HEADER OXIDOREDUCTASE 12-APR-16 5JAM
TITLE YERSINIA PESTIS FABV VARIANT T276V
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ENR;
COMPND 5 EC: 1.3.1.9;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA PESTIS;
SOURCE 3 ORGANISM_TAXID: 632;
SOURCE 4 GENE: FABV, YPO4104, Y4119, YP_4011;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS FATTY ACID BIOSYNTHESIS FABV, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.PSCHIBUL,J.KUPER,M.HIRSCHBECK,C.KISKER
REVDAT 3 10-JAN-24 5JAM 1 REMARK
REVDAT 2 08-JUN-16 5JAM 1 JRNL
REVDAT 1 25-MAY-16 5JAM 0
JRNL AUTH C.NECKLES,A.PSCHIBUL,C.T.LAI,M.HIRSCHBECK,J.KUPER,S.DAVOODI,
JRNL AUTH 2 J.ZOU,N.LIU,P.PAN,S.SHAH,F.DARYAEE,G.R.BOMMINENI,C.LAI,
JRNL AUTH 3 C.SIMMERLING,C.KISKER,P.J.TONGE
JRNL TITL SELECTIVITY OF PYRIDONE- AND DIPHENYL ETHER-BASED INHIBITORS
JRNL TITL 2 FOR THE YERSINIA PESTIS FABV ENOYL-ACP REDUCTASE.
JRNL REF BIOCHEMISTRY V. 55 2992 2016
JRNL REFN ISSN 0006-2960
JRNL PMID 27136302
JRNL DOI 10.1021/ACS.BIOCHEM.5B01301
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 35384
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1772
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 44.5559 - 4.7011 1.00 2747 119 0.1686 0.2039
REMARK 3 2 4.7011 - 3.7320 1.00 2623 143 0.1477 0.1701
REMARK 3 3 3.7320 - 3.2604 1.00 2610 129 0.1870 0.1779
REMARK 3 4 3.2604 - 2.9624 1.00 2575 145 0.2019 0.2421
REMARK 3 5 2.9624 - 2.7501 1.00 2592 138 0.2199 0.2385
REMARK 3 6 2.7501 - 2.5880 1.00 2560 131 0.2117 0.2393
REMARK 3 7 2.5880 - 2.4584 1.00 2565 153 0.2283 0.2726
REMARK 3 8 2.4584 - 2.3514 1.00 2577 127 0.2304 0.2706
REMARK 3 9 2.3514 - 2.2609 1.00 2539 146 0.2426 0.2433
REMARK 3 10 2.2609 - 2.1828 1.00 2543 138 0.2587 0.3110
REMARK 3 11 2.1828 - 2.1146 1.00 2560 138 0.2851 0.2994
REMARK 3 12 2.1146 - 2.0541 1.00 2539 148 0.2971 0.3394
REMARK 3 13 2.0541 - 2.0001 1.00 2582 117 0.3230 0.3604
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.960
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.002 3535
REMARK 3 ANGLE : 0.590 4802
REMARK 3 CHIRALITY : 0.042 534
REMARK 3 PLANARITY : 0.003 646
REMARK 3 DIHEDRAL : 11.444 2127
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -5 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5410 -38.0397 0.9131
REMARK 3 T TENSOR
REMARK 3 T11: 0.1722 T22: 0.3397
REMARK 3 T33: 0.1364 T12: -0.0686
REMARK 3 T13: -0.0019 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 3.1709 L22: 2.2233
REMARK 3 L33: 3.0248 L12: 1.5998
REMARK 3 L13: 1.1729 L23: 0.1470
REMARK 3 S TENSOR
REMARK 3 S11: 0.0050 S12: 0.0541 S13: 0.0010
REMARK 3 S21: 0.0731 S22: -0.0526 S23: -0.0531
REMARK 3 S31: -0.1982 S32: 0.5063 S33: 0.0470
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5444 -29.2325 -10.3023
