HEADER OXIDOREDUCTASE 08-MAY-11 3RWB
TITLE CRYSTAL STRUCTURE OF COMPLEX OF 4PAL (4-PYRIDOXOLACTONE) AND PLDH
TITLE 2 (TETRAMERIC PYRIDOXAL 4-DEHYDROGENASE) FROM MESORHIZOBIUM LOTI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRIDOXAL 4-DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: TPLDH;
COMPND 5 EC: 1.1.1.107;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MESORHIZOBIUM LOTI;
SOURCE 3 ORGANISM_TAXID: 381;
SOURCE 4 GENE: MLR6807, PLDH-T;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS SHORT CHAIN DEHYDROGENASE/REDUCTASE, PYRIDOXAL, 4-PYRIDOXOLACTONE,
KEYWDS 2 NAD+, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.N.CHU
REVDAT 2 01-NOV-23 3RWB 1 REMARK
REVDAT 1 09-MAY-12 3RWB 0
JRNL AUTH T.YAGI,H.N.CHU
JRNL TITL CRYSTAL STRUCTURE OF COMPLEX OF 4PAL (4-PYRIDOXOLACTONE) AND
JRNL TITL 2 PLDH (TETRAMERIC PYRIDOXAL 4-DEHYDROGENASE) FROM
JRNL TITL 3 MESORHIZOBIUM LOTI
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 88381
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.135
REMARK 3 FREE R VALUE : 0.166
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4427
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.0762 - 5.2753 0.99 2921 149 0.1753 0.1937
REMARK 3 2 5.2753 - 4.1888 1.00 2856 158 0.1222 0.1324
REMARK 3 3 4.1888 - 3.6597 1.00 2835 156 0.1153 0.1402
REMARK 3 4 3.6597 - 3.3253 1.00 2826 150 0.1229 0.1363
REMARK 3 5 3.3253 - 3.0871 1.00 2852 139 0.1286 0.1536
REMARK 3 6 3.0871 - 2.9051 1.00 2804 155 0.1302 0.1856
REMARK 3 7 2.9051 - 2.7597 1.00 2779 161 0.1285 0.1496
REMARK 3 8 2.7597 - 2.6396 1.00 2816 147 0.1332 0.1725
REMARK 3 9 2.6396 - 2.5380 1.00 2790 151 0.1332 0.1583
REMARK 3 10 2.5380 - 2.4504 1.00 2823 168 0.1327 0.1815
REMARK 3 11 2.4504 - 2.3738 1.00 2747 144 0.1417 0.1797
REMARK 3 12 2.3738 - 2.3060 1.00 2808 165 0.1350 0.1626
REMARK 3 13 2.3060 - 2.2453 1.00 2811 149 0.1318 0.1603
REMARK 3 14 2.2453 - 2.1905 1.00 2783 148 0.1209 0.1599
REMARK 3 15 2.1905 - 2.1407 1.00 2785 158 0.1282 0.1618
REMARK 3 16 2.1407 - 2.0951 1.00 2790 127 0.1240 0.1747
REMARK 3 17 2.0951 - 2.0532 1.00 2816 161 0.1292 0.1472
REMARK 3 18 2.0532 - 2.0145 1.00 2766 166 0.1246 0.1773
REMARK 3 19 2.0145 - 1.9785 1.00 2806 144 0.1286 0.1843
REMARK 3 20 1.9785 - 1.9450 1.00 2753 148 0.1258 0.1827
REMARK 3 21 1.9450 - 1.9136 1.00 2805 142 0.1227 0.1560
REMARK 3 22 1.9136 - 1.8842 1.00 2830 135 0.1252 0.1674
REMARK 3 23 1.8842 - 1.8564 1.00 2749 143 0.1299 0.1925
REMARK 3 24 1.8564 - 1.8303 1.00 2810 150 0.1288 0.1751
