HEADER OXIDOREDUCTASE 27-JAN-01 1I01
TITLE CRYSTAL STRUCTURE OF BETA-KETOACYL [ACYL CARRIER PROTEIN] REDUCTASE
TITLE 2 FROM E. COLI.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-KETOACYL [ACP] REDUCTASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: 3-OXOACYL-[ACYL-CARRIER PROTEIN] REDUCTASE, 3-KETOACYL-ACYL
COMPND 5 CARRIER PROTEIN REDUCTASE;
COMPND 6 EC: 1.1.1.100;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ROSSMANN FOLD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.PRICE,C.O.ROCK,S.W.WHITE
REVDAT 5 07-FEB-24 1I01 1 REMARK
REVDAT 4 12-NOV-14 1I01 1 KEYWDS
REVDAT 3 24-FEB-09 1I01 1 VERSN
REVDAT 2 21-DEC-01 1I01 1 JRNL
REVDAT 1 07-FEB-01 1I01 0
JRNL AUTH A.C.PRICE,Y.M.ZHANG,C.O.ROCK,S.W.WHITE
JRNL TITL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] REDUCTASE
JRNL TITL 2 FROM ESCHERICHIA COLI: NEGATIVE COOPERATIVITY AND ITS
JRNL TITL 3 STRUCTURAL BASIS.
JRNL REF BIOCHEMISTRY V. 40 12772 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11669613
JRNL DOI 10.1021/BI010737G
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 55982
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) : 0.228
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2826
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13253
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 349
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.60
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.700
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I01 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012736.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97938, 0.95373
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRANDEIS - B4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARMAD
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56511
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.09300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10000, HEPES, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 60.05000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A
REMARK 300 TETRAMER FORMED BY MOLECULES
REMARK 300 A, B, C, AND D.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 88
REMARK 465 ILE A 89
REMARK 465 THR A 90
REMARK 465 ARG A 91
REMARK 465 ASP A 92
REMARK 465 GLY A 144
REMARK 465 ASN A 145
REMARK 465 GLY A 146
REMARK 465 GLY A 147
REMARK 465 GLN A 148
REMARK 465 ALA A 149
REMARK 465 ASN A 150
REMARK 465 TYR A 151
REMARK 465 TYR A 242
REMARK 465 MET A 243
REMARK 465 VAL A 244
REMARK 465 MET B 143
REMARK 465 GLY B 144
REMARK 465 ASN B 145
REMARK 465 GLY B 146
REMARK 465 ASP B 187
REMARK 465 MET B 188
REMARK 465 THR B 189
REMARK 465 ARG B 190
REMARK 465 ALA B 191
REMARK 465 LEU B 192
REMARK 465 TYR B 242
REMARK 465 MET B 243
REMARK 465 VAL B 244
REMARK 465 ASP C 62
REMARK 465 PRO C 63
REMARK 465 ALA C 64
REMARK 465 ALA C 87
REMARK 465 GLY C 88
REMARK 465 ILE C 89
REMARK 465 THR C 90
REMARK 465 ARG C 91
REMARK 465 GLY C 141
REMARK 465 THR C 142
REMARK 465 MET C 143
REMARK 465 GLY C 144
REMARK 465 ASN C 145
REMARK 465 GLY C 146
REMARK 465 GLY C 147
REMARK 465 GLN C 148
REMARK 465 LEU C 192
REMARK 465 SER C 193
REMARK 465 ASP C 194
REMARK 465 ASP C 195
REMARK 465 GLN C 196
