HEADER OXIDOREDUCTASE 30-APR-06 2GUG
TITLE NAD-DEPENDENT FORMATE DEHYDROGENASE FROM PSEUDOMONAS SP.101 IN COMPLEX
TITLE 2 WITH FORMATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FORMATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: NAD-DEPENDENT FORMATE DEHYDROGENASE, FDH;
COMPND 5 EC: 1.2.1.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP.;
SOURCE 3 ORGANISM_TAXID: 33067;
SOURCE 4 STRAIN: 101;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPSFDH8A
KEYWDS OXIDOREDUCTASE (ALDEHUDE (D), NAD+(A)), OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.V.FILIPPOVA,K.M.POLYAKOV,T.V.TIKHONOVA,K.M.BOIKO,V.I.TISHKOV,
AUTHOR 2 V.O.POPOV
REVDAT 5 15-NOV-23 2GUG 1 REMARK
REVDAT 4 30-AUG-23 2GUG 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 2GUG 1 VERSN
REVDAT 2 24-FEB-09 2GUG 1 VERSN
REVDAT 1 16-MAY-06 2GUG 0
JRNL AUTH E.V.FILIPPOVA,K.M.POLYAKOV,T.V.TIKHONOVA,T.N.STEKHANOVA,
JRNL AUTH 2 K.M.BOIKO,I.G.SADIHOV,V.I.TISHKOV,N.LABROU,V.O.POPOV
JRNL TITL CRYSTAL STRUCTURE OF THE COMPLEX OF NAD-DEPENDENT FORMATE
JRNL TITL 2 DEHYDROGENASE FROM METYLOTROPHIC BACTERIUM PSEUDOMONAS
JRNL TITL 3 SP.101 WITH FORMATE.
JRNL REF KRISTALLOGRAFIYA V. 51 663 2006
JRNL REFN ISSN 0023-4761
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 69594
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 + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3696
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.28
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4880
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 244
REMARK 3 BIN FREE R VALUE : 0.3630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11504
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 77
REMARK 3 SOLVENT ATOMS : 389
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.56000
REMARK 3 B22 (A**2) : 4.58000
REMARK 3 B33 (A**2) : -1.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.341
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.261
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.194
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.933
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11883 ; 0.020 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16170 ; 1.862 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1462 ; 7.363 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 534 ;38.671 ;23.127
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1892 ;17.353 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 95 ;18.227 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1795 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9065 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6206 ; 0.234 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8069 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 695 ; 0.163 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 82 ; 0.305 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.242 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 7519 ; 1.052 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11854 ; 1.769 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4992 ; 2.729 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4316 ; 3.982 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GUG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037563.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