REMARK 3 25 1.8303 - 1.8056 1.00 2750 148 0.1340 0.1850
REMARK 3 26 1.8056 - 1.7821 1.00 2817 136 0.1291 0.1685
REMARK 3 27 1.7821 - 1.7598 1.00 2823 136 0.1258 0.1674
REMARK 3 28 1.7598 - 1.7386 1.00 2769 131 0.1223 0.1726
REMARK 3 29 1.7386 - 1.7184 1.00 2791 138 0.1269 0.1680
REMARK 3 30 1.7184 - 1.6991 0.95 2643 124 0.1255 0.1826
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 60.16
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04240
REMARK 3 B22 (A**2) : -1.07730
REMARK 3 B33 (A**2) : 1.03480
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.14580
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 7797
REMARK 3 ANGLE : 1.192 10667
REMARK 3 CHIRALITY : 0.078 1254
REMARK 3 PLANARITY : 0.004 1363
REMARK 3 DIHEDRAL : 16.686 2811
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RWB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065456.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88415
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.699
REMARK 200 RESOLUTION RANGE LOW (A) : 39.066
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: 3NUG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, 0.1M TRIS-HCL,
REMARK 280 PEG 4000 30%, 0.65MM PYRIDOXAL, PH 7.0, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 25.10550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS C 45 CE
REMARK 480 GLU C 199 OE1
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 OD1 ASP B 110 O HOH B 796 2.17
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 LYS A 53 -134.65 50.70
REMARK 500 ALA A 140 -126.59 -98.99
REMARK 500 SER A 141 141.96 -171.80
REMARK 500 MET A 151 33.66 -147.08
REMARK 500 ASP A 242 21.54 -154.10
REMARK 500 LYS B 53 -72.92 51.32
REMARK 500 ALA B 140 -126.66 -99.61
REMARK 500 SER B 141 139.60 -172.11
REMARK 500 MET B 151 34.94 -152.10
REMARK 500 ASP B 242 23.01 -157.05
REMARK 500 GLU C 3 90.40 135.04
REMARK 500 GLU C 3 86.75 137.15
REMARK 500 ALA C 140 -127.00 -99.07
REMARK 500 SER C 141 139.43 -171.68
REMARK 500 MET C 151 34.13 -153.38
REMARK 500 ASP C 242 23.50 -155.20
REMARK 500 ALA D 140 -127.30 -96.73
REMARK 500 SER D 141 139.20 -170.77
REMARK 500 MET D 151 34.36 -150.49
REMARK 500 ASP D 242 23.23 -152.65
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 GLY B 52 LYS B 53 -148.86
REMARK 500 LYS B 53 LYS B 54 139.95
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 NAD A 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4PL A 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4PL B 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4PL C 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 249