REMARK 465 TYR C 242
REMARK 465 MET C 243
REMARK 465 VAL C 244
REMARK 465 ALA D 87
REMARK 465 GLY D 88
REMARK 465 ILE D 89
REMARK 465 THR D 90
REMARK 465 ARG D 91
REMARK 465 GLY D 141
REMARK 465 THR D 142
REMARK 465 MET D 143
REMARK 465 GLY D 144
REMARK 465 ASN D 145
REMARK 465 GLY D 146
REMARK 465 GLY D 147
REMARK 465 GLN D 148
REMARK 465 ASP D 187
REMARK 465 MET D 188
REMARK 465 THR D 189
REMARK 465 ARG D 190
REMARK 465 TYR D 242
REMARK 465 MET D 243
REMARK 465 VAL D 244
REMARK 465 MET E 1
REMARK 465 GLY E 141
REMARK 465 THR E 142
REMARK 465 MET E 143
REMARK 465 GLY E 144
REMARK 465 ASN E 145
REMARK 465 GLY E 146
REMARK 465 TYR E 242
REMARK 465 MET E 243
REMARK 465 VAL E 244
REMARK 465 MET F 1
REMARK 465 ILE F 89
REMARK 465 THR F 90
REMARK 465 ARG F 91
REMARK 465 ASP F 92
REMARK 465 GLY F 141
REMARK 465 THR F 142
REMARK 465 MET F 143
REMARK 465 GLY F 144
REMARK 465 ASN F 145
REMARK 465 GLY F 146
REMARK 465 GLY F 147
REMARK 465 GLN F 148
REMARK 465 ALA F 149
REMARK 465 ASN F 150
REMARK 465 TYR F 151
REMARK 465 TYR F 242
REMARK 465 MET F 243
REMARK 465 VAL F 244
REMARK 465 GLY G 88
REMARK 465 ILE G 89
REMARK 465 THR G 90
REMARK 465 ARG G 91
REMARK 465 SER G 138
REMARK 465 VAL G 139
REMARK 465 VAL G 140
REMARK 465 GLY G 141
REMARK 465 THR G 142
REMARK 465 MET G 143
REMARK 465 GLY G 144
REMARK 465 ASN G 145
REMARK 465 GLY G 146
REMARK 465 GLY G 147
REMARK 465 GLN G 148
REMARK 465 ALA G 149
REMARK 465 ASN G 150
REMARK 465 TYR G 242
REMARK 465 MET G 243
REMARK 465 VAL G 244
REMARK 465 MET H 1
REMARK 465 ASN H 2
REMARK 465 GLY H 88
REMARK 465 ILE H 89
REMARK 465 THR H 90
REMARK 465 ARG H 91
REMARK 465 SER H 138
REMARK 465 VAL H 139
REMARK 465 VAL H 140
REMARK 465 GLY H 141
REMARK 465 THR H 142
REMARK 465 MET H 143
REMARK 465 GLY H 144
REMARK 465 ASN H 145
REMARK 465 GLY H 146
REMARK 465 GLY H 147
REMARK 465 GLN H 148
REMARK 465 SER H 193
REMARK 465 ASP H 194
REMARK 465 ASP H 195
REMARK 465 TYR H 242
REMARK 465 MET H 243
REMARK 465 VAL H 244
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP B 47 O HOH B 293 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG B 19 NH1 ARG H 19 2646 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET B 96 SD MET B 96 CE -0.344
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 LEU A 95 -4.55 -46.29
REMARK 500 ARG A 97 -10.23 -157.32
REMARK 500 MET B 96 2.65 -67.88
REMARK 500 GLU C 185 107.88 -48.10
REMARK 500 THR C 186 -129.28 -117.92
REMARK 500 GLU D 4 122.64 -37.80
REMARK 500 ALA D 51 2.93 -69.60
REMARK 500 VAL D 60 -1.79 -52.89
REMARK 500 MET D 96 6.74 -69.59
REMARK 500 LEU D 192 164.29 -46.28
REMARK 500 ASN D 238 14.79 -140.15
REMARK 500 ARG F 15 -175.80 -171.07
REMARK 500 VAL G 60 -5.56 -56.22
REMARK 500 ASN G 238 20.36 -144.56
REMARK 500 ASN H 238 22.26 -142.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 HOH 1-36 IS ASSOCIATED WITH CHAIN A.
REMARK 600 HOH 101-136 IS ASSOCIATED WITH CHAIN B.
REMARK 600 HOH 201-236 IS ASSOCIATED WITH CHAIN C.
REMARK 600 HOH 301-336 IS ASSOCIATED WITH CHAIN D.
REMARK 600 HOH 401-436 IS ASSOCIATED WITH CHAIN E.
REMARK 600 HOH 501-536 IS ASSOCIATED WITH CHAIN F.
REMARK 600 HOH 601-636 IS ASSOCIATED WITH CHAIN G.
REMARK 600 HOH 701-736 IS ASSOCIATED WITH CHAIN H.
