HEADER OXIDOREDUCTASE 20-APR-00 1EVJ
TITLE CRYSTAL STRUCTURE OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE (GFOR) DELTA1-22
TITLE 2 S64D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE-FRUCTOSE OXIDOREDUCTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GFOR;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZYMOMONAS MOBILIS;
SOURCE 3 ORGANISM_TAXID: 542;
SOURCE 4 EXPRESSION_SYSTEM: ZYMOMONAS MOBILIS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 542;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PZY470
KEYWDS NADP/NAD BINDING, OSMOTIC PROTECTION, PERIPLASM, OLIGOMERIZATION
KEYWDS 2 STATE, N-TERMINAL ARM, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.LOTT,D.HALBIG,H.M.BAKER,M.J.HARDMAN,G.A.SPRENGER,E.N.BAKER
REVDAT 4 07-FEB-24 1EVJ 1 REMARK
REVDAT 3 03-NOV-21 1EVJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1EVJ 1 VERSN
REVDAT 1 04-DEC-00 1EVJ 0
JRNL AUTH J.S.LOTT,D.HALBIG,H.M.BAKER,M.J.HARDMAN,G.A.SPRENGER,
JRNL AUTH 2 E.N.BAKER
JRNL TITL CRYSTAL STRUCTURE OF A TRUNCATED MUTANT OF GLUCOSE-FRUCTOSE
JRNL TITL 2 OXIDOREDUCTASE SHOWS THAT AN N-TERMINAL ARM CONTROLS
JRNL TITL 3 TETRAMER FORMATION.
JRNL REF J.MOL.BIOL. V. 304 575 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11099381
JRNL DOI 10.1006/JMBI.2000.4245
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1832235.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 38846
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3897
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.80
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3392
REMARK 3 BIN R VALUE (WORKING SET) : 0.3350
REMARK 3 BIN FREE R VALUE : 0.3870
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 388
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10303
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 176
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 55.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 17.85000
REMARK 3 B22 (A**2) : -19.14000
REMARK 3 B33 (A**2) : 1.30000
REMARK 3 B12 (A**2) : -3.68000
REMARK 3 B13 (A**2) : 5.24000
REMARK 3 B23 (A**2) : 3.53000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.43
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.46
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.52
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 64.78
REMARK 3
REMARK 3 NCS MODEL : RESTRAINED
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; 1000
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; 2
REMARK 3 GROUP 2 POSITIONAL (A) : NULL ; 1000
REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; 2
REMARK 3 GROUP 3 POSITIONAL (A) : NULL ; 1000
REMARK 3 GROUP 3 B-FACTOR (A**2) : NULL ; 2
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 USED SLOWCOOL SIMULATED ANNEALING WITH TORSION-ANGLE MOLECULAR
REMARK 3 DYNAMICS, USING A MAXIMUM-LIKELIHOOD
REMARK 3 TARGET FUNCTION (MLF)
REMARK 4
REMARK 4 1EVJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010928.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-SEP-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38847
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.06
