA VAL GLY ALA LYS LEU LEU THR LEU PRO
SEQRES 15 G 438 LEU GLU GLY GLY ARG THR PRO LEU PRO GLU VAL GLY GLU
SEQRES 16 G 438 GLU VAL GLY ALA VAL VAL VAL GLN ASN PRO ASN PHE LEU
SEQRES 17 G 438 GLY ALA LEU GLU ASP LEU GLY PRO PHE ALA GLU ALA ALA
SEQRES 18 G 438 HIS GLY ALA GLY ALA LEU PHE VAL ALA VAL ALA ASP PRO
SEQRES 19 G 438 LEU SER LEU GLY VAL LEU LYS PRO PRO GLY ALA TYR GLY
SEQRES 20 G 438 ALA ASP ILE ALA VAL GLY ASP GLY GLN SER LEU GLY LEU
SEQRES 21 G 438 PRO MET GLY PHE GLY GLY PRO HIS PHE GLY PHE LEU ALA
SEQRES 22 G 438 THR LYS LYS ALA PHE VAL ARG GLN LEU PRO GLY ARG LEU
SEQRES 23 G 438 VAL SER GLU THR VAL ASP VAL GLU GLY ARG ARG GLY PHE
SEQRES 24 G 438 ILE LEU THR LEU GLN ALA ARG GLU GLN TYR ILE ARG ARG
SEQRES 25 G 438 ALA LYS ALA LYS SER ASN ILE THR THR ASN ALA GLN LEU
SEQRES 26 G 438 THR ALA LEU MET GLY ALA MET TYR LEU ALA ALA LEU GLY
SEQRES 27 G 438 PRO GLU GLY LEU ARG GLU VAL ALA LEU LYS SER VAL GLU
SEQRES 28 G 438 MET ALA HIS LYS LEU HIS ALA LEU LEU LEU GLU VAL PRO
SEQRES 29 G 438 GLY VAL ARG PRO PHE THR PRO LYS PRO PHE PHE ASN GLU
SEQRES 30 G 438 PHE ALA LEU ALA LEU PRO LYS ASP PRO GLU ALA VAL ARG
SEQRES 31 G 438 ARG ALA LEU ALA GLU ARG GLY PHE HIS GLY ALA THR PRO
SEQRES 32 G 438 VAL PRO ARG GLU TYR GLY GLU ASN LEU ALA LEU PHE ALA
SEQRES 33 G 438 ALA THR GLU LEU HIS GLU GLU GLU ASP LEU LEU ALA LEU
SEQRES 34 G 438 ARG GLU ALA LEU LYS GLU VAL LEU ALA
SEQRES 1 H 474 MET SER PHE PRO LEU ILE PHE GLU ARG SER ARG LYS GLY
SEQRES 2 H 474 ARG ARG GLY LEU LYS LEU VAL LYS ALA VAL PRO LYS ALA
SEQRES 3 H 474 GLU ASP LEU ILE PRO LYS GLU HIS LEU ARG GLU VAL PRO
SEQRES 4 H 474 PRO ARG LEU PRO GLU VAL ASP GLU LEU THR LEU VAL ARG
SEQRES 5 H 474 HIS TYR THR GLY LEU SER ARG ARG GLN VAL GLY VAL ASP
SEQRES 6 H 474 THR THR PHE TYR PRO LEU GLY SER CYS THR MET LYS TYR
SEQRES 7 H 474 ASN PRO LYS LEU HIS GLU GLU ALA ALA ARG LEU PHE ALA
SEQRES 8 H 474 ASP LEU HIS PRO TYR GLN ASP PRO ARG THR ALA GLN GLY
SEQRES 9 H 474 ALA LEU ARG LEU MET TRP GLU LEU GLY GLU TYR LEU LYS
SEQRES 10 H 474 ALA LEU THR GLY MET ASP ALA ILE THR LEU GLU PRO ALA
SEQRES 11 H 474 ALA GLY ALA HIS GLY GLU LEU THR GLY ILE LEU ILE ILE
SEQRES 12 H 474 ARG ALA TYR HIS GLU ASP ARG GLY GLU GLY ARG THR ARG
SEQRES 13 H 474 ARG VAL VAL LEU VAL PRO ASP SER ALA HIS GLY SER ASN
SEQRES 14 H 474 PRO ALA THR ALA SER MET ALA GLY TYR GLN VAL ARG GLU
