HEADER OXIDOREDUCTASE 07-APR-11 3RFV
TITLE CRYSTAL STRUCTURE OF URONATE DEHYDROGENASE FROM AGROBACTERIUM
TITLE 2 TUMEFACIENS COMPLEXED WITH NADH AND PRODUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: URONATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 1.1.1.203;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AGROBACTERIUM TUMEFACIENS;
SOURCE 3 ORGANISM_TAXID: 176299;
SOURCE 4 STRAIN: C58 / ATCC 33970;
SOURCE 5 GENE: UDH, AGR_L_3333, ATU3143;
SOURCE 6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4932
KEYWDS TERNARY COMPLEX, ROSSMANN FOLD, NAD BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.PARKKINEN,J.ROUVINEN
REVDAT 5 13-SEP-23 3RFV 1 HETSYN
REVDAT 4 29-JUL-20 3RFV 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 SITE
REVDAT 3 17-AUG-11 3RFV 1 JRNL VERSN
REVDAT 2 29-JUN-11 3RFV 1 JRNL
REVDAT 1 15-JUN-11 3RFV 0
JRNL AUTH T.PARKKINEN,H.BOER,J.JANIS,M.ANDBERG,M.PENTTILA,A.KOIVULA,
JRNL AUTH 2 J.ROUVINEN
JRNL TITL CRYSTAL STRUCTURE OF URONATE DEHYDROGENASE FROM
JRNL TITL 2 AGROBACTERIUM TUMEFACIENS.
JRNL REF J.BIOL.CHEM. V. 286 27294 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21676870
JRNL DOI 10.1074/JBC.M111.254854
REMARK 2
REMARK 2 RESOLUTION. 2.10 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 81549
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4078
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 19.7589 - 4.5081 1.00 8165 430 0.1579 0.1642
REMARK 3 2 4.5081 - 3.5852 1.00 7845 413 0.1355 0.1701
REMARK 3 3 3.5852 - 3.1340 1.00 7786 409 0.1514 0.1754
REMARK 3 4 3.1340 - 2.8484 1.00 7723 407 0.1600 0.1939
REMARK 3 5 2.8484 - 2.6447 1.00 7724 406 0.1654 0.2042
REMARK 3 6 2.6447 - 2.4891 1.00 7679 405 0.1670 0.2001
REMARK 3 7 2.4891 - 2.3647 1.00 7640 402 0.1672 0.2188
REMARK 3 8 2.3647 - 2.2619 1.00 7649 402 0.1633 0.2215
REMARK 3 9 2.2619 - 2.1749 1.00 7633 402 0.1603 0.1938
REMARK 3 10 2.1749 - 2.1000 1.00 7627 402 0.1700 0.2200
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 : 0.38
REMARK 3 B_SOL : 38.80
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.040
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) : 3.11600
REMARK 3 B22 (A**2) : 3.11600
REMARK 3 B33 (A**2) : -6.23200
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 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 6512
REMARK 3 ANGLE : 1.091 8898
REMARK 3 CHIRALITY : 0.081 951
REMARK 3 PLANARITY : 0.005 1164
REMARK 3 DIHEDRAL : 23.111 2526
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 3RFV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064879.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 2.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X12
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81563
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.00
REMARK 200 R MERGE FOR SHELL (I) : 0.36700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3RFT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM PHOSPHATE, TRIS-HCL, PH
REMARK 280 2.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
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 115.75333