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 : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8019
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARHKL, DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73290
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
REMARK 200 RESOLUTION RANGE LOW (A) : 16.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04900
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: MOLREP
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2NAC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8% PEG400, 2M NA FORMATE, 0.1M
REMARK 280 HEPES, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 27.49000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 LEU A 257
REMARK 465 HIS A 258
REMARK 465 PRO A 259
REMARK 465 GLU A 260
REMARK 465 THR A 261
REMARK 465 GLU A 262
REMARK 465 GLY A 375
REMARK 465 THR A 376
REMARK 465 GLY A 377
REMARK 465 ALA A 378
REMARK 465 HIS A 379
REMARK 465 SER A 380
REMARK 465 TYR A 381
REMARK 465 SER A 382
REMARK 465 LYS A 383
REMARK 465 GLY A 384
REMARK 465 ASN A 385
REMARK 465 ALA A 386
REMARK 465 THR A 387
REMARK 465 GLY A 388
REMARK 465 GLY A 389
REMARK 465 SER A 390
REMARK 465 GLU A 391
REMARK 465 GLU A 392
REMARK 465 ALA A 393
REMARK 465 ALA A 394
REMARK 465 LYS A 395
REMARK 465 PHE A 396
REMARK 465 LYS A 397
REMARK 465 LYS A 398
REMARK 465 ALA A 399
REMARK 465 VAL A 400
REMARK 465 MET B 0
REMARK 465 GLY B 370
REMARK 465 GLY B 371
REMARK 465 ALA B 372
REMARK 465 LEU B 373
REMARK 465 ALA B 374
REMARK 465 GLY B 375
REMARK 465 THR B 376
REMARK 465 GLY B 377
REMARK 465 ALA B 378
REMARK 465 HIS B 379
REMARK 465 SER B 380
REMARK 465 TYR B 381
REMARK 465 SER B 382
REMARK 465 LYS B 383
REMARK 465 GLY B 384
REMARK 465 ASN B 385
REMARK 465 ALA B 386
REMARK 465 THR B 387
REMARK 465 GLY B 388
REMARK 465 GLY B 389
REMARK 465 SER B 390
REMARK 465 GLU B 391
REMARK 465 GLU B 392
REMARK 465 ALA B 393
REMARK 465 ALA B 394
REMARK 465 LYS B 395
REMARK 465 PHE B 396
REMARK 465 LYS B 397
REMARK 465 LYS B 398
REMARK 465 ALA B 399
REMARK 465 VAL B 400
REMARK 465 MET C 0
REMARK 465 GLY C 370
REMARK 465 GLY C 371
REMARK 465 ALA C 372
REMARK 465 LEU C 373
REMARK 465 ALA C 374
REMARK 465 GLY C 375
REMARK 465 THR C 376
REMARK 465 GLY C 377
REMARK 465 ALA C 378
REMARK 465 HIS C 379
REMARK 465 SER C 380
REMARK 465 TYR C 381
REMARK 465 SER C 382
REMARK 465 LYS C 383
REMARK 465 GLY C 384
REMARK 465 ASN C 385
REMARK 465 ALA C 386
REMARK 465 THR C 387
REMARK 465 GLY C 388
REMARK 465 GLY C 389
REMARK 465 SER C 390
REMARK 465 GLU C 391
REMARK 465 GLU C 392
REMARK 465 ALA C 393
REMARK 465 ALA C 394
REMARK 465 LYS C 395
REMARK 465 PHE C 396
REMARK 465 LYS C 397
REMARK 465 LYS C 398
REMARK 465 ALA C 399
REMARK 465 VAL C 400
REMARK 465 MET D 0
REMARK 465 LEU D 257
REMARK 465 HIS D 258
REMARK 465 PRO D 259
REMARK 465 GLU D 260
REMARK 465 THR D 261
REMARK 465 GLU D 262
REMARK 465 HIS D 263
REMARK 465 GLY D 370
REMARK 465 GLY D 371
REMARK 465 ALA D 372
REMARK 465 LEU D 373
REMARK 465 ALA D 374
REMARK 465 GLY D 375
REMARK 465 THR D 376
REMARK 465 GLY D 377