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M ACETATE/KOH, 8.6% PEG6000, PH
REMARK 280 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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
REMARK 350 TOTAL BURIED SURFACE AREA: 5210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24750 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
REMARK 350 TOTAL BURIED SURFACE AREA: 5180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 GLY A 307
REMARK 465 HIS A 308
REMARK 465 ALA A 309
REMARK 465 ASN A 310
REMARK 465 GLN A 311
REMARK 465 SER A 312
REMARK 465 MET A 313
REMARK 465 MET A 314
REMARK 465 PRO A 315
REMARK 465 GLN A 316
REMARK 465 PHE A 317
REMARK 465 ILE A 318
REMARK 465 PRO B 306
REMARK 465 GLY B 307
REMARK 465 HIS B 308
REMARK 465 ALA B 309
REMARK 465 ASN B 310
REMARK 465 GLN B 311
REMARK 465 SER B 312
REMARK 465 MET B 313
REMARK 465 MET B 314
REMARK 465 PRO B 315
REMARK 465 GLN B 316
REMARK 465 PHE B 317
REMARK 465 ILE B 318
REMARK 465 MET B 319
REMARK 465 PRO C 306
REMARK 465 GLY C 307
REMARK 465 HIS C 308
REMARK 465 ALA C 309
REMARK 465 ASN C 310
REMARK 465 GLN C 311
REMARK 465 SER C 312
REMARK 465 MET C 313
REMARK 465 MET C 314
REMARK 465 PRO C 315
REMARK 465 GLN C 316
REMARK 465 PHE C 317
REMARK 465 ILE C 318
REMARK 465 MET C 319
REMARK 465 PRO C 320
REMARK 465 HIS D 308
REMARK 465 ALA D 309
REMARK 465 ASN D 310
REMARK 465 GLN D 311
REMARK 465 SER D 312
REMARK 465 MET D 313
REMARK 465 MET D 314
REMARK 465 PRO D 315
REMARK 465 GLN D 316
REMARK 465 PHE D 317
REMARK 465 ILE D 318
REMARK 465 MET D 319
REMARK 465 PRO D 320
REMARK 465 ALA D 321
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 30 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 31 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 55 CG CD OE1 NE2
REMARK 470 GLU A 68 CG CD OE1 OE2
REMARK 470 LYS A 69 CG CD CE NZ
REMARK 470 LYS A 71 CG CD CE NZ
REMARK 470 ARG A 82 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 92 CG CD CE NZ
REMARK 470 LYS A 95 CG CD CE NZ
REMARK 470 ASP A 194 CG OD1 OD2
REMARK 470 GLN A 197 CG CD OE1 NE2
REMARK 470 ARG A 202 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 203 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 339 CG OD1 ND2
REMARK 470 GLN A 357 CG CD OE1 NE2
REMARK 470 ARG A 367 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 378 CG CD OE1 NE2
REMARK 470 ARG B 30 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 55 CG CD OE1 NE2
REMARK 470 GLU B 68 CG CD OE1 OE2
REMARK 470 LYS B 69 CG CD CE NZ
REMARK 470 LYS B 71 CG CD CE NZ
REMARK 470 ARG B 82 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 92 CG CD CE NZ
REMARK 470 LYS B 95 CG CD CE NZ
REMARK 470 LYS B 98 CG CD CE NZ
REMARK 470 LYS B 150 CG CD CE NZ
REMARK 470 ASP B 194 CG OD1 OD2
REMARK 470 GLN B 197 CG CD OE1 NE2
REMARK 470 ARG B 203 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 339 CG OD1 ND2
REMARK 470 LYS B 340 CG CD CE NZ
REMARK 470 GLN B 357 CG CD OE1 NE2
REMARK 470 ARG C 30 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 55 CG CD OE1 NE2
REMARK 470 LYS C 69 CG CD CE NZ
REMARK 470 LYS C 71 CG CD CE NZ
REMARK 470 ARG C 82 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 92 CG CD CE NZ
REMARK 470 LYS C 95 CG CD CE NZ