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 57.87667
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 115.75333
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 57.87667
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 115.75333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 57.87667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 115.75333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 57.87667
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 27540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -199.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 BIOMT1 2 -1.000000 0.000000 0.000000 165.39000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 647 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 699 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 701 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 SER A 267
REMARK 465 MET B 1
REMARK 465 SER B 267
REMARK 465 MET C 1
REMARK 465 SER C 267
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 O HOH B 396 O HOH C 604 2.19
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 ILE A 88 -71.69 -108.67
REMARK 500 SER B 110 -159.43 -81.00
REMARK 500 SER C 110 -156.90 -80.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RFT RELATED DB: PDB
REMARK 900 RELATED ID: 3RFX RELATED DB: PDB
DBREF 3RFV A 3 267 UNP Q7CRQ0 Q7CRQ0_AGRT5 1 265
DBREF 3RFV B 3 267 UNP Q7CRQ0 Q7CRQ0_AGRT5 1 265
DBREF 3RFV C 3 267 UNP Q7CRQ0 Q7CRQ0_AGRT5 1 265
SEQADV 3RFV MET A 1 UNP Q7CRQ0 EXPRESSION TAG
SEQADV 3RFV ALA A 2 UNP Q7CRQ0 EXPRESSION TAG
SEQADV 3RFV MET B 1 UNP Q7CRQ0 EXPRESSION TAG
SEQADV 3RFV ALA B 2 UNP Q7CRQ0 EXPRESSION TAG
SEQADV 3RFV MET C 1 UNP Q7CRQ0 EXPRESSION TAG
SEQADV 3RFV ALA C 2 UNP Q7CRQ0 EXPRESSION TAG
SEQRES 1 A 267 MET ALA MET LYS ARG LEU LEU VAL THR GLY ALA ALA GLY
SEQRES 2 A 267 GLN LEU GLY ARG VAL MET ARG GLU ARG LEU ALA PRO MET
SEQRES 3 A 267 ALA GLU ILE LEU ARG LEU ALA ASP LEU SER PRO LEU ASP
SEQRES 4 A 267 PRO ALA GLY PRO ASN GLU GLU CYS VAL GLN CYS ASP LEU
SEQRES 5 A 267 ALA ASP ALA ASN ALA VAL ASN ALA MET VAL ALA GLY CYS
SEQRES 6 A 267 ASP GLY ILE VAL HIS LEU GLY GLY ILE SER VAL GLU LYS
SEQRES 7 A 267 PRO PHE GLU GLN ILE LEU GLN GLY ASN ILE ILE GLY LEU
SEQRES 8 A 267 TYR ASN LEU TYR GLU ALA ALA ARG ALA HIS GLY GLN PRO
SEQRES 9 A 267 ARG ILE VAL PHE ALA SER SER ASN HIS THR ILE GLY TYR
SEQRES 10 A 267 TYR PRO GLN THR GLU ARG LEU GLY PRO ASP VAL PRO ALA
SEQRES 11 A 267 ARG PRO ASP GLY LEU TYR GLY VAL SER LYS CYS PHE GLY
SEQRES 12 A 267 GLU ASN LEU ALA ARG MET TYR PHE ASP LYS PHE GLY GLN
SEQRES 13 A 267 GLU THR ALA LEU VAL ARG ILE GLY SER CYS THR PRO GLU
SEQRES 14 A 267 PRO ASN ASN TYR ARG MET LEU SER THR TRP PHE SER HIS
SEQRES 15 A 267 ASP ASP PHE VAL SER LEU ILE GLU ALA VAL PHE ARG ALA
SEQRES 16 A 267 PRO VAL LEU GLY CYS PRO VAL VAL TRP GLY ALA SER ALA
SEQRES 17 A 267 ASN ASP ALA GLY TRP TRP ASP ASN SER HIS LEU GLY PHE
SEQRES 18 A 267 LEU GLY TRP LYS PRO LYS ASP ASN ALA GLU ALA PHE ARG
SEQRES 19 A 267 ARG HIS ILE THR GLU THR THR PRO PRO PRO ASP PRO ASN
SEQRES 20 A 267 ASP ALA LEU VAL ARG PHE GLN GLY GLY THR PHE VAL ASP