REMARK 465 ALA D 378
REMARK 465 HIS D 379
REMARK 465 SER D 380
REMARK 465 TYR D 381
REMARK 465 SER D 382
REMARK 465 LYS D 383
REMARK 465 GLY D 384
REMARK 465 ASN D 385
REMARK 465 ALA D 386
REMARK 465 THR D 387
REMARK 465 GLY D 388
REMARK 465 GLY D 389
REMARK 465 SER D 390
REMARK 465 GLU D 391
REMARK 465 GLU D 392
REMARK 465 ALA D 393
REMARK 465 ALA D 394
REMARK 465 LYS D 395
REMARK 465 PHE D 396
REMARK 465 LYS D 397
REMARK 465 LYS D 398
REMARK 465 ALA D 399
REMARK 465 VAL D 400
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG D 343 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 23 -178.77 -171.91
REMARK 500 PRO A 31 117.18 -39.68
REMARK 500 LEU A 57 21.01 45.75
REMARK 500 VAL A 88 -39.54 -36.80
REMARK 500 TRP A 99 72.64 -156.99
REMARK 500 SER A 124 21.46 -150.85
REMARK 500 TYR A 144 -10.33 70.09
REMARK 500 TRP A 177 -68.39 -145.68
REMARK 500 ALA A 191 -0.77 69.44
REMARK 500 ALA A 198 139.63 77.61
REMARK 500 GLU A 242 -33.32 -34.97
REMARK 500 CYS A 255 -58.04 5.14
REMARK 500 ALA A 283 -74.64 -91.43
REMARK 500 LYS A 317 -32.75 -29.47
REMARK 500 ILE A 333 -7.90 -149.18
REMARK 500 LEU B 57 19.34 49.79
REMARK 500 TRP B 99 68.02 -156.29
REMARK 500 LEU B 103 67.13 -103.68
REMARK 500 SER B 124 37.82 -150.77
REMARK 500 ASN B 146 17.80 -140.89
REMARK 500 TRP B 177 -68.12 -139.76
REMARK 500 ALA B 191 -1.19 62.81
REMARK 500 ALA B 198 126.82 76.99
REMARK 500 ARG B 224 160.17 -49.20
REMARK 500 ALA B 283 -82.93 -87.81
REMARK 500 PRO B 331 177.10 -58.54
REMARK 500 GLU C 56 18.91 57.80
REMARK 500 LEU C 57 19.14 55.78
REMARK 500 TRP C 99 69.41 -161.04
REMARK 500 LEU C 103 78.51 -105.42
REMARK 500 ALA C 111 71.46 -67.79
REMARK 500 SER C 124 28.99 -153.35
REMARK 500 TYR C 144 -2.81 65.02
REMARK 500 TRP C 177 -73.08 -142.68
REMARK 500 GLU C 190 126.25 -37.12
REMARK 500 ALA C 198 133.56 78.77
REMARK 500 PRO C 259 94.47 -58.90
REMARK 500 GLU C 260 -50.29 155.06
REMARK 500 ALA C 283 -81.74 -88.85
REMARK 500 ARG C 295 -71.31 -35.20
REMARK 500 LYS C 317 -39.65 -34.71
REMARK 500 ILE C 333 -4.21 -141.09
REMARK 500 ARG C 362 138.24 -36.95
REMARK 500 LEU D 57 19.01 50.32
REMARK 500 ASP D 75 91.69 -66.99
REMARK 500 TRP D 99 76.19 -162.29
REMARK 500 SER D 124 33.58 -163.24
REMARK 500 THR D 143 134.47 -33.96
REMARK 500 TYR D 144 -2.52 75.17
REMARK 500 TRP D 177 -68.52 -147.90
REMARK 500
REMARK 500 THIS ENTRY HAS 55 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 PG4 A 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 479
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 482
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG C 483
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NAC RELATED DB: PDB
REMARK 900 APO-FORM
REMARK 900 RELATED ID: 2NAD RELATED DB: PDB
REMARK 900 COMPLEX WITH NAD AND AZIDE
DBREF 2GUG A 0 400 UNP P33160 FDH_PSESR 0 400
DBREF 2GUG B 0 400 UNP P33160 FDH_PSESR 0 400
DBREF 2GUG C 0 400 UNP P33160 FDH_PSESR 0 400
DBREF 2GUG D 0 400 UNP P33160 FDH_PSESR 0 400
SEQADV 2GUG OCS A 354 UNP P33160 CYS 354 MODIFIED RESIDUE
SEQADV 2GUG OCS B 354 UNP P33160 CYS 354 MODIFIED RESIDUE
SEQADV 2GUG OCS C 354 UNP P33160 CYS 354 MODIFIED RESIDUE
SEQADV 2GUG OCS D 354 UNP P33160 CYS 354 MODIFIED RESIDUE