REMARK 470 LYS C 98 CG CD CE NZ
REMARK 470 ASP C 194 CG OD1 OD2
REMARK 470 ARG C 202 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 203 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 339 CG OD1 ND2
REMARK 470 ARG C 367 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 30 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 31 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 55 CG CD OE1 NE2
REMARK 470 LYS D 71 CG CD CE NZ
REMARK 470 ARG D 82 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 92 CG CD CE NZ
REMARK 470 LYS D 95 CG CD CE NZ
REMARK 470 LYS D 98 CG CD CE NZ
REMARK 470 LYS D 150 CG CD CE NZ
REMARK 470 ASP D 194 CG OD1 OD2
REMARK 470 GLN D 197 CG CD OE1 NE2
REMARK 470 ARG D 202 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 203 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 339 CG OD1 ND2
REMARK 470 LYS D 340 CG CD CE NZ
REMARK 470 GLN D 357 CG CD OE1 NE2
REMARK 470 ARG D 367 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 378 CG CD OE1 NE2
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 A 58 CD - NE - CZ ANGL. DEV. = 21.2 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH1 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG B 58 CD - NE - CZ ANGL. DEV. = 20.9 DEGREES
REMARK 500 ARG B 58 NE - CZ - NH1 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ARG B 58 NE - CZ - NH2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG C 58 CD - NE - CZ ANGL. DEV. = 21.0 DEGREES
REMARK 500 ARG C 58 NE - CZ - NH1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG C 58 NE - CZ - NH2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 ARG D 58 CD - NE - CZ ANGL. DEV. = 20.9 DEGREES
REMARK 500 ARG D 58 NE - CZ - NH1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG D 58 NE - CZ - NH2 ANGL. DEV. = -10.7 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 HIS A 56 -37.32 -158.07
REMARK 500 ASP A 64 148.85 -178.28
REMARK 500 ASN A 66 104.71 -161.61
REMARK 500 PRO A 81 -2.17 -52.77
REMARK 500 ILE A 105 51.18 -144.63
REMARK 500 PRO A 107 153.05 -49.64
REMARK 500 ALA A 147 -72.91 -50.90
REMARK 500 ALA A 148 -4.67 -54.31
REMARK 500 ASN A 193 97.85 -38.41
REMARK 500 ASP A 194 86.78 35.88
REMARK 500 PHE A 246 52.60 -104.88
REMARK 500 THR A 274 171.81 -59.62
REMARK 500 THR A 275 112.52 -38.77
REMARK 500 GLN A 298 93.98 2.72
REMARK 500 PRO A 320 105.92 -19.81
REMARK 500 ALA A 321 37.79 28.59
REMARK 500 ASN A 322 52.16 -145.28
REMARK 500 ILE A 337 -2.15 -55.19
REMARK 500 ASN A 338 10.46 -141.22
REMARK 500 ASN A 339 9.24 54.45
REMARK 500 SER A 344 77.48 -116.18
REMARK 500 ARG B 31 -20.14 -146.91
REMARK 500 HIS B 56 -37.43 -158.02
REMARK 500 ASP B 64 148.67 -178.09
REMARK 500 ASN B 66 107.96 -161.73
REMARK 500 PRO B 81 -1.89 -52.53
REMARK 500 ILE B 105 52.05 -144.10
REMARK 500 PRO B 107 152.53 -49.32
REMARK 500 ALA B 147 -72.93 -50.57
REMARK 500 ALA B 148 -8.32 -55.16
REMARK 500 ASP B 188 135.95 -170.54
REMARK 500 ASN B 193 97.85 -38.31
REMARK 500 ASP B 194 86.89 35.78
REMARK 500 PRO B 195 -0.56 -49.93
REMARK 500 PHE B 246 52.34 -104.38
REMARK 500 THR B 274 171.33 -59.01
REMARK 500 THR B 275 112.64 -38.08
REMARK 500 GLN B 298 95.30 3.02
REMARK 500 ALA B 321 92.65 165.82