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 251
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4PL D 252
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 249
DBREF 3RWB A 2 248 UNP Q988B7 PLDH_RHILO 2 248
DBREF 3RWB B 2 248 UNP Q988B7 PLDH_RHILO 2 248
DBREF 3RWB C 2 248 UNP Q988B7 PLDH_RHILO 2 248
DBREF 3RWB D 2 248 UNP Q988B7 PLDH_RHILO 2 248
SEQRES 1 A 247 THR GLU ARG LEU ALA GLY LYS THR ALA LEU VAL THR GLY
SEQRES 2 A 247 ALA ALA GLN GLY ILE GLY LYS ALA ILE ALA ALA ARG LEU
SEQRES 3 A 247 ALA ALA ASP GLY ALA THR VAL ILE VAL SER ASP ILE ASN
SEQRES 4 A 247 ALA GLU GLY ALA LYS ALA ALA ALA ALA SER ILE GLY LYS
SEQRES 5 A 247 LYS ALA ARG ALA ILE ALA ALA ASP ILE SER ASP PRO GLY
SEQRES 6 A 247 SER VAL LYS ALA LEU PHE ALA GLU ILE GLN ALA LEU THR
SEQRES 7 A 247 GLY GLY ILE ASP ILE LEU VAL ASN ASN ALA SER ILE VAL
SEQRES 8 A 247 PRO PHE VAL ALA TRP ASP ASP VAL ASP LEU ASP HIS TRP
SEQRES 9 A 247 ARG LYS ILE ILE ASP VAL ASN LEU THR GLY THR PHE ILE
SEQRES 10 A 247 VAL THR ARG ALA GLY THR ASP GLN MET ARG ALA ALA GLY
SEQRES 11 A 247 LYS ALA GLY ARG VAL ILE SER ILE ALA SER ASN THR PHE
SEQRES 12 A 247 PHE ALA GLY THR PRO ASN MET ALA ALA TYR VAL ALA ALA
SEQRES 13 A 247 LYS GLY GLY VAL ILE GLY PHE THR ARG ALA LEU ALA THR
SEQRES 14 A 247 GLU LEU GLY LYS TYR ASN ILE THR ALA ASN ALA VAL THR
SEQRES 15 A 247 PRO GLY LEU ILE GLU SER ASP GLY VAL LYS ALA SER PRO
SEQRES 16 A 247 HIS ASN GLU ALA PHE GLY PHE VAL GLU MET LEU GLN ALA
SEQRES 17 A 247 MET LYS GLY LYS GLY GLN PRO GLU HIS ILE ALA ASP VAL
SEQRES 18 A 247 VAL SER PHE LEU ALA SER ASP ASP ALA ARG TRP ILE THR
SEQRES 19 A 247 GLY GLN THR LEU ASN VAL ASP ALA GLY MET VAL ARG HIS
SEQRES 1 B 247 THR GLU ARG LEU ALA GLY LYS THR ALA LEU VAL THR GLY
SEQRES 2 B 247 ALA ALA GLN GLY ILE GLY LYS ALA ILE ALA ALA ARG LEU
SEQRES 3 B 247 ALA ALA ASP GLY ALA THR VAL ILE VAL SER ASP ILE ASN
SEQRES 4 B 247 ALA GLU GLY ALA LYS ALA ALA ALA ALA SER ILE GLY LYS
SEQRES 5 B 247 LYS ALA ARG ALA ILE ALA ALA ASP ILE SER ASP PRO GLY
SEQRES 6 B 247 SER VAL LYS ALA LEU PHE ALA GLU ILE GLN ALA LEU THR
SEQRES 7 B 247 GLY GLY ILE ASP ILE LEU VAL ASN ASN ALA SER ILE VAL
SEQRES 8 B 247 PRO PHE VAL ALA TRP ASP ASP VAL ASP LEU ASP HIS TRP
SEQRES 9 B 247 ARG LYS ILE ILE ASP VAL ASN LEU THR GLY THR PHE ILE
SEQRES 10 B 247 VAL THR ARG ALA GLY THR ASP GLN MET ARG ALA ALA GLY