SEQRES 15 H 474 ILE PRO SER GLY PRO GLU GLY GLU VAL ASP LEU GLU ALA
SEQRES 16 H 474 LEU LYS ARG GLU LEU GLY PRO HIS VAL ALA ALA LEU MET
SEQRES 17 H 474 LEU THR ASN PRO ASN THR LEU GLY LEU PHE GLU ARG ARG
SEQRES 18 H 474 ILE LEU GLU ILE SER ARG LEU CYS LYS GLU ALA GLY VAL
SEQRES 19 H 474 GLN LEU TYR TYR ASP GLY ALA ASN LEU ASN ALA ILE MET
SEQRES 20 H 474 GLY TRP ALA ARG PRO GLY ASP MET GLY PHE ASP VAL VAL
SEQRES 21 H 474 HIS LEU ASN LEU HIS LYS THR PHE THR VAL PRO HIS GLY
SEQRES 22 H 474 GLY GLY GLY PRO GLY SER GLY PRO VAL GLY VAL LYS ALA
SEQRES 23 H 474 HIS LEU ALA PRO TYR LEU PRO VAL PRO LEU VAL GLU ARG
SEQRES 24 H 474 GLY GLU GLU GLY PHE TYR LEU ASP PHE ASP ARG PRO LYS
SEQRES 25 H 474 SER ILE GLY ARG VAL ARG SER PHE TYR GLY ASN PHE LEU
SEQRES 26 H 474 ALA LEU VAL ARG ALA TRP ALA TYR ILE ARG THR LEU GLY
SEQRES 27 H 474 LEU GLU GLY LEU LYS LYS ALA ALA ALA LEU ALA VAL LEU
SEQRES 28 H 474 ASN ALA ARG TYR LEU LYS GLU LEU LEU LYS GLU LYS GLY
SEQRES 29 H 474 TYR ARG VAL PRO TYR ASP GLY PRO SER MET HIS GLU PHE
SEQRES 30 H 474 VAL ALA GLN PRO PRO GLU GLY PHE ARG ALA LEU ASP LEU
SEQRES 31 H 474 ALA LYS GLY LEU LEU GLU LEU GLY PHE HIS PRO PRO THR
SEQRES 32 H 474 VAL TYR PHE PRO LEU ILE VAL LYS GLU ALA LEU MET VAL
SEQRES 33 H 474 GLU PRO THR GLU THR GLU ALA LYS GLU THR LEU GLU ALA
SEQRES 34 H 474 PHE ALA GLU ALA MET GLY ALA LEU LEU LYS LYS PRO LYS
SEQRES 35 H 474 GLU TRP LEU GLU ASN ALA PRO TYR SER THR PRO VAL ARG
SEQRES 36 H 474 ARG LEU ASP GLU LEU ARG ALA ASN LYS HIS PRO LYS LEU
SEQRES 37 H 474 THR TYR PHE ASP GLU GLY
HET PLP B1475 15
HET AOA B1476 6
HET PLP D2475 15
HET AOA D2476 6
HET PLP F3475 15
HET AOA F3476 6
HET PLP H4475 15
HET AOA H4476 6
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM AOA (AMINOOXY)ACETIC ACID
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 9 PLP 4(C8 H10 N O6 P)
FORMUL 10 AOA 4(C2 H5 N O3)
FORMUL 17 HOH *1192(H2 O)
HELIX 1 1 THR A 7 VAL A 18 1 12
HELIX 2 2 LEU A 23 ALA A 28 5 6
HELIX 3 3 PRO A 31 LEU A 35 5 5
HELIX 4 4 PRO A 46 ALA A 59 1 14
HELIX 5 5 PRO A 79 ALA A 86 1 8
HELIX 6 6 ARG A 88 ALA A 94 1 7
HELIX 7 7 GLN A 99 VAL A 102 5 4
HELIX 8 8 SER A 103 GLY A 122 1 20
HELIX 9 9 ASP A 132 GLY A 149 1 18
HELIX 10 10 HIS A 160 VAL A 174 1 15
HELIX 11 11 LEU A 214 GLY A 223 1 10
HELIX 12 12 LEU A 235 VAL A 239 5 5