REMARK 500 ILE B 337 -2.56 -54.90
REMARK 500 ASN B 339 17.35 46.36
REMARK 500 PRO B 341 171.10 -57.83
REMARK 500 SER B 344 77.20 -116.37
REMARK 500 ARG B 377 89.53 -66.37
REMARK 500 GLN B 378 108.38 -58.15
REMARK 500 HIS C 56 -37.39 -157.93
REMARK 500 ASP C 64 149.06 -178.46
REMARK 500 ASN C 66 98.53 -161.88
REMARK 500 PRO C 81 -2.04 -52.64
REMARK 500 ILE C 105 51.80 -144.59
REMARK 500
REMARK 500 THIS ENTRY HAS 86 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 160 0.09 SIDE CHAIN
REMARK 500 TYR B 160 0.08 SIDE CHAIN
REMARK 500 TYR C 160 0.08 SIDE CHAIN
REMARK 500 TYR D 160 0.09 SIDE CHAIN
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OFG RELATED DB: PDB
REMARK 900 1OFG IS WILD-TYPE GFOR
DBREF 1EVJ A 30 381 UNP Q07982 GFO_ZYMMO 82 433
DBREF 1EVJ B 30 381 UNP Q07982 GFO_ZYMMO 82 433
DBREF 1EVJ C 30 381 UNP Q07982 GFO_ZYMMO 82 433
DBREF 1EVJ D 30 381 UNP Q07982 GFO_ZYMMO 82 433
SEQADV 1EVJ ASP A 64 UNP Q07982 SER 116 ENGINEERED MUTATION
SEQADV 1EVJ ASP B 64 UNP Q07982 SER 116 ENGINEERED MUTATION
SEQADV 1EVJ ASP C 64 UNP Q07982 SER 116 ENGINEERED MUTATION
SEQADV 1EVJ ASP D 64 UNP Q07982 SER 116 ENGINEERED MUTATION
SEQRES 1 A 352 ARG ARG PHE GLY TYR ALA ILE VAL GLY LEU GLY LYS TYR
SEQRES 2 A 352 ALA LEU ASN GLN ILE LEU PRO GLY PHE ALA GLY CYS GLN
SEQRES 3 A 352 HIS SER ARG ILE GLU ALA LEU VAL ASP GLY ASN ALA GLU
SEQRES 4 A 352 LYS ALA LYS ILE VAL ALA ALA GLU TYR GLY VAL ASP PRO
SEQRES 5 A 352 ARG LYS ILE TYR ASP TYR SER ASN PHE ASP LYS ILE ALA
SEQRES 6 A 352 LYS ASP PRO LYS ILE ASP ALA VAL TYR ILE ILE LEU PRO
SEQRES 7 A 352 ASN SER LEU HIS ALA GLU PHE ALA ILE ARG ALA PHE LYS
SEQRES 8 A 352 ALA GLY LYS HIS VAL MET CYS GLU LYS PRO MET ALA THR
SEQRES 9 A 352 SER VAL ALA ASP CYS GLN ARG MET ILE ASP ALA ALA LYS
SEQRES 10 A 352 ALA ALA ASN LYS LYS LEU MET ILE GLY TYR ARG CYS HIS
SEQRES 11 A 352 TYR ASP PRO MET ASN ARG ALA ALA VAL LYS LEU ILE ARG
SEQRES 12 A 352 GLU ASN GLN LEU GLY LYS LEU GLY MET VAL THR THR ASP
SEQRES 13 A 352 ASN SER ASP VAL MET ASP GLN ASN ASP PRO ALA GLN GLN
SEQRES 14 A 352 TRP ARG LEU ARG ARG GLU LEU ALA GLY GLY GLY SER LEU
SEQRES 15 A 352 MET ASP ILE GLY ILE TYR GLY LEU ASN GLY THR ARG TYR
SEQRES 16 A 352 LEU LEU GLY GLU GLU PRO ILE GLU VAL ARG ALA TYR THR
SEQRES 17 A 352 TYR SER ASP PRO ASN ASP GLU ARG PHE VAL GLU VAL GLU
SEQRES 18 A 352 ASP ARG ILE ILE TRP GLN MET ARG PHE ARG SER GLY ALA
SEQRES 19 A 352 LEU SER HIS GLY ALA SER SER TYR SER THR THR THR THR
SEQRES 20 A 352 SER ARG PHE SER VAL GLN GLY ASP LYS ALA VAL LEU LEU
SEQRES 21 A 352 MET ASP PRO ALA THR GLY TYR TYR GLN ASN LEU ILE SER
SEQRES 22 A 352 VAL GLN THR PRO GLY HIS ALA ASN GLN SER MET MET PRO
SEQRES 23 A 352 GLN PHE ILE MET PRO ALA ASN ASN GLN PHE SER ALA GLN
SEQRES 24 A 352 LEU ASP HIS LEU ALA GLU ALA VAL ILE ASN ASN LYS PRO
SEQRES 25 A 352 VAL ARG SER PRO GLY GLU GLU GLY MET GLN ASP VAL ARG
SEQRES 26 A 352 LEU ILE GLN ALA ILE TYR GLU ALA ALA ARG THR GLY ARG
SEQRES 27 A 352 PRO VAL ASN THR ASP TRP GLY TYR VAL ARG GLN GLY GLY
SEQRES 28 A 352 TYR
SEQRES 1 B 352 ARG ARG PHE GLY TYR ALA ILE VAL GLY LEU GLY LYS TYR
SEQRES 2 B 352 ALA LEU ASN GLN ILE LEU PRO GLY PHE ALA GLY CYS GLN
SEQRES 3 B 352 HIS SER ARG ILE GLU ALA LEU VAL ASP GLY ASN ALA GLU