SEQRES 11 B 247 LYS ALA GLY ARG VAL ILE SER ILE ALA SER ASN THR PHE
SEQRES 12 B 247 PHE ALA GLY THR PRO ASN MET ALA ALA TYR VAL ALA ALA
SEQRES 13 B 247 LYS GLY GLY VAL ILE GLY PHE THR ARG ALA LEU ALA THR
SEQRES 14 B 247 GLU LEU GLY LYS TYR ASN ILE THR ALA ASN ALA VAL THR
SEQRES 15 B 247 PRO GLY LEU ILE GLU SER ASP GLY VAL LYS ALA SER PRO
SEQRES 16 B 247 HIS ASN GLU ALA PHE GLY PHE VAL GLU MET LEU GLN ALA
SEQRES 17 B 247 MET LYS GLY LYS GLY GLN PRO GLU HIS ILE ALA ASP VAL
SEQRES 18 B 247 VAL SER PHE LEU ALA SER ASP ASP ALA ARG TRP ILE THR
SEQRES 19 B 247 GLY GLN THR LEU ASN VAL ASP ALA GLY MET VAL ARG HIS
SEQRES 1 C 247 THR GLU ARG LEU ALA GLY LYS THR ALA LEU VAL THR GLY
SEQRES 2 C 247 ALA ALA GLN GLY ILE GLY LYS ALA ILE ALA ALA ARG LEU
SEQRES 3 C 247 ALA ALA ASP GLY ALA THR VAL ILE VAL SER ASP ILE ASN
SEQRES 4 C 247 ALA GLU GLY ALA LYS ALA ALA ALA ALA SER ILE GLY LYS
SEQRES 5 C 247 LYS ALA ARG ALA ILE ALA ALA ASP ILE SER ASP PRO GLY
SEQRES 6 C 247 SER VAL LYS ALA LEU PHE ALA GLU ILE GLN ALA LEU THR
SEQRES 7 C 247 GLY GLY ILE ASP ILE LEU VAL ASN ASN ALA SER ILE VAL
SEQRES 8 C 247 PRO PHE VAL ALA TRP ASP ASP VAL ASP LEU ASP HIS TRP
SEQRES 9 C 247 ARG LYS ILE ILE ASP VAL ASN LEU THR GLY THR PHE ILE
SEQRES 10 C 247 VAL THR ARG ALA GLY THR ASP GLN MET ARG ALA ALA GLY
SEQRES 11 C 247 LYS ALA GLY ARG VAL ILE SER ILE ALA SER ASN THR PHE
SEQRES 12 C 247 PHE ALA GLY THR PRO ASN MET ALA ALA TYR VAL ALA ALA
SEQRES 13 C 247 LYS GLY GLY VAL ILE GLY PHE THR ARG ALA LEU ALA THR
SEQRES 14 C 247 GLU LEU GLY LYS TYR ASN ILE THR ALA ASN ALA VAL THR
SEQRES 15 C 247 PRO GLY LEU ILE GLU SER ASP GLY VAL LYS ALA SER PRO
SEQRES 16 C 247 HIS ASN GLU ALA PHE GLY PHE VAL GLU MET LEU GLN ALA
SEQRES 17 C 247 MET LYS GLY LYS GLY GLN PRO GLU HIS ILE ALA ASP VAL
SEQRES 18 C 247 VAL SER PHE LEU ALA SER ASP ASP ALA ARG TRP ILE THR
SEQRES 19 C 247 GLY GLN THR LEU ASN VAL ASP ALA GLY MET VAL ARG HIS
SEQRES 1 D 247 THR GLU ARG LEU ALA GLY LYS THR ALA LEU VAL THR GLY
SEQRES 2 D 247 ALA ALA GLN GLY ILE GLY LYS ALA ILE ALA ALA ARG LEU
SEQRES 3 D 247 ALA ALA ASP GLY ALA THR VAL ILE VAL SER ASP ILE ASN
SEQRES 4 D 247 ALA GLU GLY ALA LYS ALA ALA ALA ALA SER ILE GLY LYS
SEQRES 5 D 247 LYS ALA ARG ALA ILE ALA ALA ASP ILE SER ASP PRO GLY
SEQRES 6 D 247 SER VAL LYS ALA LEU PHE ALA GLU ILE GLN ALA LEU THR
SEQRES 7 D 247 GLY GLY ILE ASP ILE LEU VAL ASN ASN ALA SER ILE VAL
SEQRES 8 D 247 PRO PHE VAL ALA TRP ASP ASP VAL ASP LEU ASP HIS TRP
SEQRES 9 D 247 ARG LYS ILE ILE ASP VAL ASN LEU THR GLY THR PHE ILE