SEQRES 21 A 267 ASN PRO ILE PHE LYS GLN SER
SEQRES 1 B 267 MET ALA MET LYS ARG LEU LEU VAL THR GLY ALA ALA GLY
SEQRES 2 B 267 GLN LEU GLY ARG VAL MET ARG GLU ARG LEU ALA PRO MET
SEQRES 3 B 267 ALA GLU ILE LEU ARG LEU ALA ASP LEU SER PRO LEU ASP
SEQRES 4 B 267 PRO ALA GLY PRO ASN GLU GLU CYS VAL GLN CYS ASP LEU
SEQRES 5 B 267 ALA ASP ALA ASN ALA VAL ASN ALA MET VAL ALA GLY CYS
SEQRES 6 B 267 ASP GLY ILE VAL HIS LEU GLY GLY ILE SER VAL GLU LYS
SEQRES 7 B 267 PRO PHE GLU GLN ILE LEU GLN GLY ASN ILE ILE GLY LEU
SEQRES 8 B 267 TYR ASN LEU TYR GLU ALA ALA ARG ALA HIS GLY GLN PRO
SEQRES 9 B 267 ARG ILE VAL PHE ALA SER SER ASN HIS THR ILE GLY TYR
SEQRES 10 B 267 TYR PRO GLN THR GLU ARG LEU GLY PRO ASP VAL PRO ALA
SEQRES 11 B 267 ARG PRO ASP GLY LEU TYR GLY VAL SER LYS CYS PHE GLY
SEQRES 12 B 267 GLU ASN LEU ALA ARG MET TYR PHE ASP LYS PHE GLY GLN
SEQRES 13 B 267 GLU THR ALA LEU VAL ARG ILE GLY SER CYS THR PRO GLU
SEQRES 14 B 267 PRO ASN ASN TYR ARG MET LEU SER THR TRP PHE SER HIS
SEQRES 15 B 267 ASP ASP PHE VAL SER LEU ILE GLU ALA VAL PHE ARG ALA
SEQRES 16 B 267 PRO VAL LEU GLY CYS PRO VAL VAL TRP GLY ALA SER ALA
SEQRES 17 B 267 ASN ASP ALA GLY TRP TRP ASP ASN SER HIS LEU GLY PHE
SEQRES 18 B 267 LEU GLY TRP LYS PRO LYS ASP ASN ALA GLU ALA PHE ARG
SEQRES 19 B 267 ARG HIS ILE THR GLU THR THR PRO PRO PRO ASP PRO ASN
SEQRES 20 B 267 ASP ALA LEU VAL ARG PHE GLN GLY GLY THR PHE VAL ASP
SEQRES 21 B 267 ASN PRO ILE PHE LYS GLN SER
SEQRES 1 C 267 MET ALA MET LYS ARG LEU LEU VAL THR GLY ALA ALA GLY
SEQRES 2 C 267 GLN LEU GLY ARG VAL MET ARG GLU ARG LEU ALA PRO MET
SEQRES 3 C 267 ALA GLU ILE LEU ARG LEU ALA ASP LEU SER PRO LEU ASP
SEQRES 4 C 267 PRO ALA GLY PRO ASN GLU GLU CYS VAL GLN CYS ASP LEU
SEQRES 5 C 267 ALA ASP ALA ASN ALA VAL ASN ALA MET VAL ALA GLY CYS
SEQRES 6 C 267 ASP GLY ILE VAL HIS LEU GLY GLY ILE SER VAL GLU LYS
SEQRES 7 C 267 PRO PHE GLU GLN ILE LEU GLN GLY ASN ILE ILE GLY LEU
SEQRES 8 C 267 TYR ASN LEU TYR GLU ALA ALA ARG ALA HIS GLY GLN PRO
SEQRES 9 C 267 ARG ILE VAL PHE ALA SER SER ASN HIS THR ILE GLY TYR
SEQRES 10 C 267 TYR PRO GLN THR GLU ARG LEU GLY PRO ASP VAL PRO ALA
SEQRES 11 C 267 ARG PRO ASP GLY LEU TYR GLY VAL SER LYS CYS PHE GLY
SEQRES 12 C 267 GLU ASN LEU ALA ARG MET TYR PHE ASP LYS PHE GLY GLN
SEQRES 13 C 267 GLU THR ALA LEU VAL ARG ILE GLY SER CYS THR PRO GLU
SEQRES 14 C 267 PRO ASN ASN TYR ARG MET LEU SER THR TRP PHE SER HIS
SEQRES 15 C 267 ASP ASP PHE VAL SER LEU ILE GLU ALA VAL PHE ARG ALA
SEQRES 16 C 267 PRO VAL LEU GLY CYS PRO VAL VAL TRP GLY ALA SER ALA
SEQRES 17 C 267 ASN ASP ALA GLY TRP TRP ASP ASN SER HIS LEU GLY PHE
SEQRES 18 C 267 LEU GLY TRP LYS PRO LYS ASP ASN ALA GLU ALA PHE ARG
SEQRES 19 C 267 ARG HIS ILE THR GLU THR THR PRO PRO PRO ASP PRO ASN
SEQRES 20 C 267 ASP ALA LEU VAL ARG PHE GLN GLY GLY THR PHE VAL ASP
SEQRES 21 C 267 ASN PRO ILE PHE LYS GLN SER
HET NAI A 400 44
HET 15L A 401 13
HET PO4 A 268 5
HET PO4 A 269 5
HET PO4 A 270 5
HET PO4 A 271 5
HET NAI B 400 44
HET 15L B 401 13
HET PO4 B 268 5
HET PO4 B 269 5
HET NAI C 400 44
HET 15L C 401 13
HET PO4 C 268 5
HET PO4 C 269 5
HETNAM NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