SEQRES 4 B 352 LYS ALA LYS ILE VAL ALA ALA GLU TYR GLY VAL ASP PRO
SEQRES 5 B 352 ARG LYS ILE TYR ASP TYR SER ASN PHE ASP LYS ILE ALA
SEQRES 6 B 352 LYS ASP PRO LYS ILE ASP ALA VAL TYR ILE ILE LEU PRO
SEQRES 7 B 352 ASN SER LEU HIS ALA GLU PHE ALA ILE ARG ALA PHE LYS
SEQRES 8 B 352 ALA GLY LYS HIS VAL MET CYS GLU LYS PRO MET ALA THR
SEQRES 9 B 352 SER VAL ALA ASP CYS GLN ARG MET ILE ASP ALA ALA LYS
SEQRES 10 B 352 ALA ALA ASN LYS LYS LEU MET ILE GLY TYR ARG CYS HIS
SEQRES 11 B 352 TYR ASP PRO MET ASN ARG ALA ALA VAL LYS LEU ILE ARG
SEQRES 12 B 352 GLU ASN GLN LEU GLY LYS LEU GLY MET VAL THR THR ASP
SEQRES 13 B 352 ASN SER ASP VAL MET ASP GLN ASN ASP PRO ALA GLN GLN
SEQRES 14 B 352 TRP ARG LEU ARG ARG GLU LEU ALA GLY GLY GLY SER LEU
SEQRES 15 B 352 MET ASP ILE GLY ILE TYR GLY LEU ASN GLY THR ARG TYR
SEQRES 16 B 352 LEU LEU GLY GLU GLU PRO ILE GLU VAL ARG ALA TYR THR
SEQRES 17 B 352 TYR SER ASP PRO ASN ASP GLU ARG PHE VAL GLU VAL GLU
SEQRES 18 B 352 ASP ARG ILE ILE TRP GLN MET ARG PHE ARG SER GLY ALA
SEQRES 19 B 352 LEU SER HIS GLY ALA SER SER TYR SER THR THR THR THR
SEQRES 20 B 352 SER ARG PHE SER VAL GLN GLY ASP LYS ALA VAL LEU LEU
SEQRES 21 B 352 MET ASP PRO ALA THR GLY TYR TYR GLN ASN LEU ILE SER
SEQRES 22 B 352 VAL GLN THR PRO GLY HIS ALA ASN GLN SER MET MET PRO
SEQRES 23 B 352 GLN PHE ILE MET PRO ALA ASN ASN GLN PHE SER ALA GLN
SEQRES 24 B 352 LEU ASP HIS LEU ALA GLU ALA VAL ILE ASN ASN LYS PRO
SEQRES 25 B 352 VAL ARG SER PRO GLY GLU GLU GLY MET GLN ASP VAL ARG
SEQRES 26 B 352 LEU ILE GLN ALA ILE TYR GLU ALA ALA ARG THR GLY ARG
SEQRES 27 B 352 PRO VAL ASN THR ASP TRP GLY TYR VAL ARG GLN GLY GLY
SEQRES 28 B 352 TYR
SEQRES 1 C 352 ARG ARG PHE GLY TYR ALA ILE VAL GLY LEU GLY LYS TYR
SEQRES 2 C 352 ALA LEU ASN GLN ILE LEU PRO GLY PHE ALA GLY CYS GLN
SEQRES 3 C 352 HIS SER ARG ILE GLU ALA LEU VAL ASP GLY ASN ALA GLU
SEQRES 4 C 352 LYS ALA LYS ILE VAL ALA ALA GLU TYR GLY VAL ASP PRO
SEQRES 5 C 352 ARG LYS ILE TYR ASP TYR SER ASN PHE ASP LYS ILE ALA
SEQRES 6 C 352 LYS ASP PRO LYS ILE ASP ALA VAL TYR ILE ILE LEU PRO
SEQRES 7 C 352 ASN SER LEU HIS ALA GLU PHE ALA ILE ARG ALA PHE LYS
SEQRES 8 C 352 ALA GLY LYS HIS VAL MET CYS GLU LYS PRO MET ALA THR
SEQRES 9 C 352 SER VAL ALA ASP CYS GLN ARG MET ILE ASP ALA ALA LYS
SEQRES 10 C 352 ALA ALA ASN LYS LYS LEU MET ILE GLY TYR ARG CYS HIS
SEQRES 11 C 352 TYR ASP PRO MET ASN ARG ALA ALA VAL LYS LEU ILE ARG
SEQRES 12 C 352 GLU ASN GLN LEU GLY LYS LEU GLY MET VAL THR THR ASP
SEQRES 13 C 352 ASN SER ASP VAL MET ASP GLN ASN ASP PRO ALA GLN GLN
SEQRES 14 C 352 TRP ARG LEU ARG ARG GLU LEU ALA GLY GLY GLY SER LEU
SEQRES 15 C 352 MET ASP ILE GLY ILE TYR GLY LEU ASN GLY THR ARG TYR
SEQRES 16 C 352 LEU LEU GLY GLU GLU PRO ILE GLU VAL ARG ALA TYR THR
SEQRES 17 C 352 TYR SER ASP PRO ASN ASP GLU ARG PHE VAL GLU VAL GLU
SEQRES 18 C 352 ASP ARG ILE ILE TRP GLN MET ARG PHE ARG SER GLY ALA
SEQRES 19 C 352 LEU SER HIS GLY ALA SER SER TYR SER THR THR THR THR
SEQRES 20 C 352 SER ARG PHE SER VAL GLN GLY ASP LYS ALA VAL LEU LEU
SEQRES 21 C 352 MET ASP PRO ALA THR GLY TYR TYR GLN ASN LEU ILE SER
SEQRES 22 C 352 VAL GLN THR PRO GLY HIS ALA ASN GLN SER MET MET PRO
SEQRES 23 C 352 GLN PHE ILE MET PRO ALA ASN ASN GLN PHE SER ALA GLN