SEQRES 10 D 247 VAL THR ARG ALA GLY THR ASP GLN MET ARG ALA ALA GLY
SEQRES 11 D 247 LYS ALA GLY ARG VAL ILE SER ILE ALA SER ASN THR PHE
SEQRES 12 D 247 PHE ALA GLY THR PRO ASN MET ALA ALA TYR VAL ALA ALA
SEQRES 13 D 247 LYS GLY GLY VAL ILE GLY PHE THR ARG ALA LEU ALA THR
SEQRES 14 D 247 GLU LEU GLY LYS TYR ASN ILE THR ALA ASN ALA VAL THR
SEQRES 15 D 247 PRO GLY LEU ILE GLU SER ASP GLY VAL LYS ALA SER PRO
SEQRES 16 D 247 HIS ASN GLU ALA PHE GLY PHE VAL GLU MET LEU GLN ALA
SEQRES 17 D 247 MET LYS GLY LYS GLY GLN PRO GLU HIS ILE ALA ASP VAL
SEQRES 18 D 247 VAL SER PHE LEU ALA SER ASP ASP ALA ARG TRP ILE THR
SEQRES 19 D 247 GLY GLN THR LEU ASN VAL ASP ALA GLY MET VAL ARG HIS
HET NAD A 251 44
HET 4PL A 252 12
HET GOL A 1 6
HET GOL A 249 6
HET GOL A 250 6
HET NAD B 251 44
HET 4PL B 252 12
HET NAD C 251 44
HET 4PL C 252 12
HET GOL C 249 6
HET NAD D 251 44
HET 4PL D 252 12
HET GOL D 249 6
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 4PL 7-HYDROXY-6-METHYLFURO[3,4-C]PYRIDIN-1(3H)-ONE
HETNAM GOL GLYCEROL
HETSYN 4PL 4-PYRIDOXOLACTONE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 NAD 4(C21 H27 N7 O14 P2)
FORMUL 6 4PL 4(C8 H7 N O3)
FORMUL 7 GOL 5(C3 H8 O3)
FORMUL 18 HOH *914(H2 O)
HELIX 1 1 GLN A 17 ASP A 30 1 14
HELIX 2 2 ASN A 40 GLY A 52 1 13
HELIX 3 3 ASP A 64 GLY A 80 1 17
HELIX 4 4 ALA A 96 VAL A 100 5 5
HELIX 5 5 ASP A 101 LEU A 113 1 13
HELIX 6 6 LEU A 113 GLY A 131 1 19
HELIX 7 7 ASN A 142 GLY A 147 1 6
HELIX 8 8 MET A 151 GLY A 173 1 23
HELIX 9 9 SER A 189 ALA A 194 1 6
HELIX 10 10 SER A 195 GLU A 199 5 5
HELIX 11 11 ALA A 200 GLN A 208 1 9
HELIX 12 12 GLN A 215 SER A 228 1 14
HELIX 13 13 ASP A 229 ARG A 232 5 4
HELIX 14 14 GLN B 17 ASP B 30 1 14
HELIX 15 15 ASN B 40 GLY B 52 1 13
HELIX 16 16 ASP B 64 GLY B 80 1 17
HELIX 17 17 ALA B 96 VAL B 100 5 5
HELIX 18 18 ASP B 101 LEU B 113 1 13
HELIX 19 19 LEU B 113 ALA B 130 1 18
HELIX 20 20 ASN B 142 GLY B 147 1 6
HELIX 21 21 MET B 151 GLY B 173 1 23
HELIX 22 22 SER B 189 ALA B 194 1 6
HELIX 23 23 SER B 195 GLU B 199 5 5
HELIX 24 24 ALA B 200 GLN B 208 1 9
HELIX 25 25 GLN B 215 SER B 228 1 14
HELIX 26 26 ASP B 229 ARG B 232 5 4
HELIX 27 27 GLN C 17 ASP C 30 1 14
HELIX 28 28 ASN C 40 GLY C 52 1 13
HELIX 29 29 ASP C 64 GLY C 80 1 17
HELIX 30 30 ALA C 96 VAL C 100 5 5
HELIX 31 31 ASP C 101 LEU C 113 1 13
HELIX 32 32 LEU C 113 ALA C 130 1 18
HELIX 33 33 ASN C 142 GLY C 147 1 6
HELIX 34 34 MET C 151 GLY C 173 1 23
HELIX 35 35 LYS C 174 ASN C 176 5 3
HELIX 36 36 SER C 189 ALA C 194 1 6