HELIX 13 13 MET A 262 GLY A 266 5 5
HELIX 14 14 LYS A 276 LEU A 282 5 7
HELIX 15 15 LEU A 303 ARG A 306 5 4
HELIX 16 16 GLU A 307 ARG A 312 1 6
HELIX 17 17 ALA A 313 ALA A 315 5 3
HELIX 18 18 ALA A 323 LEU A 361 1 39
HELIX 19 19 ASP A 385 ARG A 396 1 12
HELIX 20 20 PRO A 405 GLY A 409 5 5
HELIX 21 21 GLU A 422 LEU A 437 1 16
HELIX 22 22 LEU B 5 SER B 10 1 6
HELIX 23 23 LYS B 25 LEU B 29 5 5
HELIX 24 24 PRO B 31 LEU B 35 5 5
HELIX 25 25 ASP B 46 ARG B 59 1 14
HELIX 26 26 PRO B 80 LEU B 89 1 10
HELIX 27 27 ASP B 98 THR B 101 5 4
HELIX 28 28 ALA B 102 GLY B 121 1 20
HELIX 29 29 ALA B 131 ARG B 150 1 20
HELIX 30 30 GLY B 167 ALA B 176 1 10
HELIX 31 31 ASP B 192 ARG B 198 1 7
HELIX 32 32 ARG B 221 ALA B 232 1 12
HELIX 33 33 ALA B 241 ILE B 246 5 6
HELIX 34 34 ARG B 251 MET B 255 5 5
HELIX 35 35 ALA B 286 LEU B 292 5 7
HELIX 36 36 ASN B 323 LYS B 363 1 41
HELIX 37 37 ARG B 386 LEU B 397 1 12
HELIX 38 38 ALA B 423 LYS B 440 1 18
HELIX 39 39 PRO B 441 ASN B 447 1 7
HELIX 40 40 ASP B 458 HIS B 465 1 8
HELIX 41 41 THR C 7 VAL C 18 1 12
HELIX 42 42 LEU C 23 ALA C 28 5 6
HELIX 43 43 PRO C 31 LEU C 35 5 5
HELIX 44 44 PRO C 46 ALA C 59 1 14
HELIX 45 45 PRO C 79 ALA C 87 1 9
HELIX 46 46 ARG C 88 ALA C 94 1 7
HELIX 47 47 GLN C 99 VAL C 102 5 4
HELIX 48 48 SER C 103 GLY C 122 1 20
HELIX 49 49 ASP C 132 GLY C 149 1 18
HELIX 50 50 HIS C 160 VAL C 174 1 15
HELIX 51 51 LEU C 214 ALA C 224 1 11
HELIX 52 52 PRO C 234 VAL C 239 5 6
HELIX 53 53 PRO C 242 GLY C 247 5 6
HELIX 54 54 MET C 262 GLY C 266 5 5
HELIX 55 55 LYS C 276 VAL C 279 5 4
HELIX 56 56 LEU C 303 ARG C 306 5 4
HELIX 57 57 GLU C 307 ARG C 312 1 6
HELIX 58 58 ALA C 313 ALA C 315 5 3
HELIX 59 59 ALA C 323 LEU C 361 1 39
HELIX 60 60 ASP C 385 ARG C 396 1 12
HELIX 61 61 PRO C 405 GLY C 409 5 5
HELIX 62 62 GLU C 422 LEU C 437 1 16
HELIX 63 63 LEU D 5 SER D 10 1 6
HELIX 64 64 LYS D 25 ILE D 30 1 6
HELIX 65 65 PRO D 31 LEU D 35 5 5
HELIX 66 66 ASP D 46 ARG D 59 1 14
HELIX 67 67 PRO D 80 LEU D 89 1 10
HELIX 68 68 ASP D 98 THR D 101 5 4
HELIX 69 69 ALA D 102 GLY D 121 1 20
HELIX 70 70 ALA D 131 ASP D 149 1 19
HELIX 71 71 GLY D 167 ALA D 176 1 10
HELIX 72 72 ASP D 192 LEU D 200 1 9
HELIX 73 73 ARG D 221 GLY D 233 1 13
HELIX 74 74 ALA D 241 ILE D 246 5 6
HELIX 75 75 ARG D 251 GLY D 256 5 6
HELIX 76 76 HIS D 272 GLY D 276 5 5