SEQRES 24 C 352 LEU ASP HIS LEU ALA GLU ALA VAL ILE ASN ASN LYS PRO
SEQRES 25 C 352 VAL ARG SER PRO GLY GLU GLU GLY MET GLN ASP VAL ARG
SEQRES 26 C 352 LEU ILE GLN ALA ILE TYR GLU ALA ALA ARG THR GLY ARG
SEQRES 27 C 352 PRO VAL ASN THR ASP TRP GLY TYR VAL ARG GLN GLY GLY
SEQRES 28 C 352 TYR
SEQRES 1 D 352 ARG ARG PHE GLY TYR ALA ILE VAL GLY LEU GLY LYS TYR
SEQRES 2 D 352 ALA LEU ASN GLN ILE LEU PRO GLY PHE ALA GLY CYS GLN
SEQRES 3 D 352 HIS SER ARG ILE GLU ALA LEU VAL ASP GLY ASN ALA GLU
SEQRES 4 D 352 LYS ALA LYS ILE VAL ALA ALA GLU TYR GLY VAL ASP PRO
SEQRES 5 D 352 ARG LYS ILE TYR ASP TYR SER ASN PHE ASP LYS ILE ALA
SEQRES 6 D 352 LYS ASP PRO LYS ILE ASP ALA VAL TYR ILE ILE LEU PRO
SEQRES 7 D 352 ASN SER LEU HIS ALA GLU PHE ALA ILE ARG ALA PHE LYS
SEQRES 8 D 352 ALA GLY LYS HIS VAL MET CYS GLU LYS PRO MET ALA THR
SEQRES 9 D 352 SER VAL ALA ASP CYS GLN ARG MET ILE ASP ALA ALA LYS
SEQRES 10 D 352 ALA ALA ASN LYS LYS LEU MET ILE GLY TYR ARG CYS HIS
SEQRES 11 D 352 TYR ASP PRO MET ASN ARG ALA ALA VAL LYS LEU ILE ARG
SEQRES 12 D 352 GLU ASN GLN LEU GLY LYS LEU GLY MET VAL THR THR ASP
SEQRES 13 D 352 ASN SER ASP VAL MET ASP GLN ASN ASP PRO ALA GLN GLN
SEQRES 14 D 352 TRP ARG LEU ARG ARG GLU LEU ALA GLY GLY GLY SER LEU
SEQRES 15 D 352 MET ASP ILE GLY ILE TYR GLY LEU ASN GLY THR ARG TYR
SEQRES 16 D 352 LEU LEU GLY GLU GLU PRO ILE GLU VAL ARG ALA TYR THR
SEQRES 17 D 352 TYR SER ASP PRO ASN ASP GLU ARG PHE VAL GLU VAL GLU
SEQRES 18 D 352 ASP ARG ILE ILE TRP GLN MET ARG PHE ARG SER GLY ALA
SEQRES 19 D 352 LEU SER HIS GLY ALA SER SER TYR SER THR THR THR THR
SEQRES 20 D 352 SER ARG PHE SER VAL GLN GLY ASP LYS ALA VAL LEU LEU
SEQRES 21 D 352 MET ASP PRO ALA THR GLY TYR TYR GLN ASN LEU ILE SER
SEQRES 22 D 352 VAL GLN THR PRO GLY HIS ALA ASN GLN SER MET MET PRO
SEQRES 23 D 352 GLN PHE ILE MET PRO ALA ASN ASN GLN PHE SER ALA GLN
SEQRES 24 D 352 LEU ASP HIS LEU ALA GLU ALA VAL ILE ASN ASN LYS PRO
SEQRES 25 D 352 VAL ARG SER PRO GLY GLU GLU GLY MET GLN ASP VAL ARG
SEQRES 26 D 352 LEU ILE GLN ALA ILE TYR GLU ALA ALA ARG THR GLY ARG
SEQRES 27 D 352 PRO VAL ASN THR ASP TRP GLY TYR VAL ARG GLN GLY GLY
SEQRES 28 D 352 TYR
HET NAD A 500 44
HET NAD B 501 44
HET NAD C 502 44
HET NAD D 503 44
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 5 NAD 4(C21 H27 N7 O14 P2)
FORMUL 9 HOH *130(H2 O)
HELIX 1 1 GLY A 40 GLN A 46 1 7
HELIX 2 2 GLN A 46 PHE A 51 1 6
HELIX 3 3 ALA A 52 CYS A 54 5 3
HELIX 4 4 ASN A 66 GLY A 78 1 13
HELIX 5 5 ASP A 80 ARG A 82 5 3
HELIX 6 6 ASN A 89 ASP A 96 5 8
HELIX 7 7 SER A 109 ALA A 121 1 13
HELIX 8 8 SER A 134 ASN A 149 1 16
HELIX 9 9 TYR A 156 TYR A 160 5 5
HELIX 10 10 ASP A 161 GLU A 173 1 13
HELIX 11 11 GLN A 198 LEU A 201 5 4
HELIX 12 12 ARG A 202 GLY A 207 1 6
HELIX 13 13 GLY A 209 ILE A 214 1 6
HELIX 14 14 ILE A 214 GLY A 227 1 14
HELIX 15 15 ASP A 243 VAL A 247 5 5
HELIX 16 16 ASN A 323 ASN A 338 1 16
HELIX 17 17 PRO A 345 GLY A 366 1 22
HELIX 18 18 GLY B 40 GLN B 46 1 7
HELIX 19 19 GLN B 46 PHE B 51 1 6
HELIX 20 20 ALA B 52 CYS B 54 5 3
HELIX 21 21 ASN B 66 GLY B 78 1 13
HELIX 22 22 ASP B 80 ARG B 82 5 3
HELIX 23 23 ASN B 89 ASP B 96 5 8
HELIX 24 24 SER B 109 ALA B 121 1 13
HELIX 25 25 SER B 134 ASN B 149 1 16