REMARK 3 T TENSOR
REMARK 3 T11: 0.3493 T22: 0.3629
REMARK 3 T33: 0.4070 T12: -0.0495
REMARK 3 T13: -0.0979 T23: 0.0726
REMARK 3 L TENSOR
REMARK 3 L11: 2.9634 L22: 0.6712
REMARK 3 L33: 2.7869 L12: 1.1591
REMARK 3 L13: 1.6383 L23: 0.2996
REMARK 3 S TENSOR
REMARK 3 S11: -0.4934 S12: 0.2434 S13: 0.6297
REMARK 3 S21: -0.1575 S22: -0.0451 S23: 0.3068
REMARK 3 S31: -0.6559 S32: -0.0687 S33: 0.2012
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 315 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5817 -38.1551 -17.1393
REMARK 3 T TENSOR
REMARK 3 T11: 0.2631 T22: 0.4992
REMARK 3 T33: 0.1955 T12: -0.1163
REMARK 3 T13: -0.0476 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 1.4062 L22: 2.6795
REMARK 3 L33: 1.1830 L12: 2.6198
REMARK 3 L13: 0.1706 L23: -0.2642
REMARK 3 S TENSOR
REMARK 3 S11: -0.2866 S12: 0.4035 S13: 0.1380
REMARK 3 S21: -0.2560 S22: 0.3215 S23: 0.4227
REMARK 3 S31: -0.0707 S32: 0.2919 S33: -0.0690
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 316 THROUGH 399 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9073 -48.1928 -9.1673
REMARK 3 T TENSOR
REMARK 3 T11: 0.2121 T22: 0.3547
REMARK 3 T33: 0.1635 T12: 0.0022
REMARK 3 T13: 0.0100 T23: -0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 2.7918 L22: 2.0677
REMARK 3 L33: 3.1340 L12: 1.4427
REMARK 3 L13: 1.2905 L23: 0.6341
REMARK 3 S TENSOR
REMARK 3 S11: -0.0396 S12: 0.3917 S13: -0.1946
REMARK 3 S21: -0.1497 S22: 0.1044 S23: 0.0178
REMARK 3 S31: 0.2418 S32: 0.2836 S33: -0.0111
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 5JAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220258.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6-5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35422
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 44.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.18000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.20
REMARK 200 R MERGE FOR SHELL (I) : 1.88500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4BKR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 MM (NH4)2SO4 25-38% PEG 4000 100
REMARK 280 MM MES PH 5.6-5.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -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 28.26467
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 56.52933
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 56.52933
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 28.26467
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 ARG A -6
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 OG1 THR A 224 HZ2 LYS A 244 1.57
REMARK 500 O2A NAI A 401 O HOH A 501 2.14
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 ASP A 210 42.05 -89.14