SEQRES 1 A 401 MET ALA LYS VAL LEU CYS VAL LEU TYR ASP ASP PRO VAL
SEQRES 2 A 401 ASP GLY TYR PRO LYS THR TYR ALA ARG ASP ASP LEU PRO
SEQRES 3 A 401 LYS ILE ASP HIS TYR PRO GLY GLY GLN THR LEU PRO THR
SEQRES 4 A 401 PRO LYS ALA ILE ASP PHE THR PRO GLY GLN LEU LEU GLY
SEQRES 5 A 401 SER VAL SER GLY GLU LEU GLY LEU ARG LYS TYR LEU GLU
SEQRES 6 A 401 SER ASN GLY HIS THR LEU VAL VAL THR SER ASP LYS ASP
SEQRES 7 A 401 GLY PRO ASP SER VAL PHE GLU ARG GLU LEU VAL ASP ALA
SEQRES 8 A 401 ASP VAL VAL ILE SER GLN PRO PHE TRP PRO ALA TYR LEU
SEQRES 9 A 401 THR PRO GLU ARG ILE ALA LYS ALA LYS ASN LEU LYS LEU
SEQRES 10 A 401 ALA LEU THR ALA GLY ILE GLY SER ASP HIS VAL ASP LEU
SEQRES 11 A 401 GLN SER ALA ILE ASP ARG ASN VAL THR VAL ALA GLU VAL
SEQRES 12 A 401 THR TYR CYS ASN SER ILE SER VAL ALA GLU HIS VAL VAL
SEQRES 13 A 401 MET MET ILE LEU SER LEU VAL ARG ASN TYR LEU PRO SER
SEQRES 14 A 401 HIS GLU TRP ALA ARG LYS GLY GLY TRP ASN ILE ALA ASP
SEQRES 15 A 401 CYS VAL SER HIS ALA TYR ASP LEU GLU ALA MET HIS VAL
SEQRES 16 A 401 GLY THR VAL ALA ALA GLY ARG ILE GLY LEU ALA VAL LEU
SEQRES 17 A 401 ARG ARG LEU ALA PRO PHE ASP VAL HIS LEU HIS TYR THR
SEQRES 18 A 401 ASP ARG HIS ARG LEU PRO GLU SER VAL GLU LYS GLU LEU
SEQRES 19 A 401 ASN LEU THR TRP HIS ALA THR ARG GLU ASP MET TYR PRO
SEQRES 20 A 401 VAL CYS ASP VAL VAL THR LEU ASN CYS PRO LEU HIS PRO
SEQRES 21 A 401 GLU THR GLU HIS MET ILE ASN ASP GLU THR LEU LYS LEU
SEQRES 22 A 401 PHE LYS ARG GLY ALA TYR ILE VAL ASN THR ALA ARG GLY
SEQRES 23 A 401 LYS LEU CYS ASP ARG ASP ALA VAL ALA ARG ALA LEU GLU
SEQRES 24 A 401 SER GLY ARG LEU ALA GLY TYR ALA GLY ASP VAL TRP PHE
SEQRES 25 A 401 PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG THR MET
SEQRES 26 A 401 PRO TYR ASN GLY MET THR PRO HIS ILE SER GLY THR THR
SEQRES 27 A 401 LEU THR ALA GLN ALA ARG TYR ALA ALA GLY THR ARG GLU
SEQRES 28 A 401 ILE LEU GLU OCS PHE PHE GLU GLY ARG PRO ILE ARG ASP
SEQRES 29 A 401 GLU TYR LEU ILE VAL GLN GLY GLY ALA LEU ALA GLY THR
SEQRES 30 A 401 GLY ALA HIS SER TYR SER LYS GLY ASN ALA THR GLY GLY
SEQRES 31 A 401 SER GLU GLU ALA ALA LYS PHE LYS LYS ALA VAL
SEQRES 1 B 401 MET ALA LYS VAL LEU CYS VAL LEU TYR ASP ASP PRO VAL
SEQRES 2 B 401 ASP GLY TYR PRO LYS THR TYR ALA ARG ASP ASP LEU PRO
SEQRES 3 B 401 LYS ILE ASP HIS TYR PRO GLY GLY GLN THR LEU PRO THR
SEQRES 4 B 401 PRO LYS ALA ILE ASP PHE THR PRO GLY GLN LEU LEU GLY
SEQRES 5 B 401 SER VAL SER GLY GLU LEU GLY LEU ARG LYS TYR LEU GLU
SEQRES 6 B 401 SER ASN GLY HIS THR LEU VAL VAL THR SER ASP LYS ASP
SEQRES 7 B 401 GLY PRO ASP SER VAL PHE GLU ARG GLU LEU VAL ASP ALA
SEQRES 8 B 401 ASP VAL VAL ILE SER GLN PRO PHE TRP PRO ALA TYR LEU
SEQRES 9 B 401 THR PRO GLU ARG ILE ALA LYS ALA LYS ASN LEU LYS LEU
SEQRES 10 B 401 ALA LEU THR ALA GLY ILE GLY SER ASP HIS VAL ASP LEU
SEQRES 11 B 401 GLN SER ALA ILE ASP ARG ASN VAL THR VAL ALA GLU VAL
SEQRES 12 B 401 THR TYR CYS ASN SER ILE SER VAL ALA GLU HIS VAL VAL
SEQRES 13 B 401 MET MET ILE LEU SER LEU VAL ARG ASN TYR LEU PRO SER
SEQRES 14 B 401 HIS GLU TRP ALA ARG LYS GLY GLY TRP ASN ILE ALA ASP
SEQRES 15 B 401 CYS VAL SER HIS ALA TYR ASP LEU GLU ALA MET HIS VAL
SEQRES 16 B 401 GLY THR VAL ALA ALA GLY ARG ILE GLY LEU ALA VAL LEU
SEQRES 17 B 401 ARG ARG LEU ALA PRO PHE ASP VAL HIS LEU HIS TYR THR