HELIX 26 26 TYR B 156 TYR B 160 5 5
HELIX 27 27 ASP B 161 GLU B 173 1 13
HELIX 28 28 GLN B 198 LEU B 201 5 4
HELIX 29 29 ARG B 202 GLY B 207 1 6
HELIX 30 30 GLY B 209 ILE B 214 1 6
HELIX 31 31 ILE B 214 GLY B 227 1 14
HELIX 32 32 ASP B 243 VAL B 247 5 5
HELIX 33 33 ASN B 323 ASN B 338 1 16
HELIX 34 34 PRO B 345 GLY B 366 1 22
HELIX 35 35 GLY C 40 GLN C 46 1 7
HELIX 36 36 GLN C 46 PHE C 51 1 6
HELIX 37 37 ALA C 52 CYS C 54 5 3
HELIX 38 38 ASN C 66 GLY C 78 1 13
HELIX 39 39 ASP C 80 ARG C 82 5 3
HELIX 40 40 ASN C 89 ASP C 96 5 8
HELIX 41 41 SER C 109 ALA C 121 1 13
HELIX 42 42 SER C 134 ASN C 149 1 16
HELIX 43 43 TYR C 156 TYR C 160 5 5
HELIX 44 44 ASP C 161 GLU C 173 1 13
HELIX 45 45 GLN C 198 LEU C 201 5 4
HELIX 46 46 ARG C 202 GLY C 207 1 6
HELIX 47 47 GLY C 209 ILE C 214 1 6
HELIX 48 48 ILE C 214 GLY C 227 1 14
HELIX 49 49 ASP C 243 VAL C 247 5 5
HELIX 50 50 ASN C 323 ASN C 338 1 16
HELIX 51 51 PRO C 345 GLY C 366 1 22
HELIX 52 52 GLY D 40 GLN D 46 1 7
HELIX 53 53 GLN D 46 PHE D 51 1 6
HELIX 54 54 ALA D 52 CYS D 54 5 3
HELIX 55 55 ASN D 66 GLY D 78 1 13
HELIX 56 56 ASP D 80 ARG D 82 5 3
HELIX 57 57 ASN D 89 ASP D 96 5 8
HELIX 58 58 SER D 109 ALA D 121 1 13
HELIX 59 59 SER D 134 ASN D 149 1 16
HELIX 60 60 TYR D 156 TYR D 160 5 5
HELIX 61 61 ASP D 161 GLU D 173 1 13
HELIX 62 62 GLN D 198 LEU D 201 5 4
HELIX 63 63 ARG D 202 GLY D 207 1 6
HELIX 64 64 GLY D 209 ILE D 214 1 6
HELIX 65 65 ILE D 214 GLY D 227 1 14
HELIX 66 66 ASP D 243 VAL D 247 5 5
HELIX 67 67 ASN D 323 ASN D 338 1 16
HELIX 68 68 PRO D 345 GLY D 366 1 22
SHEET 1 A 6 ILE A 84 TYR A 85 0
SHEET 2 A 6 SER A 57 VAL A 63 1 O LEU A 62 N TYR A 85
SHEET 3 A 6 PHE A 32 VAL A 37 1 O PHE A 32 N ARG A 58
SHEET 4 A 6 ALA A 101 ILE A 104 1 N ALA A 101 O GLY A 33
SHEET 5 A 6 HIS A 124 CYS A 127 1 O HIS A 124 N VAL A 102
SHEET 6 A 6 LEU A 152 ILE A 154 1 N MET A 153 O VAL A 125
SHEET 1 B 8 ILE A 301 GLN A 304 0
SHEET 2 B 8 VAL A 287 MET A 290 -1 O VAL A 287 N GLN A 304
SHEET 3 B 8 THR A 276 GLN A 282 -1 O PHE A 279 N MET A 290
SHEET 4 B 8 MET A 181 SER A 187 -1 O MET A 181 N GLN A 282
SHEET 5 B 8 LEU A 264 SER A 270 1 O LEU A 264 N VAL A 182
SHEET 6 B 8 ARG A 252 PHE A 259 -1 N ILE A 253 O SER A 269
SHEET 7 B 8 PRO A 230 TYR A 238 -1 N ILE A 231 O ARG A 258
SHEET 8 B 8 VAL A 369 ASN A 370 -1 N VAL A 369 O VAL A 233
SHEET 1 C 6 ILE B 84 TYR B 85 0
SHEET 2 C 6 SER B 57 VAL B 63 1 O LEU B 62 N TYR B 85
SHEET 3 C 6 PHE B 32 VAL B 37 1 O PHE B 32 N ARG B 58
SHEET 4 C 6 ALA B 101 ILE B 104 1 N ALA B 101 O GLY B 33
SHEET 5 C 6 HIS B 124 CYS B 127 1 O HIS B 124 N VAL B 102
SHEET 6 C 6 LEU B 152 ILE B 154 1 N MET B 153 O VAL B 125
SHEET 1 D 8 ILE B 301 GLN B 304 0
SHEET 2 D 8 VAL B 287 MET B 290 -1 O VAL B 287 N GLN B 304
SHEET 3 D 8 THR B 276 GLN B 282 -1 O PHE B 279 N MET B 290
SHEET 4 D 8 MET B 181 SER B 187 -1 O MET B 181 N GLN B 282
SHEET 5 D 8 LEU B 264 SER B 270 1 O LEU B 264 N VAL B 182
SHEET 6 D 8 ARG B 252 PHE B 259 -1 N ILE B 253 O SER B 269
SHEET 7 D 8 PRO B 230 TYR B 238 -1 N ILE B 231 O ARG B 258
SHEET 8 D 8 VAL B 369 ASN B 370 -1 N VAL B 369 O VAL B 233
SHEET 1 E 6 ILE C 84 TYR C 85 0
SHEET 2 E 6 SER C 57 VAL C 63 1 O LEU C 62 N TYR C 85