REMARK 500 GLU A 228 -154.59 -129.90
REMARK 500 HIS A 261 64.82 -101.43
REMARK 500 HIS A 261 56.87 -101.41
REMARK 500 HIS A 323 72.50 -115.93
REMARK 500 HIS A 323 68.46 -115.93
REMARK 500 ASP A 325 -166.85 -101.56
REMARK 500 ASP A 362 48.67 -101.26
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 NAI A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 404
DBREF 5JAM A 1 399 UNP Q8Z9U1 FABV_YERPE 1 399
SEQADV 5JAM ARG A -6 UNP Q8Z9U1 EXPRESSION TAG
SEQADV 5JAM GLY A -5 UNP Q8Z9U1 EXPRESSION TAG
SEQADV 5JAM SER A -4 UNP Q8Z9U1 EXPRESSION TAG
SEQADV 5JAM HIS A -3 UNP Q8Z9U1 EXPRESSION TAG
SEQADV 5JAM MET A -2 UNP Q8Z9U1 EXPRESSION TAG
SEQADV 5JAM LEU A -1 UNP Q8Z9U1 EXPRESSION TAG
SEQADV 5JAM GLU A 0 UNP Q8Z9U1 EXPRESSION TAG
SEQADV 5JAM VAL A 276 UNP Q8Z9U1 THR 276 ENGINEERED MUTATION
SEQRES 1 A 406 ARG GLY SER HIS MET LEU GLU MET ILE ILE LYS PRO ARG
SEQRES 2 A 406 VAL ARG GLY PHE ILE CYS VAL THR ALA HIS PRO THR GLY
SEQRES 3 A 406 CYS GLU ALA ASN VAL LYS LYS GLN ILE ASP TYR VAL THR
SEQRES 4 A 406 THR GLU GLY PRO ILE ALA ASN GLY PRO LYS ARG VAL LEU
SEQRES 5 A 406 VAL ILE GLY ALA SER THR GLY TYR GLY LEU ALA ALA ARG
SEQRES 6 A 406 ILE THR ALA ALA PHE GLY CYS GLY ALA ASP THR LEU GLY
SEQRES 7 A 406 VAL PHE PHE GLU ARG PRO GLY GLU GLU GLY LYS PRO GLY
SEQRES 8 A 406 THR SER GLY TRP TYR ASN SER ALA ALA PHE HIS LYS PHE
SEQRES 9 A 406 ALA ALA GLN LYS GLY LEU TYR ALA LYS SER ILE ASN GLY
SEQRES 10 A 406 ASP ALA PHE SER ASP GLU ILE LYS GLN LEU THR ILE ASP
SEQRES 11 A 406 ALA ILE LYS GLN ASP LEU GLY GLN VAL ASP GLN VAL ILE
SEQRES 12 A 406 TYR SER LEU ALA SER PRO ARG ARG THR HIS PRO LYS THR
SEQRES 13 A 406 GLY GLU VAL PHE ASN SER ALA LEU LYS PRO ILE GLY ASN
SEQRES 14 A 406 ALA VAL ASN LEU ARG GLY LEU ASP THR ASP LYS GLU VAL
SEQRES 15 A 406 ILE LYS GLU SER VAL LEU GLN PRO ALA THR GLN SER GLU
SEQRES 16 A 406 ILE ASP SER THR VAL ALA VAL MET GLY GLY GLU ASP TRP
SEQRES 17 A 406 GLN MET TRP ILE ASP ALA LEU LEU ASP ALA GLY VAL LEU
SEQRES 18 A 406 ALA GLU GLY ALA GLN THR THR ALA PHE THR TYR LEU GLY
SEQRES 19 A 406 GLU LYS ILE THR HIS ASP ILE TYR TRP ASN GLY SER ILE
SEQRES 20 A 406 GLY ALA ALA LYS LYS ASP LEU ASP GLN LYS VAL LEU ALA
SEQRES 21 A 406 ILE ARG GLU SER LEU ALA ALA HIS GLY GLY GLY ASP ALA
SEQRES 22 A 406 ARG VAL SER VAL LEU LYS ALA VAL VAL VAL GLN ALA SER
SEQRES 23 A 406 SER ALA ILE PRO MET MET PRO LEU TYR LEU SER LEU LEU
SEQRES 24 A 406 PHE LYS VAL MET LYS GLU LYS GLY THR HIS GLU GLY CYS
SEQRES 25 A 406 ILE GLU GLN VAL TYR SER LEU TYR LYS ASP SER LEU CYS
SEQRES 26 A 406 GLY ASP SER PRO HIS MET ASP GLN GLU GLY ARG LEU ARG
SEQRES 27 A 406 ALA ASP TYR LYS GLU LEU ASP PRO GLU VAL GLN ASN GLN
SEQRES 28 A 406 VAL GLN GLN LEU TRP ASP GLN VAL THR ASN ASP ASN ILE