SEQRES 18 B 401 ASP ARG HIS ARG LEU PRO GLU SER VAL GLU LYS GLU LEU
SEQRES 19 B 401 ASN LEU THR TRP HIS ALA THR ARG GLU ASP MET TYR PRO
SEQRES 20 B 401 VAL CYS ASP VAL VAL THR LEU ASN CYS PRO LEU HIS PRO
SEQRES 21 B 401 GLU THR GLU HIS MET ILE ASN ASP GLU THR LEU LYS LEU
SEQRES 22 B 401 PHE LYS ARG GLY ALA TYR ILE VAL ASN THR ALA ARG GLY
SEQRES 23 B 401 LYS LEU CYS ASP ARG ASP ALA VAL ALA ARG ALA LEU GLU
SEQRES 24 B 401 SER GLY ARG LEU ALA GLY TYR ALA GLY ASP VAL TRP PHE
SEQRES 25 B 401 PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG THR MET
SEQRES 26 B 401 PRO TYR ASN GLY MET THR PRO HIS ILE SER GLY THR THR
SEQRES 27 B 401 LEU THR ALA GLN ALA ARG TYR ALA ALA GLY THR ARG GLU
SEQRES 28 B 401 ILE LEU GLU OCS PHE PHE GLU GLY ARG PRO ILE ARG ASP
SEQRES 29 B 401 GLU TYR LEU ILE VAL GLN GLY GLY ALA LEU ALA GLY THR
SEQRES 30 B 401 GLY ALA HIS SER TYR SER LYS GLY ASN ALA THR GLY GLY
SEQRES 31 B 401 SER GLU GLU ALA ALA LYS PHE LYS LYS ALA VAL
SEQRES 1 C 401 MET ALA LYS VAL LEU CYS VAL LEU TYR ASP ASP PRO VAL
SEQRES 2 C 401 ASP GLY TYR PRO LYS THR TYR ALA ARG ASP ASP LEU PRO
SEQRES 3 C 401 LYS ILE ASP HIS TYR PRO GLY GLY GLN THR LEU PRO THR
SEQRES 4 C 401 PRO LYS ALA ILE ASP PHE THR PRO GLY GLN LEU LEU GLY
SEQRES 5 C 401 SER VAL SER GLY GLU LEU GLY LEU ARG LYS TYR LEU GLU
SEQRES 6 C 401 SER ASN GLY HIS THR LEU VAL VAL THR SER ASP LYS ASP
SEQRES 7 C 401 GLY PRO ASP SER VAL PHE GLU ARG GLU LEU VAL ASP ALA
SEQRES 8 C 401 ASP VAL VAL ILE SER GLN PRO PHE TRP PRO ALA TYR LEU
SEQRES 9 C 401 THR PRO GLU ARG ILE ALA LYS ALA LYS ASN LEU LYS LEU
SEQRES 10 C 401 ALA LEU THR ALA GLY ILE GLY SER ASP HIS VAL ASP LEU
SEQRES 11 C 401 GLN SER ALA ILE ASP ARG ASN VAL THR VAL ALA GLU VAL
SEQRES 12 C 401 THR TYR CYS ASN SER ILE SER VAL ALA GLU HIS VAL VAL
SEQRES 13 C 401 MET MET ILE LEU SER LEU VAL ARG ASN TYR LEU PRO SER
SEQRES 14 C 401 HIS GLU TRP ALA ARG LYS GLY GLY TRP ASN ILE ALA ASP
SEQRES 15 C 401 CYS VAL SER HIS ALA TYR ASP LEU GLU ALA MET HIS VAL
SEQRES 16 C 401 GLY THR VAL ALA ALA GLY ARG ILE GLY LEU ALA VAL LEU
SEQRES 17 C 401 ARG ARG LEU ALA PRO PHE ASP VAL HIS LEU HIS TYR THR
SEQRES 18 C 401 ASP ARG HIS ARG LEU PRO GLU SER VAL GLU LYS GLU LEU
SEQRES 19 C 401 ASN LEU THR TRP HIS ALA THR ARG GLU ASP MET TYR PRO
SEQRES 20 C 401 VAL CYS ASP VAL VAL THR LEU ASN CYS PRO LEU HIS PRO
SEQRES 21 C 401 GLU THR GLU HIS MET ILE ASN ASP GLU THR LEU LYS LEU
SEQRES 22 C 401 PHE LYS ARG GLY ALA TYR ILE VAL ASN THR ALA ARG GLY
SEQRES 23 C 401 LYS LEU CYS ASP ARG ASP ALA VAL ALA ARG ALA LEU GLU
SEQRES 24 C 401 SER GLY ARG LEU ALA GLY TYR ALA GLY ASP VAL TRP PHE
SEQRES 25 C 401 PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG THR MET
SEQRES 26 C 401 PRO TYR ASN GLY MET THR PRO HIS ILE SER GLY THR THR
SEQRES 27 C 401 LEU THR ALA GLN ALA ARG TYR ALA ALA GLY THR ARG GLU
SEQRES 28 C 401 ILE LEU GLU OCS PHE PHE GLU GLY ARG PRO ILE ARG ASP
SEQRES 29 C 401 GLU TYR LEU ILE VAL GLN GLY GLY ALA LEU ALA GLY THR
SEQRES 30 C 401 GLY ALA HIS SER TYR SER LYS GLY ASN ALA THR GLY GLY
SEQRES 31 C 401 SER GLU GLU ALA ALA LYS PHE LYS LYS ALA VAL
SEQRES 1 D 401 MET ALA LYS VAL LEU CYS VAL LEU TYR ASP ASP PRO VAL
SEQRES 2 D 401 ASP GLY TYR PRO LYS THR TYR ALA ARG ASP ASP LEU PRO