HELIX 37 37 SER C 195 GLU C 199 5 5
HELIX 38 38 ALA C 200 GLN C 208 1 9
HELIX 39 39 GLN C 215 SER C 228 1 14
HELIX 40 40 ASP C 229 ARG C 232 5 4
HELIX 41 41 GLN D 17 ASP D 30 1 14
HELIX 42 42 ASN D 40 GLY D 52 1 13
HELIX 43 43 ASP D 64 GLY D 80 1 17
HELIX 44 44 ALA D 96 VAL D 100 5 5
HELIX 45 45 ASP D 101 LEU D 113 1 13
HELIX 46 46 LEU D 113 ALA D 130 1 18
HELIX 47 47 ASN D 142 GLY D 147 1 6
HELIX 48 48 MET D 151 GLY D 173 1 23
HELIX 49 49 SER D 189 ALA D 194 1 6
HELIX 50 50 SER D 195 GLU D 199 5 5
HELIX 51 51 ALA D 200 GLN D 208 1 9
HELIX 52 52 GLN D 215 SER D 228 1 14
HELIX 53 53 ASP D 229 ARG D 232 5 4
SHEET 1 A 7 ALA A 55 ALA A 57 0
SHEET 2 A 7 THR A 33 SER A 37 1 N VAL A 36 O ARG A 56
SHEET 3 A 7 THR A 9 THR A 13 1 N ALA A 10 O ILE A 35
SHEET 4 A 7 ILE A 84 ASN A 87 1 O VAL A 86 N LEU A 11
SHEET 5 A 7 GLY A 134 ILE A 139 1 O ARG A 135 N LEU A 85
SHEET 6 A 7 ILE A 177 PRO A 184 1 O THR A 178 N VAL A 136
SHEET 7 A 7 THR A 238 VAL A 241 1 O LEU A 239 N ALA A 181
SHEET 1 B 7 ALA B 55 ALA B 57 0
SHEET 2 B 7 THR B 33 SER B 37 1 N VAL B 36 O ARG B 56
SHEET 3 B 7 THR B 9 THR B 13 1 N ALA B 10 O ILE B 35
SHEET 4 B 7 ILE B 84 ASN B 87 1 O VAL B 86 N LEU B 11
SHEET 5 B 7 GLY B 134 ILE B 139 1 O ILE B 137 N LEU B 85
SHEET 6 B 7 ILE B 177 PRO B 184 1 O THR B 178 N VAL B 136
SHEET 7 B 7 THR B 238 VAL B 241 1 O VAL B 241 N THR B 183
SHEET 1 C 7 ALA C 55 ALA C 57 0
SHEET 2 C 7 THR C 33 VAL C 36 1 N VAL C 36 O ARG C 56
SHEET 3 C 7 THR C 9 VAL C 12 1 N ALA C 10 O ILE C 35
SHEET 4 C 7 ILE C 84 ASN C 87 1 O VAL C 86 N LEU C 11
SHEET 5 C 7 ARG C 135 ILE C 139 1 O ARG C 135 N LEU C 85
SHEET 6 C 7 THR C 178 PRO C 184 1 O THR C 178 N VAL C 136
SHEET 7 C 7 THR C 238 VAL C 241 1 O LEU C 239 N ALA C 181
SHEET 1 D 7 ALA D 55 ALA D 57 0
SHEET 2 D 7 THR D 33 SER D 37 1 N VAL D 34 O ARG D 56
SHEET 3 D 7 THR D 9 THR D 13 1 N ALA D 10 O ILE D 35
SHEET 4 D 7 ILE D 84 ASN D 87 1 O VAL D 86 N LEU D 11
SHEET 5 D 7 GLY D 134 ILE D 139 1 O ARG D 135 N LEU D 85
SHEET 6 D 7 ILE D 177 PRO D 184 1 O THR D 178 N VAL D 136
SHEET 7 D 7 THR D 238 VAL D 241 1 O LEU D 239 N ALA D 181
CISPEP 1 THR C 2 GLU C 3 0 -3.03
CISPEP 2 THR C 2 GLU C 3 0 -0.54
SITE 1 AC1 29 GLY A 14 GLN A 17 GLY A 18 ILE A 19
SITE 2 AC1 29 ASP A 38 ILE A 39 ALA A 60 ASP A 61
SITE 3 AC1 29 ILE A 62 ASN A 88 ALA A 89 SER A 90
SITE 4 AC1 29 ILE A 139 ALA A 140 TYR A 154 LYS A 158
SITE 5 AC1 29 PRO A 184 GLY A 185 LEU A 186 ILE A 187
SITE 6 AC1 29 SER A 189 GLY A 191 VAL A 192 4PL A 252
SITE 7 AC1 29 HOH A 254 HOH A 270 HOH A 273 HOH A 466