SHEET 3 E 6 PHE C 32 VAL C 37 1 O PHE C 32 N ARG C 58
SHEET 4 E 6 ALA C 101 ILE C 104 1 N ALA C 101 O GLY C 33
SHEET 5 E 6 HIS C 124 CYS C 127 1 O HIS C 124 N VAL C 102
SHEET 6 E 6 LEU C 152 ILE C 154 1 N MET C 153 O VAL C 125
SHEET 1 F 8 ILE C 301 GLN C 304 0
SHEET 2 F 8 VAL C 287 MET C 290 -1 O VAL C 287 N GLN C 304
SHEET 3 F 8 THR C 276 GLN C 282 -1 O PHE C 279 N MET C 290
SHEET 4 F 8 MET C 181 SER C 187 -1 O MET C 181 N GLN C 282
SHEET 5 F 8 LEU C 264 SER C 270 1 O LEU C 264 N VAL C 182
SHEET 6 F 8 ARG C 252 PHE C 259 -1 N ILE C 253 O SER C 269
SHEET 7 F 8 PRO C 230 TYR C 238 -1 N ILE C 231 O ARG C 258
SHEET 8 F 8 VAL C 369 ASN C 370 -1 N VAL C 369 O VAL C 233
SHEET 1 G 6 ILE D 84 TYR D 85 0
SHEET 2 G 6 SER D 57 VAL D 63 1 O LEU D 62 N TYR D 85
SHEET 3 G 6 PHE D 32 VAL D 37 1 O PHE D 32 N ARG D 58
SHEET 4 G 6 ALA D 101 ILE D 104 1 N ALA D 101 O GLY D 33
SHEET 5 G 6 HIS D 124 CYS D 127 1 O HIS D 124 N VAL D 102
SHEET 6 G 6 LEU D 152 ILE D 154 1 N MET D 153 O VAL D 125
SHEET 1 H 8 ILE D 301 GLN D 304 0
SHEET 2 H 8 VAL D 287 MET D 290 -1 O VAL D 287 N GLN D 304
SHEET 3 H 8 THR D 276 GLN D 282 -1 O PHE D 279 N MET D 290
SHEET 4 H 8 MET D 181 SER D 187 -1 O MET D 181 N GLN D 282
SHEET 5 H 8 LEU D 264 SER D 270 1 O LEU D 264 N VAL D 182
SHEET 6 H 8 ARG D 252 PHE D 259 -1 N ILE D 253 O SER D 269
SHEET 7 H 8 PRO D 230 TYR D 238 -1 N ILE D 231 O ARG D 258
SHEET 8 H 8 VAL D 369 ASN D 370 -1 O VAL D 369 N VAL D 233
CISPEP 1 LYS A 129 PRO A 130 0 -2.52
CISPEP 2 ASP A 291 PRO A 292 0 -0.62
CISPEP 3 LYS B 129 PRO B 130 0 -2.48
CISPEP 4 ASP B 291 PRO B 292 0 -0.73
CISPEP 5 LYS C 129 PRO C 130 0 -2.28
CISPEP 6 ASP C 291 PRO C 292 0 -0.63
CISPEP 7 LYS D 129 PRO D 130 0 -2.14
CISPEP 8 ASP D 291 PRO D 292 0 -0.67
SITE 1 AC1 23 GLY A 38 LEU A 39 GLY A 40 LYS A 41
SITE 2 AC1 23 TYR A 42 ASP A 64 TYR A 87 ILE A 105
SITE 3 AC1 23 LEU A 106 PRO A 107 ASN A 108 HIS A 111
SITE 4 AC1 23 GLU A 128 LYS A 129 ARG A 157 TRP A 199
SITE 5 AC1 23 ARG A 200 TYR A 217 TYR A 296 HOH A 605
SITE 6 AC1 23 HOH A 647 HOH A 656 HOH A 657
SITE 1 AC2 22 GLY B 38 LEU B 39 GLY B 40 LYS B 41
SITE 2 AC2 22 TYR B 42 ASP B 64 TYR B 87 ILE B 105
SITE 3 AC2 22 LEU B 106 PRO B 107 ASN B 108 HIS B 111
SITE 4 AC2 22 GLU B 128 LYS B 129 ARG B 157 TRP B 199
SITE 5 AC2 22 ARG B 200 TYR B 217 TYR B 296 HOH B 600
SITE 6 AC2 22 HOH B 638 HOH B 675
SITE 1 AC3 24 GLY C 38 LEU C 39 GLY C 40 LYS C 41
SITE 2 AC3 24 TYR C 42 ASP C 64 TYR C 87 ILE C 105
SITE 3 AC3 24 LEU C 106 PRO C 107 ASN C 108 HIS C 111
SITE 4 AC3 24 GLU C 128 LYS C 129 ARG C 157 TRP C 199
SITE 5 AC3 24 ARG C 200 TYR C 217 TYR C 296 HOH C 601
SITE 6 AC3 24 HOH C 658 HOH C 659 HOH C 706 HOH C 728
SITE 1 AC4 22 GLY D 38 LEU D 39 GLY D 40 LYS D 41
SITE 2 AC4 22 TYR D 42 ASP D 64 TYR D 87 ILE D 105
SITE 3 AC4 22 LEU D 106 PRO D 107 ASN D 108 HIS D 111
SITE 4 AC4 22 GLU D 128 LYS D 129 ARG D 157 TRP D 199
SITE 5 AC4 22 ARG D 200 TYR D 217 TYR D 296 HOH D 651
SITE 6 AC4 22 HOH D 652 HOH D 661
CRYST1 47.710 91.460 98.920 64.53 84.45 75.28 P 1 4
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 0.020960 -0.005507 0.000312 0.00000
SCALE2 0.000000 0.011305 -0.005250 0.00000
SCALE3 0.000000 0.000000 0.011199 0.00000
(ATOM LINES ARE NOT SHOWN.)
END