SEQRES 29 A 406 TYR GLN LEU THR ASP PHE VAL GLY TYR LYS SER GLU PHE
SEQRES 30 A 406 LEU ASN LEU PHE GLY PHE GLY ILE ASP GLY VAL ASP TYR
SEQRES 31 A 406 ASP ALA ASP VAL ASN PRO ASP VAL LYS ILE PRO ASN LEU
SEQRES 32 A 406 ILE GLN GLY
HET NAI A 401 73
HET DMS A 402 10
HET DMS A 403 10
HET DMS A 404 10
HETNAM NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN NAI NADH
FORMUL 2 NAI C21 H29 N7 O14 P2
FORMUL 3 DMS 3(C2 H6 O S)
FORMUL 6 HOH *102(H2 O)
HELIX 1 AA1 GLY A -5 LEU A -1 5 5
HELIX 2 AA2 HIS A 16 GLY A 35 1 20
HELIX 3 AA3 THR A 51 GLY A 64 1 14
HELIX 4 AA4 THR A 85 LYS A 101 1 17
HELIX 5 AA5 SER A 114 LEU A 129 1 16
HELIX 6 AA6 THR A 185 GLY A 197 1 13
HELIX 7 AA7 GLY A 198 ASP A 210 1 13
HELIX 8 AA8 GLU A 228 TRP A 236 1 9
HELIX 9 AA9 GLY A 238 ALA A 260 1 23
HELIX 10 AB1 ALA A 278 ILE A 282 5 5
HELIX 11 AB2 PRO A 283 LYS A 299 1 17
HELIX 12 AB3 GLY A 304 SER A 316 1 13
HELIX 13 AB4 ASP A 338 ASP A 350 1 13
HELIX 14 AB5 ASN A 356 THR A 361 1 6
HELIX 15 AB6 ASP A 362 PHE A 374 1 13
SHEET 1 AA1 2 VAL A 7 ARG A 8 0
SHEET 2 AA1 2 ILE A 11 CYS A 12 -1 O ILE A 11 N ARG A 8
SHEET 1 AA2 8 ARG A 329 ARG A 331 0
SHEET 2 AA2 8 ASP A 265 VAL A 270 1 N VAL A 270 O LEU A 330
SHEET 3 AA2 8 LEU A 214 THR A 224 1 N ALA A 222 O SER A 269
SHEET 4 AA2 8 VAL A 132 TYR A 137 1 N ASP A 133 O GLN A 219
SHEET 5 AA2 8 ARG A 43 ILE A 47 1 N ILE A 47 O ILE A 136
SHEET 6 AA2 8 ASP A 68 PHE A 73 1 O LEU A 70 N VAL A 44
SHEET 7 AA2 8 ALA A 105 ASN A 109 1 O ILE A 108 N GLY A 71
SHEET 8 AA2 8 LEU A 396 GLN A 398 1 O ILE A 397 N SER A 107
SHEET 1 AA3 2 ARG A 143 THR A 145 0
SHEET 2 AA3 2 VAL A 152 ASN A 154 -1 O PHE A 153 N ARG A 144
SHEET 1 AA4 2 VAL A 164 ASP A 170 0
SHEET 2 AA4 2 VAL A 175 LEU A 181 -1 O LYS A 177 N GLY A 168
CISPEP 1 ALA A 211 GLY A 212 0 -3.56
CISPEP 2 ALA A 211 GLY A 212 0 -4.08
SITE 1 AC1 31 GLY A 48 ALA A 49 SER A 50 THR A 51
SITE 2 AC1 31 GLY A 52 TYR A 53 PHE A 73 PHE A 74
SITE 3 AC1 31 GLU A 75 GLY A 110 ASP A 111 ALA A 112
SITE 4 AC1 31 PHE A 113 SER A 138 LEU A 139 ALA A 140
SITE 5 AC1 31 SER A 141 PHE A 223 THR A 224 TYR A 225
SITE 6 AC1 31 LYS A 244 LEU A 271 LYS A 272 ALA A 273
SITE 7 AC1 31 VAL A 274 VAL A 276 DMS A 404 HOH A 501
SITE 8 AC1 31 HOH A 517 HOH A 571 HOH A 575
SITE 1 AC2 7 GLU A 79 GLU A 80 LYS A 106 ASP A 390
SITE 2 AC2 7 ASN A 395 ILE A 397 HOH A 595
SITE 1 AC3 2 GLY A 377 ASP A 379
SITE 1 AC4 4 TYR A 225 TYR A 235 MET A 285 NAI A 401
CRYST1 102.872 102.872 84.794 90.00 90.00 120.00 P 31 2 1 6
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 0.009721 0.005612 0.000000 0.00000
SCALE2 0.000000 0.011225 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011793 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