HELIX 77 77 LEU D 288 LEU D 292 5 5
HELIX 78 78 ASN D 323 LYS D 363 1 41
HELIX 79 79 ARG D 386 LEU D 397 1 12
HELIX 80 80 ALA D 423 LYS D 439 1 17
HELIX 81 81 PRO D 441 ASN D 447 1 7
HELIX 82 82 ASP D 458 HIS D 465 1 8
HELIX 83 83 THR E 7 GLY E 19 1 13
HELIX 84 84 LEU E 23 ALA E 28 5 6
HELIX 85 85 PRO E 46 ALA E 59 1 14
HELIX 86 86 PRO E 79 ALA E 86 1 8
HELIX 87 87 ARG E 88 ALA E 94 1 7
HELIX 88 88 GLN E 99 VAL E 102 5 4
HELIX 89 89 SER E 103 GLY E 122 1 20
HELIX 90 90 ASP E 132 GLY E 149 1 18
HELIX 91 91 HIS E 160 VAL E 174 1 15
HELIX 92 92 LEU E 214 ALA E 224 1 11
HELIX 93 93 LEU E 235 VAL E 239 5 5
HELIX 94 94 PRO E 242 GLY E 247 5 6
HELIX 95 95 MET E 262 GLY E 266 5 5
HELIX 96 96 LYS E 276 LEU E 282 5 7
HELIX 97 97 LEU E 303 ARG E 306 5 4
HELIX 98 98 GLU E 307 ARG E 312 1 6
HELIX 99 99 ALA E 313 ALA E 315 5 3
HELIX 100 100 ALA E 323 VAL E 363 1 41
HELIX 101 101 ASP E 385 ARG E 396 1 12
HELIX 102 102 PRO E 405 GLY E 409 5 5
HELIX 103 103 GLU E 422 LEU E 437 1 16
HELIX 104 104 LEU F 5 SER F 10 1 6
HELIX 105 105 LYS F 25 ILE F 30 1 6
HELIX 106 106 ASP F 46 ARG F 59 1 14
HELIX 107 107 LYS F 81 LEU F 89 1 9
HELIX 108 108 ASP F 98 THR F 101 5 4
HELIX 109 109 ALA F 102 GLY F 121 1 20
HELIX 110 110 ALA F 131 ARG F 150 1 20
HELIX 111 111 GLY F 167 ALA F 176 1 10
HELIX 112 112 ASP F 192 LEU F 200 1 9
HELIX 113 113 ARG F 221 ALA F 232 1 12
HELIX 114 114 ALA F 241 ILE F 246 5 6
HELIX 115 115 ARG F 251 GLY F 256 5 6
HELIX 116 116 HIS F 272 GLY F 276 5 5
HELIX 117 117 ALA F 286 LEU F 292 5 7
HELIX 118 118 ASN F 323 LYS F 363 1 41
HELIX 119 119 ARG F 386 LEU F 397 1 12
HELIX 120 120 ALA F 423 LEU F 438 1 16
HELIX 121 121 PRO F 441 ASN F 447 1 7
HELIX 122 122 ASP F 458 HIS F 465 1 8
HELIX 123 123 THR G 7 VAL G 18 1 12
HELIX 124 124 LEU G 23 ALA G 28 5 6
HELIX 125 125 PRO G 31 LEU G 35 5 5
HELIX 126 126 PRO G 46 ALA G 59 1 14
HELIX 127 127 PRO G 79 ALA G 86 1 8
HELIX 128 128 ARG G 88 ALA G 94 1 7
HELIX 129 129 GLN G 99 VAL G 102 5 4
HELIX 130 130 SER G 103 GLY G 122 1 20
HELIX 131 131 ASP G 132 GLY G 149 1 18
HELIX 132 132 HIS G 160 VAL G 174 1 15
HELIX 133 133 LEU G 214 GLY G 225 1 12
HELIX 134 134 PRO G 234 VAL G 239 5 6
HELIX 135 135 PRO G 242 GLY G 247 1 6
HELIX 136 136 GLN G 256 LEU G 258 5 3
HELIX 137 137 MET G 262 GLY G 266 5 5
HELIX 138 138 LYS G 276 LEU G 282 5 7