HETNAM 15L D-GALACTARO-1,5-LACTONE
HETNAM PO4 PHOSPHATE ION
HETSYN NAI NADH
HETSYN 15L GALACTARO-1,5-LACTONE; (2S,3R,4S,5R,6S)-3,4,5-
HETSYN 2 15L TRIHYDROXY-6-OXIDOTETRAHYDRO-2H-PYRAN-2-CARBOXYLATE
FORMUL 4 NAI 3(C21 H29 N7 O14 P2)
FORMUL 5 15L 3(C6 H8 O7)
FORMUL 6 PO4 8(O4 P 3-)
FORMUL 18 HOH *770(H2 O)
HELIX 1 1 GLY A 13 LEU A 23 1 11
HELIX 2 2 ASP A 54 ALA A 63 1 10
HELIX 3 3 PRO A 79 ILE A 88 1 10
HELIX 4 4 ILE A 88 HIS A 101 1 14
HELIX 5 5 HIS A 113 GLY A 116 5 4
HELIX 6 6 GLY A 134 GLY A 155 1 22
HELIX 7 7 ARG A 174 TRP A 179 1 6
HELIX 8 8 SER A 181 ALA A 195 1 15
HELIX 9 9 ASN A 216 GLY A 223 5 8
HELIX 10 10 ASN A 229 ALA A 232 5 4
HELIX 11 11 PHE A 233 GLU A 239 1 7
HELIX 12 12 ASP A 248 PHE A 253 1 6
HELIX 13 13 GLY A 255 ASN A 261 5 7
HELIX 14 14 GLY B 13 LEU B 23 1 11
HELIX 15 15 ASP B 54 ALA B 63 1 10
HELIX 16 16 PRO B 79 ILE B 88 1 10
HELIX 17 17 ILE B 88 HIS B 101 1 14
HELIX 18 18 HIS B 113 GLY B 116 5 4
HELIX 19 19 GLY B 134 GLY B 155 1 22
HELIX 20 20 ARG B 174 TRP B 179 1 6
HELIX 21 21 SER B 181 ALA B 195 1 15
HELIX 22 22 ASN B 216 GLY B 223 5 8
HELIX 23 23 ASN B 229 ALA B 232 5 4
HELIX 24 24 PHE B 233 THR B 241 1 9
HELIX 25 25 ASP B 248 ARG B 252 5 5
HELIX 26 26 GLY B 255 ASN B 261 5 7
HELIX 27 27 GLY C 13 LEU C 23 1 11
HELIX 28 28 ASP C 54 ALA C 63 1 10
HELIX 29 29 PRO C 79 ILE C 88 1 10
HELIX 30 30 ILE C 88 HIS C 101 1 14
HELIX 31 31 HIS C 113 GLY C 116 5 4
HELIX 32 32 GLY C 134 GLY C 155 1 22
HELIX 33 33 ARG C 174 TRP C 179 1 6
HELIX 34 34 SER C 181 ALA C 195 1 15
HELIX 35 35 ASN C 216 GLY C 223 5 8
HELIX 36 36 ASN C 229 ALA C 232 5 4
HELIX 37 37 PHE C 233 THR C 241 1 9
HELIX 38 38 ASP C 248 PHE C 253 1 6
HELIX 39 39 GLY C 255 ASN C 261 5 7
SHEET 1 A 7 GLU A 45 GLN A 49 0
SHEET 2 A 7 ALA A 27 ASP A 34 1 N LEU A 32 O GLU A 46
SHEET 3 A 7 MET A 3 THR A 9 1 N VAL A 8 O ARG A 31
SHEET 4 A 7 GLY A 67 HIS A 70 1 O VAL A 69 N LEU A 7
SHEET 5 A 7 ARG A 105 SER A 111 1 O VAL A 107 N ILE A 68
SHEET 6 A 7 THR A 158 ILE A 163 1 O ALA A 159 N ILE A 106
SHEET 7 A 7 VAL A 202 GLY A 205 1 O VAL A 203 N ARG A 162
SHEET 1 B 7 GLU B 45 GLN B 49 0
SHEET 2 B 7 ALA B 27 ASP B 34 1 N LEU B 32 O GLU B 46
SHEET 3 B 7 MET B 3 THR B 9 1 N VAL B 8 O ARG B 31
SHEET 4 B 7 GLY B 67 HIS B 70 1 O VAL B 69 N LEU B 7
SHEET 5 B 7 ARG B 105 SER B 111 1 O VAL B 107 N ILE B 68
SHEET 6 B 7 THR B 158 ILE B 163 1 O ALA B 159 N PHE B 108
SHEET 7 B 7 VAL B 202 GLY B 205 1 O VAL B 203 N ARG B 162
SHEET 1 C 7 GLU C 45 GLN C 49 0
SHEET 2 C 7 ALA C 27 ASP C 34 1 N LEU C 32 O GLU C 46
SHEET 3 C 7 MET C 3 THR C 9 1 N VAL C 8 O ARG C 31
SHEET 4 C 7 GLY C 67 HIS C 70 1 O VAL C 69 N LEU C 7
SHEET 5 C 7 ARG C 105 SER C 111 1 O VAL C 107 N ILE C 68
SHEET 6 C 7 THR C 158 ILE C 163 1 O ALA C 159 N ILE C 106
SHEET 7 C 7 VAL C 202 GLY C 205 1 O VAL C 203 N ARG C 162
CRYST1 165.390 165.390 173.630 90.00 90.00 120.00 P 62 2 2 36
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 0.006046 0.003491 0.000000 0.00000
SCALE2 0.000000 0.006982 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005759 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