SITE 8 AC1 29 HOH A 887
SITE 1 AC2 10 VAL A 92 SER A 141 ASN A 142 THR A 143
SITE 2 AC2 10 MET A 151 TYR A 154 LEU A 186 HIS A 197
SITE 3 AC2 10 NAD A 251 HOH A 902
SITE 1 AC3 4 PRO A 93 HIS A 104 HOH A 480 HOH A 481
SITE 1 AC4 6 ARG A 247 HOH A 337 HOH A 345 HOH A 511
SITE 2 AC4 6 HOH A 805 ARG B 247
SITE 1 AC5 3 ARG A 232 GLU C 217 HIS C 218
SITE 1 AC6 34 GLY B 14 GLN B 17 GLY B 18 ILE B 19
SITE 2 AC6 34 ASP B 38 ILE B 39 ALA B 60 ASP B 61
SITE 3 AC6 34 ILE B 62 ASN B 88 ALA B 89 SER B 90
SITE 4 AC6 34 VAL B 92 VAL B 111 ILE B 139 ALA B 140
SITE 5 AC6 34 TYR B 154 LYS B 158 PRO B 184 GLY B 185
SITE 6 AC6 34 LEU B 186 ILE B 187 SER B 189 GLY B 191
SITE 7 AC6 34 VAL B 192 4PL B 252 HOH B 262 HOH B 264
SITE 8 AC6 34 HOH B 270 HOH B 337 HOH B 533 HOH B 767
SITE 9 AC6 34 HOH B 785 HOH B 904
SITE 1 AC7 10 VAL B 92 SER B 141 ASN B 142 THR B 143
SITE 2 AC7 10 MET B 151 TYR B 154 LEU B 186 HIS B 197
SITE 3 AC7 10 NAD B 251 HOH B 919
SITE 1 AC8 34 GLY C 14 GLN C 17 GLY C 18 ILE C 19
SITE 2 AC8 34 ASP C 38 ILE C 39 ALA C 60 ASP C 61
SITE 3 AC8 34 ILE C 62 ASN C 88 ALA C 89 SER C 90
SITE 4 AC8 34 VAL C 92 VAL C 111 ILE C 139 ALA C 140
SITE 5 AC8 34 TYR C 154 LYS C 158 PRO C 184 GLY C 185
SITE 6 AC8 34 LEU C 186 ILE C 187 SER C 189 GLY C 191
SITE 7 AC8 34 VAL C 192 4PL C 252 HOH C 257 HOH C 286
SITE 8 AC8 34 HOH C 305 HOH C 575 HOH C 602 HOH C 820
SITE 9 AC8 34 HOH C 821 HOH C 926
SITE 1 AC9 9 VAL C 92 SER C 141 ASN C 142 THR C 143
SITE 2 AC9 9 MET C 151 TYR C 154 HIS C 197 NAD C 251
SITE 3 AC9 9 HOH C 869
SITE 1 BC1 4 ASP C 99 ASP C 101 HIS C 104 HOH C 674
SITE 1 BC2 32 GLY D 14 GLN D 17 GLY D 18 ILE D 19
SITE 2 BC2 32 ASP D 38 ILE D 39 ALA D 60 ASP D 61
SITE 3 BC2 32 ILE D 62 ASN D 88 ALA D 89 SER D 90
SITE 4 BC2 32 VAL D 111 ILE D 139 ALA D 140 SER D 141
SITE 5 BC2 32 TYR D 154 LYS D 158 PRO D 184 GLY D 185
SITE 6 BC2 32 LEU D 186 ILE D 187 SER D 189 GLY D 191
SITE 7 BC2 32 VAL D 192 4PL D 252 HOH D 279 HOH D 291
SITE 8 BC2 32 HOH D 403 HOH D 426 HOH D 669 HOH D 868
SITE 1 BC3 9 VAL D 92 SER D 141 ASN D 142 THR D 143
SITE 2 BC3 9 MET D 151 TYR D 154 LEU D 186 NAD D 251
SITE 3 BC3 9 HOH D 944
SITE 1 BC4 5 GLN B 215 GLU B 217 HIS B 218 ARG D 232
SITE 2 BC4 5 HOH D 693
CRYST1 85.537 50.211 94.266 90.00 90.47 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011691 0.000000 0.000095 0.00000
SCALE2 0.000000 0.019916 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010609 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