HELIX 139 139 LEU G 303 ARG G 306 5 4
HELIX 140 140 GLU G 307 ARG G 312 1 6
HELIX 141 141 ALA G 313 ALA G 315 5 3
HELIX 142 142 ALA G 323 LEU G 361 1 39
HELIX 143 143 ASP G 385 ARG G 396 1 12
HELIX 144 144 PRO G 405 GLY G 409 5 5
HELIX 145 145 GLU G 422 LEU G 437 1 16
HELIX 146 146 LEU H 5 SER H 10 1 6
HELIX 147 147 LYS H 25 ILE H 30 1 6
HELIX 148 148 PRO H 31 LEU H 35 5 5
HELIX 149 149 ASP H 46 ARG H 59 1 14
HELIX 150 150 PRO H 80 LEU H 89 1 10
HELIX 151 151 ASP H 98 THR H 101 5 4
HELIX 152 152 ALA H 102 GLY H 121 1 20
HELIX 153 153 ALA H 131 ARG H 150 1 20
HELIX 154 154 GLY H 167 ALA H 176 1 10
HELIX 155 155 ASP H 192 LEU H 200 1 9
HELIX 156 156 ARG H 221 ALA H 232 1 12
HELIX 157 157 ALA H 241 ILE H 246 5 6
HELIX 158 158 ALA H 286 LEU H 292 5 7
HELIX 159 159 ASN H 323 GLU H 362 1 40
HELIX 160 160 ARG H 386 LEU H 397 1 12
HELIX 161 161 ALA H 423 LEU H 437 1 15
HELIX 162 162 LEU H 438 LYS H 440 5 3
HELIX 163 163 PRO H 441 ASN H 447 1 7
HELIX 164 164 ASP H 458 HIS H 465 1 8
SHEET 1 A 7 ILE A 125 ALA A 126 0
SHEET 2 A 7 GLY A 270 THR A 274 -1 O THR A 274 N ILE A 125
SHEET 3 A 7 ILE A 250 ASP A 254 -1 N ALA A 251 O ALA A 273
SHEET 4 A 7 LEU A 227 VAL A 231 1 N ALA A 230 O ILE A 250
SHEET 5 A 7 VAL A 197 GLN A 203 1 N VAL A 202 O VAL A 231
SHEET 6 A 7 GLY A 152 SER A 156 1 N LEU A 154 O VAL A 201
SHEET 7 A 7 LYS A 177 LEU A 181 1 O LEU A 179 N VAL A 155
SHEET 1 B 2 VAL A 287 VAL A 291 0
SHEET 2 B 2 ARG A 297 LEU A 301 -1 O ILE A 300 N SER A 288
SHEET 1 C 4 ARG A 367 PRO A 368 0
SHEET 2 C 4 GLU A 377 ALA A 381 -1 O ALA A 381 N ARG A 367
SHEET 3 C 4 LEU A 412 ALA A 416 -1 O ALA A 413 N LEU A 380
SHEET 4 C 4 THR A 402 PRO A 403 -1 N THR A 402 O LEU A 414
SHEET 1 D 7 ALA B 124 THR B 126 0
SHEET 2 D 7 VAL B 282 VAL B 284 -1 O VAL B 284 N ALA B 124
SHEET 3 D 7 VAL B 259 HIS B 261 -1 N VAL B 260 O GLY B 283
SHEET 4 D 7 GLN B 235 ASP B 239 1 N TYR B 238 O VAL B 259
SHEET 5 D 7 VAL B 204 LEU B 209 1 N LEU B 209 O ASP B 239
SHEET 6 D 7 VAL B 158 PRO B 162 1 N VAL B 158 O ALA B 205
SHEET 7 D 7 GLN B 179 ILE B 183 1 O GLN B 179 N VAL B 159
SHEET 1 E 2 LEU B 296 ARG B 299 0
SHEET 2 E 2 PHE B 304 ASP B 307 -1 O ASP B 307 N LEU B 296
SHEET 1 F 3 PHE B 377 ALA B 379 0
SHEET 2 F 3 LEU B 414 VAL B 416 -1 O LEU B 414 N ALA B 379
SHEET 3 F 3 THR B 403 VAL B 404 -1 N THR B 403 O MET B 415