SEQRES 3 D 401 LYS ILE ASP HIS TYR PRO GLY GLY GLN THR LEU PRO THR
SEQRES 4 D 401 PRO LYS ALA ILE ASP PHE THR PRO GLY GLN LEU LEU GLY
SEQRES 5 D 401 SER VAL SER GLY GLU LEU GLY LEU ARG LYS TYR LEU GLU
SEQRES 6 D 401 SER ASN GLY HIS THR LEU VAL VAL THR SER ASP LYS ASP
SEQRES 7 D 401 GLY PRO ASP SER VAL PHE GLU ARG GLU LEU VAL ASP ALA
SEQRES 8 D 401 ASP VAL VAL ILE SER GLN PRO PHE TRP PRO ALA TYR LEU
SEQRES 9 D 401 THR PRO GLU ARG ILE ALA LYS ALA LYS ASN LEU LYS LEU
SEQRES 10 D 401 ALA LEU THR ALA GLY ILE GLY SER ASP HIS VAL ASP LEU
SEQRES 11 D 401 GLN SER ALA ILE ASP ARG ASN VAL THR VAL ALA GLU VAL
SEQRES 12 D 401 THR TYR CYS ASN SER ILE SER VAL ALA GLU HIS VAL VAL
SEQRES 13 D 401 MET MET ILE LEU SER LEU VAL ARG ASN TYR LEU PRO SER
SEQRES 14 D 401 HIS GLU TRP ALA ARG LYS GLY GLY TRP ASN ILE ALA ASP
SEQRES 15 D 401 CYS VAL SER HIS ALA TYR ASP LEU GLU ALA MET HIS VAL
SEQRES 16 D 401 GLY THR VAL ALA ALA GLY ARG ILE GLY LEU ALA VAL LEU
SEQRES 17 D 401 ARG ARG LEU ALA PRO PHE ASP VAL HIS LEU HIS TYR THR
SEQRES 18 D 401 ASP ARG HIS ARG LEU PRO GLU SER VAL GLU LYS GLU LEU
SEQRES 19 D 401 ASN LEU THR TRP HIS ALA THR ARG GLU ASP MET TYR PRO
SEQRES 20 D 401 VAL CYS ASP VAL VAL THR LEU ASN CYS PRO LEU HIS PRO
SEQRES 21 D 401 GLU THR GLU HIS MET ILE ASN ASP GLU THR LEU LYS LEU
SEQRES 22 D 401 PHE LYS ARG GLY ALA TYR ILE VAL ASN THR ALA ARG GLY
SEQRES 23 D 401 LYS LEU CYS ASP ARG ASP ALA VAL ALA ARG ALA LEU GLU
SEQRES 24 D 401 SER GLY ARG LEU ALA GLY TYR ALA GLY ASP VAL TRP PHE
SEQRES 25 D 401 PRO GLN PRO ALA PRO LYS ASP HIS PRO TRP ARG THR MET
SEQRES 26 D 401 PRO TYR ASN GLY MET THR PRO HIS ILE SER GLY THR THR
SEQRES 27 D 401 LEU THR ALA GLN ALA ARG TYR ALA ALA GLY THR ARG GLU
SEQRES 28 D 401 ILE LEU GLU OCS PHE PHE GLU GLY ARG PRO ILE ARG ASP
SEQRES 29 D 401 GLU TYR LEU ILE VAL GLN GLY GLY ALA LEU ALA GLY THR
SEQRES 30 D 401 GLY ALA HIS SER TYR SER LYS GLY ASN ALA THR GLY GLY
SEQRES 31 D 401 SER GLU GLU ALA ALA LYS PHE LYS LYS ALA VAL
MODRES 2GUG OCS A 354 CYS CYSTEINESULFONIC ACID
MODRES 2GUG OCS B 354 CYS CYSTEINESULFONIC ACID
MODRES 2GUG OCS C 354 CYS CYSTEINESULFONIC ACID
MODRES 2GUG OCS D 354 CYS CYSTEINESULFONIC ACID
HET OCS A 354 9
HET OCS B 354 9
HET OCS C 354 9
HET OCS D 354 9
HET PG4 A 478 13
HET FMT A 479 3
HET PEG A 476 7
HET PEG A 477 7
HET PEG A 480 7
HET FMT B 401 3
HET PEG B 481 7
HET FMT C 401 3
HET PEG C 482 7
HET PEG C 483 7
HET PG4 D 480 13
HETNAM OCS CYSTEINESULFONIC ACID
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM FMT FORMIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 1 OCS 4(C3 H7 N O5 S)
FORMUL 5 PG4 2(C8 H18 O5)
FORMUL 6 FMT 3(C H2 O2)
FORMUL 7 PEG 6(C4 H10 O3)
FORMUL 16 HOH *389(H2 O)
HELIX 1 1 GLY A 55 GLY A 58 5 4
HELIX 2 2 LEU A 59 ASN A 66 1 8
HELIX 3 3 SER A 81 VAL A 88 1 8
HELIX 4 4 THR A 104 ALA A 111 1 8
HELIX 5 5 ASP A 128 ARG A 135 1 8
HELIX 6 6 ASN A 146 ASN A 164 1 19
HELIX 7 7 ASN A 164 LYS A 174 1 11
HELIX 8 8 ASN A 178 SER A 184 1 7
HELIX 9 9 GLY A 200 ALA A 211 1 12
HELIX 10 10 PRO A 212 ASP A 214 5 3
HELIX 11 11 PRO A 226 LEU A 233 1 8
HELIX 12 12 THR A 240 TYR A 245 1 6
HELIX 13 13 PRO A 246 CYS A 248 5 3
HELIX 14 14 GLU A 268 PHE A 273 5 6
HELIX 15 15 ARG A 284 CYS A 288 5 5