SHEET 1 G 7 ILE C 125 ALA C 126 0
SHEET 2 G 7 GLY C 270 THR C 274 -1 O THR C 274 N ILE C 125
SHEET 3 G 7 ILE C 250 ASP C 254 -1 N ALA C 251 O ALA C 273
SHEET 4 G 7 LEU C 227 VAL C 231 1 N ALA C 230 O ILE C 250
SHEET 5 G 7 VAL C 197 GLN C 203 1 N VAL C 200 O VAL C 229
SHEET 6 G 7 GLY C 152 SER C 156 1 N LEU C 154 O VAL C 201
SHEET 7 G 7 LYS C 177 LEU C 181 1 O LEU C 179 N VAL C 153
SHEET 1 H 2 VAL C 287 VAL C 291 0
SHEET 2 H 2 ARG C 297 LEU C 301 -1 O ILE C 300 N SER C 288
SHEET 1 I 4 ARG C 367 PRO C 368 0
SHEET 2 I 4 GLU C 377 ALA C 381 -1 O ALA C 381 N ARG C 367
SHEET 3 I 4 LEU C 412 ALA C 416 -1 O ALA C 413 N LEU C 380
SHEET 4 I 4 THR C 402 PRO C 403 -1 N THR C 402 O LEU C 414
SHEET 1 J 7 ALA D 124 THR D 126 0
SHEET 2 J 7 VAL D 282 VAL D 284 -1 O VAL D 282 N THR D 126
SHEET 3 J 7 VAL D 259 HIS D 261 -1 N VAL D 260 O GLY D 283
SHEET 4 J 7 GLN D 235 ASP D 239 1 N TYR D 238 O VAL D 259
SHEET 5 J 7 VAL D 204 THR D 210 1 N LEU D 209 O ASP D 239
SHEET 6 J 7 VAL D 158 PRO D 162 1 N VAL D 158 O ALA D 205
SHEET 7 J 7 GLN D 179 ILE D 183 1 O GLN D 179 N VAL D 159
SHEET 1 K 2 LEU D 296 ARG D 299 0
SHEET 2 K 2 PHE D 304 ASP D 307 -1 O ASP D 307 N LEU D 296
SHEET 1 L 3 PHE D 377 ALA D 379 0
SHEET 2 L 3 LEU D 414 VAL D 416 -1 O VAL D 416 N PHE D 377
SHEET 3 L 3 THR D 403 VAL D 404 -1 N THR D 403 O MET D 415
SHEET 1 M 7 ILE E 125 ALA E 126 0
SHEET 2 M 7 GLY E 270 THR E 274 -1 O THR E 274 N ILE E 125
SHEET 3 M 7 ILE E 250 ASP E 254 -1 N ALA E 251 O ALA E 273
SHEET 4 M 7 LEU E 227 VAL E 231 1 N ALA E 230 O ILE E 250
SHEET 5 M 7 VAL E 197 GLN E 203 1 N VAL E 200 O VAL E 229
SHEET 6 M 7 GLY E 152 SER E 156 1 N LEU E 154 O VAL E 201
SHEET 7 M 7 LYS E 177 LEU E 181 1 O LEU E 179 N VAL E 155
SHEET 1 N 2 VAL E 287 VAL E 291 0
SHEET 2 N 2 ARG E 297 LEU E 301 -1 O ILE E 300 N SER E 288
SHEET 1 O 4 ARG E 367 PRO E 368 0
SHEET 2 O 4 GLU E 377 ALA E 381 -1 O ALA E 381 N ARG E 367
SHEET 3 O 4 LEU E 412 ALA E 416 -1 O ALA E 413 N LEU E 380
SHEET 4 O 4 THR E 402 VAL E 404 -1 N VAL E 404 O LEU E 412
SHEET 1 P 7 ALA F 124 THR F 126 0
SHEET 2 P 7 VAL F 282 VAL F 284 -1 O VAL F 284 N ALA F 124
SHEET 3 P 7 VAL F 259 HIS F 261 -1 N VAL F 260 O GLY F 283
SHEET 4 P 7 GLN F 235 ASP F 239 1 N TYR F 238 O VAL F 259
SHEET 5 P 7 VAL F 204 LEU F 209 1 N LEU F 207 O TYR F 237
SHEET 6 P 7 VAL F 158 PRO F 162 1 N LEU F 160 O ALA F 206
SHEET 7 P 7 GLN F 179 ILE F 183 1 O GLN F 179 N VAL F 159
SHEET 1 Q 2 LEU F 296 ARG F 299 0
SHEET 2 Q 2 PHE F 304 ASP F 307 -1 O ASP F 307 N LEU F 296
SHEET 1 R 3 PHE F 377 ALA F 379 0
SHEET 2 R 3 LEU F 414 VAL F 416 -1 O VAL F 416 N PHE F 377
SHEET 3 R 3 THR F 403 VAL F 404 -1 N THR F 403 O MET F 415
SHEET 1 S 7 ILE G 125 ALA G 126 0
SHEET 2 S 7 GLY G 270 THR G 274 -1 O THR G 274 N ILE G 125
SHEET 3 S 7 ILE G 250 ASP G 254 -1 N ALA G 251 O ALA G 273
SHEET 4 S 7 LEU G 227 VAL G 231 1 N ALA G 230 O VAL G 252
SHEET 5 S 7 VAL G 197 GLN G 203 1 N VAL G 200 O VAL G 229
SHEET 6 S 7 GLY G 152 SER G 156 1 N GLY G 152 O GLY G 198
SHEET 7 S 7 LYS G 177 LEU G 181 1 O LEU G 181 N VAL G 155
SHEET 1 T 2 VAL G 287 VAL G 291 0
SHEET 2 T 2 ARG G 297 LEU G 301 -1 O ILE G 300 N SER G 288
SHEET 1 U 4 ARG G 367 PRO G 368 0
SHEET 2 U 4 GLU G 377 ALA G 381 -1 O ALA G 381 N ARG G 367
SHEET 3 U 4 LEU G 412 ALA G 416 -1 O ALA G 413 N LEU G 380
SHEET 4 U 4 THR G 402 PRO G 403 -1 N THR G 402 O LEU G 414
SHEET 1 V 7 ALA H 124 THR H 126 0
SHEET 2 V 7 VAL H 282 VAL H 284 -1 O VAL H 282 N THR H 126
SHEET 3 V 7 VAL H 259 HIS H 261 -1 N VAL H 260 O GLY H 283
SHEET 4 V 7 GLN H 235 ASP H 239 1 N TYR H 238 O VAL H 259
SHEET 5 V 7 VAL H 204 THR H 210 1 N LEU H 207 O TYR H 237
SHEET 6 V 7 VAL H 158 PRO H 162 1 N LEU H 160 O ALA H 206
SHEET 7 V 7 GLN H 179 ILE H 183 1 O GLN H 179 N VAL H 159
SHEET 1 W 2 LEU H 296 GLY H 300 0
SHEET 2 W 2 GLY H 303 ASP H 307 -1 O ASP H 307 N LEU H 296
SHEET 1 X 3 PHE H 377 ALA H 379 0
SHEET 2 X 3 LEU H 414 VAL H 416 -1 O VAL H 416 N PHE H 377
SHEET 3 X 3 THR H 403 VAL H 404 -1 N THR H 403 O MET H 415
LINK C4A PLP B1475 N1 AOA B1476 1555 1555 1.39
LINK C4A PLP D2475 N1 AOA D2476 1555 1555 1.39
LINK C4A PLP F3475 N1 AOA F3476 1555 1555 1.39
LINK C4A PLP H4475 N1 AOA H4476 1555 1555 1.39
CISPEP 1 ASN A 204 PRO A 205 0 -0.54
CISPEP 2 GLY A 266 PRO A 267 0 0.12
CISPEP 3 LYS A 372 PRO A 373 0 -0.10
CISPEP 4 ASN B 211 PRO B 212 0 0.03
CISPEP 5 GLY B 276 PRO B 277 0 -0.03
CISPEP 6 VAL B 294 PRO B 295 0 -0.25
CISPEP 7 PHE B 406 PRO B 407 0 0.04
CISPEP 8 ALA B 448 PRO B 449 0 -0.15
CISPEP 9 ASN C 204 PRO C 205 0 -0.14
CISPEP 10 GLY C 266 PRO C 267 0 -0.15
CISPEP 11 LYS C 372 PRO C 373 0 0.02
CISPEP 12 ASN D 211 PRO D 212 0 0.17
CISPEP 13 GLY D 276 PRO D 277 0 0.10