HELIX 16 16 ASP A 289 SER A 299 1 11
HELIX 17 17 HIS A 319 THR A 323 5 5
HELIX 18 18 THR A 337 GLU A 357 1 21
HELIX 19 19 ARG A 362 GLU A 364 5 3
HELIX 20 20 SER B 52 GLY B 58 5 7
HELIX 21 21 LEU B 59 SER B 65 1 7
HELIX 22 22 SER B 81 VAL B 88 1 8
HELIX 23 23 THR B 104 ALA B 111 1 8
HELIX 24 24 ASP B 128 ARG B 135 1 8
HELIX 25 25 ASN B 146 ARG B 163 1 18
HELIX 26 26 ASN B 164 LYS B 174 1 11
HELIX 27 27 ASN B 178 SER B 184 1 7
HELIX 28 28 GLY B 200 ALA B 211 1 12
HELIX 29 29 PRO B 212 ASP B 214 5 3
HELIX 30 30 PRO B 226 ASN B 234 1 9
HELIX 31 31 THR B 240 TYR B 245 1 6
HELIX 32 32 PRO B 246 CYS B 248 5 3
HELIX 33 33 ASN B 266 LYS B 271 1 6
HELIX 34 34 ARG B 284 CYS B 288 5 5
HELIX 35 35 ASP B 289 GLY B 300 1 12
HELIX 36 36 HIS B 319 THR B 323 5 5
HELIX 37 37 THR B 337 GLY B 358 1 22
HELIX 38 38 GLY C 55 GLY C 58 5 4
HELIX 39 39 LEU C 59 ASN C 66 1 8
HELIX 40 40 SER C 81 VAL C 88 1 8
HELIX 41 41 THR C 104 ALA C 111 1 8
HELIX 42 42 ASP C 128 ARG C 135 1 8
HELIX 43 43 ASN C 146 ARG C 163 1 18
HELIX 44 44 ASN C 164 LYS C 174 1 11
HELIX 45 45 ASN C 178 SER C 184 1 7
HELIX 46 46 GLY C 200 ALA C 211 1 12
HELIX 47 47 PRO C 212 ASP C 214 5 3
HELIX 48 48 PRO C 226 ASN C 234 1 9
HELIX 49 49 THR C 240 TYR C 245 1 6
HELIX 50 50 PRO C 246 CYS C 248 5 3
HELIX 51 51 GLU C 268 PHE C 273 5 6
HELIX 52 52 ARG C 284 CYS C 288 5 5
HELIX 53 53 ASP C 289 SER C 299 1 11
HELIX 54 54 THR C 337 GLU C 357 1 21
HELIX 55 55 GLY D 55 GLY D 58 5 4
HELIX 56 56 LEU D 59 SER D 65 1 7
HELIX 57 57 SER D 81 VAL D 88 1 8
HELIX 58 58 THR D 104 ALA D 111 1 8
HELIX 59 59 ASP D 128 ARG D 135 1 8
HELIX 60 60 ASN D 146 ASN D 164 1 19
HELIX 61 61 ASN D 164 LYS D 174 1 11
HELIX 62 62 ASN D 178 SER D 184 1 7
HELIX 63 63 GLY D 200 ALA D 211 1 12
HELIX 64 64 PRO D 212 ASP D 214 5 3
HELIX 65 65 PRO D 226 LEU D 233 1 8
HELIX 66 66 THR D 240 TYR D 245 1 6
HELIX 67 67 PRO D 246 CYS D 248 5 3
HELIX 68 68 ASN D 266 LYS D 271 1 6
HELIX 69 69 ARG D 284 CYS D 288 5 5
HELIX 70 70 ASP D 289 GLY D 300 1 12
HELIX 71 71 HIS D 319 THR D 323 5 5
HELIX 72 72 THR D 337 GLU D 357 1 21
HELIX 73 73 ARG D 362 GLU D 364 5 3
SHEET 1 A 7 THR A 69 THR A 73 0
SHEET 2 A 7 LYS A 2 VAL A 6 1 N CYS A 5 O VAL A 71
SHEET 3 A 7 VAL A 92 SER A 95 1 O VAL A 92 N LEU A 4
SHEET 4 A 7 LEU A 116 THR A 119 1 O LEU A 118 N VAL A 93
SHEET 5 A 7 THR A 138 GLU A 141 1 O ALA A 140 N THR A 119
SHEET 6 A 7 LEU A 366 GLN A 369 -1 O ILE A 367 N VAL A 139
SHEET 7 A 7 ALA A 372 LEU A 373 -1 O ALA A 372 N GLN A 369
SHEET 1 B 6 THR A 236 HIS A 238 0
SHEET 2 B 6 HIS A 216 THR A 220 1 N LEU A 217 O THR A 236
SHEET 3 B 6 HIS A 193 VAL A 197 1 N VAL A 194 O HIS A 218
SHEET 4 B 6 VAL A 250 LEU A 253 1 O VAL A 250 N GLY A 195
SHEET 5 B 6 ALA A 277 ASN A 281 1 O TYR A 278 N VAL A 251
SHEET 6 B 6 LEU A 302 GLY A 307 1 O ALA A 306 N ASN A 281
SHEET 1 C 6 THR B 69 THR B 73 0
SHEET 2 C 6 LYS B 2 VAL B 6 1 N CYS B 5 O VAL B 71
SHEET 3 C 6 VAL B 92 SER B 95 1 O ILE B 94 N VAL B 6
SHEET 4 C 6 LEU B 116 THR B 119 1 O LEU B 118 N VAL B 93
SHEET 5 C 6 THR B 138 GLU B 141 1 O THR B 138 N ALA B 117
SHEET 6 C 6 LEU B 366 VAL B 368 -1 O VAL B 368 N VAL B 139
SHEET 1 D 6 THR B 236 TRP B 237 0
SHEET 2 D 6 HIS B 216 THR B 220 1 N LEU B 217 O THR B 236