CISPEP 14 VAL D 294 PRO D 295 0 -0.05
CISPEP 15 PHE D 406 PRO D 407 0 -0.13
CISPEP 16 ALA D 448 PRO D 449 0 0.14
CISPEP 17 ASN E 204 PRO E 205 0 -0.19
CISPEP 18 GLY E 266 PRO E 267 0 0.21
CISPEP 19 LYS E 372 PRO E 373 0 -0.11
CISPEP 20 ASN F 211 PRO F 212 0 0.14
CISPEP 21 GLY F 276 PRO F 277 0 0.06
CISPEP 22 VAL F 294 PRO F 295 0 -0.24
CISPEP 23 PHE F 406 PRO F 407 0 -0.30
CISPEP 24 ALA F 448 PRO F 449 0 0.05
CISPEP 25 ASN G 204 PRO G 205 0 -0.33
CISPEP 26 GLY G 266 PRO G 267 0 0.18
CISPEP 27 LYS G 372 PRO G 373 0 -0.15
CISPEP 28 ASN H 211 PRO H 212 0 0.11
CISPEP 29 GLY H 276 PRO H 277 0 -0.06
CISPEP 30 VAL H 294 PRO H 295 0 -0.18
CISPEP 31 PHE H 406 PRO H 407 0 0.01
CISPEP 32 ALA H 448 PRO H 449 0 0.20
SITE 1 AC1 17 THR A 320 THR A 321 HOH A 496 SER B 73
SITE 2 AC1 17 ALA B 131 GLY B 132 ALA B 133 GLU B 136
SITE 3 AC1 17 HIS B 166 SER B 168 ASP B 239 ALA B 241
SITE 4 AC1 17 ASN B 263 HIS B 265 LYS B 266 AOA B1476
SITE 5 AC1 17 HOH B1516
SITE 1 AC2 8 TYR A 95 TYR A 98 GLN A 308 THR A 320
SITE 2 AC2 8 HOH A 521 HIS B 166 PLP B1475 HOH B1615
SITE 1 AC3 15 THR C 320 THR C 321 HOH C 497 SER D 73
SITE 2 AC3 15 GLY D 132 ALA D 133 GLU D 136 HIS D 166
SITE 3 AC3 15 SER D 168 ASP D 239 ALA D 241 ASN D 263
SITE 4 AC3 15 HIS D 265 LYS D 266 AOA D2476
SITE 1 AC4 8 TYR C 95 TYR C 98 GLN C 308 THR C 320
SITE 2 AC4 8 HOH C 583 HIS D 166 PLP D2475 HOH D2586
SITE 1 AC5 17 THR E 320 THR E 321 HOH E 463 HOH E 573
SITE 2 AC5 17 SER F 73 ALA F 131 GLY F 132 ALA F 133
SITE 3 AC5 17 GLU F 136 HIS F 166 SER F 168 ASP F 239
SITE 4 AC5 17 ALA F 241 ASN F 263 HIS F 265 LYS F 266
SITE 5 AC5 17 AOA F3476
SITE 1 AC6 6 TYR E 95 TYR E 98 GLN E 308 THR E 320
SITE 2 AC6 6 HIS F 166 PLP F3475
SITE 1 AC7 15 THR G 320 THR G 321 SER H 73 GLY H 132
SITE 2 AC7 15 ALA H 133 GLU H 136 HIS H 166 SER H 168
SITE 3 AC7 15 ASP H 239 ALA H 241 ASN H 263 HIS H 265
SITE 4 AC7 15 LYS H 266 AOA H4476 HOH H4496
SITE 1 AC8 7 TYR G 95 TYR G 98 GLN G 308 THR G 320
SITE 2 AC8 7 HOH G 568 HIS H 166 PLP H4475
CRYST1 134.173 166.317 190.299 90.00 90.00 90.00 P 21 21 21 16
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 0.007453 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006013 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005255 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