SHEET 3 D 6 HIS B 193 VAL B 197 1 N VAL B 194 O HIS B 218
SHEET 4 D 6 VAL B 250 LEU B 253 1 O VAL B 250 N GLY B 195
SHEET 5 D 6 TYR B 278 ASN B 281 1 O VAL B 280 N LEU B 253
SHEET 6 D 6 GLY B 304 ALA B 306 1 O ALA B 306 N ASN B 281
SHEET 1 E 6 THR C 69 THR C 73 0
SHEET 2 E 6 LYS C 2 VAL C 6 1 N VAL C 3 O VAL C 71
SHEET 3 E 6 VAL C 92 SER C 95 1 O ILE C 94 N VAL C 6
SHEET 4 E 6 LEU C 116 THR C 119 1 O LEU C 118 N VAL C 93
SHEET 5 E 6 THR C 138 GLU C 141 1 O THR C 138 N ALA C 117
SHEET 6 E 6 LEU C 366 VAL C 368 -1 O ILE C 367 N VAL C 139
SHEET 1 F 6 THR C 236 TRP C 237 0
SHEET 2 F 6 HIS C 216 THR C 220 1 N TYR C 219 O THR C 236
SHEET 3 F 6 HIS C 193 VAL C 197 1 N VAL C 194 O HIS C 218
SHEET 4 F 6 VAL C 250 LEU C 253 1 O VAL C 250 N GLY C 195
SHEET 5 F 6 ALA C 277 ASN C 281 1 O VAL C 280 N VAL C 251
SHEET 6 F 6 LEU C 302 GLY C 307 1 O ALA C 306 N ASN C 281
SHEET 1 G 6 THR D 69 THR D 73 0
SHEET 2 G 6 LYS D 2 VAL D 6 1 N CYS D 5 O VAL D 71
SHEET 3 G 6 VAL D 92 SER D 95 1 O ILE D 94 N LEU D 4
SHEET 4 G 6 LEU D 116 THR D 119 1 O LEU D 118 N VAL D 93
SHEET 5 G 6 THR D 138 GLU D 141 1 O ALA D 140 N THR D 119
SHEET 6 G 6 LEU D 366 VAL D 368 -1 O VAL D 368 N VAL D 139
SHEET 1 H 6 THR D 236 TRP D 237 0
SHEET 2 H 6 HIS D 216 THR D 220 1 N TYR D 219 O THR D 236
SHEET 3 H 6 HIS D 193 VAL D 197 1 N VAL D 194 O HIS D 216
SHEET 4 H 6 VAL D 250 LEU D 253 1 O VAL D 250 N GLY D 195
SHEET 5 H 6 ALA D 277 ASN D 281 1 O TYR D 278 N VAL D 251
SHEET 6 H 6 LEU D 302 GLY D 307 1 O ALA D 306 N ASN D 281
LINK C GLU A 353 N OCS A 354 1555 1555 1.32
LINK C OCS A 354 N PHE A 355 1555 1555 1.32
LINK C GLU B 353 N OCS B 354 1555 1555 1.31
LINK C OCS B 354 N PHE B 355 1555 1555 1.33
LINK C GLU C 353 N OCS C 354 1555 1555 1.33
LINK C OCS C 354 N PHE C 355 1555 1555 1.34
LINK C GLU D 353 N OCS D 354 1555 1555 1.34
LINK C OCS D 354 N PHE D 355 1555 1555 1.33
CISPEP 1 HIS A 263 MET A 264 0 15.83
CISPEP 2 PHE A 311 PRO A 312 0 -3.82
CISPEP 3 GLN A 313 PRO A 314 0 -2.58
CISPEP 4 PHE B 311 PRO B 312 0 2.35
CISPEP 5 GLN B 313 PRO B 314 0 -3.86
CISPEP 6 PHE C 311 PRO C 312 0 -9.72
CISPEP 7 GLN C 313 PRO C 314 0 -5.50
CISPEP 8 PHE D 311 PRO D 312 0 -16.33
CISPEP 9 GLN D 313 PRO D 314 0 4.02
SITE 1 AC1 6 SER A 184 PEG A 480 HOH A 526 ASP C 13
SITE 2 AC1 6 THR C 18 TYR C 19
SITE 1 AC2 6 THR B 18 SER D 184 HIS D 185 GLU D 298
SITE 2 AC2 6 TYR D 326 HOH D 550
SITE 1 AC3 7 PRO A 97 PHE A 98 GLY A 121 ILE A 122
SITE 2 AC3 7 ASN A 146 PEG A 476 HOH A 587
SITE 1 AC4 5 PRO B 97 PHE B 98 ILE B 122 ASN B 146
SITE 2 AC4 5 HOH B 499
SITE 1 AC5 6 PRO C 97 PHE C 98 GLY C 121 ILE C 122
SITE 2 AC5 6 ASN C 146 HOH C 531
SITE 1 AC6 8 ILE A 122 ASN A 146 SER A 147 VAL A 150
SITE 2 AC6 8 ILE A 202 THR A 282 FMT A 479 HOH A 554
SITE 1 AC7 8 PRO A 31 TYR A 144 ARG A 201 ALA A 205
SITE 2 AC7 8 ARG A 208 ARG A 209 GLU C 190 ASP C 214
SITE 1 AC8 3 GLU A 298 TYR A 326 PG4 A 478
SITE 1 AC9 1 LEU B 204
SITE 1 BC1 2 ALA C 199 GLY C 200
SITE 1 BC2 2 GLU C 298 TYR C 326
CRYST1 117.000 54.980 128.910 90.00 95.74 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 0.008547 0.000000 0.000859 0.00000
SCALE2 0.000000 0.018188 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007796 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