DBREF 1I01 A 1 244 UNP P0AEK2 FABG_ECOLI 1 244
DBREF 1I01 B 1 244 UNP P0AEK2 FABG_ECOLI 1 244
DBREF 1I01 C 1 244 UNP P0AEK2 FABG_ECOLI 1 244
DBREF 1I01 D 1 244 UNP P0AEK2 FABG_ECOLI 1 244
DBREF 1I01 E 1 244 UNP P0AEK2 FABG_ECOLI 1 244
DBREF 1I01 F 1 244 UNP P0AEK2 FABG_ECOLI 1 244
DBREF 1I01 G 1 244 UNP P0AEK2 FABG_ECOLI 1 244
DBREF 1I01 H 1 244 UNP P0AEK2 FABG_ECOLI 1 244
SEQRES 1 A 244 MET ASN PHE GLU GLY LYS ILE ALA LEU VAL THR GLY ALA
SEQRES 2 A 244 SER ARG GLY ILE GLY ARG ALA ILE ALA GLU THR LEU ALA
SEQRES 3 A 244 ALA ARG GLY ALA LYS VAL ILE GLY THR ALA THR SER GLU
SEQRES 4 A 244 ASN GLY ALA GLN ALA ILE SER ASP TYR LEU GLY ALA ASN
SEQRES 5 A 244 GLY LYS GLY LEU MET LEU ASN VAL THR ASP PRO ALA SER
SEQRES 6 A 244 ILE GLU SER VAL LEU GLU LYS ILE ARG ALA GLU PHE GLY
SEQRES 7 A 244 GLU VAL ASP ILE LEU VAL ASN ASN ALA GLY ILE THR ARG
SEQRES 8 A 244 ASP ASN LEU LEU MET ARG MET LYS ASP GLU GLU TRP ASN
SEQRES 9 A 244 ASP ILE ILE GLU THR ASN LEU SER SER VAL PHE ARG LEU
SEQRES 10 A 244 SER LYS ALA VAL MET ARG ALA MET MET LYS LYS ARG HIS
SEQRES 11 A 244 GLY ARG ILE ILE THR ILE GLY SER VAL VAL GLY THR MET
SEQRES 12 A 244 GLY ASN GLY GLY GLN ALA ASN TYR ALA ALA ALA LYS ALA
SEQRES 13 A 244 GLY LEU ILE GLY PHE SER LYS SER LEU ALA ARG GLU VAL
SEQRES 14 A 244 ALA SER ARG GLY ILE THR VAL ASN VAL VAL ALA PRO GLY
SEQRES 15 A 244 PHE ILE GLU THR ASP MET THR ARG ALA LEU SER ASP ASP
SEQRES 16 A 244 GLN ARG ALA GLY ILE LEU ALA GLN VAL PRO ALA GLY ARG
SEQRES 17 A 244 LEU GLY GLY ALA GLN GLU ILE ALA ASN ALA VAL ALA PHE
SEQRES 18 A 244 LEU ALA SER ASP GLU ALA ALA TYR ILE THR GLY GLU THR
SEQRES 19 A 244 LEU HIS VAL ASN GLY GLY MET TYR MET VAL
SEQRES 1 B 244 MET ASN PHE GLU GLY LYS ILE ALA LEU VAL THR GLY ALA
SEQRES 2 B 244 SER ARG GLY ILE GLY ARG ALA ILE ALA GLU THR LEU ALA
SEQRES 3 B 244 ALA ARG GLY ALA LYS VAL ILE GLY THR ALA THR SER GLU
SEQRES 4 B 244 ASN GLY ALA GLN ALA ILE SER ASP TYR LEU GLY ALA ASN
SEQRES 5 B 244 GLY LYS GLY LEU MET LEU ASN VAL THR ASP PRO ALA SER
SEQRES 6 B 244 ILE GLU SER VAL LEU GLU LYS ILE ARG ALA GLU PHE GLY
SEQRES 7 B 244 GLU VAL ASP ILE LEU VAL ASN ASN ALA GLY ILE THR ARG
SEQRES 8 B 244 ASP ASN LEU LEU MET ARG MET LYS ASP GLU GLU TRP ASN
SEQRES 9 B 244 ASP ILE ILE GLU THR ASN LEU SER SER VAL PHE ARG LEU
SEQRES 10 B 244 SER LYS ALA VAL MET ARG ALA MET MET LYS LYS ARG HIS
SEQRES 11 B 244 GLY ARG ILE ILE THR ILE GLY SER VAL VAL GLY THR MET
SEQRES 12 B 244 GLY ASN GLY GLY GLN ALA ASN TYR ALA ALA ALA LYS ALA
SEQRES 13 B 244 GLY LEU ILE GLY PHE SER LYS SER LEU ALA ARG GLU VAL
SEQRES 14 B 244 ALA SER ARG GLY ILE THR VAL ASN VAL VAL ALA PRO GLY
SEQRES 15 B 244 PHE ILE GLU THR ASP MET THR ARG ALA LEU SER ASP ASP
SEQRES 16 B 244 GLN ARG ALA GLY ILE LEU ALA GLN VAL PRO ALA GLY ARG
SEQRES 17 B 244 LEU GLY GLY ALA GLN GLU ILE ALA ASN ALA VAL ALA PHE
SEQRES 18 B 244 LEU ALA SER ASP GLU ALA ALA TYR ILE THR GLY GLU THR
SEQRES 19 B 244 LEU HIS VAL ASN GLY GLY MET TYR MET VAL
SEQRES 1 C 244 MET ASN PHE GLU GLY LYS ILE ALA LEU VAL THR GLY ALA
SEQRES 2 C 244 SER ARG GLY ILE GLY ARG ALA ILE ALA GLU THR LEU ALA
SEQRES 3 C 244 ALA ARG GLY ALA LYS VAL ILE GLY THR ALA THR SER GLU
SEQRES 4 C 244 ASN GLY ALA GLN ALA ILE SER ASP TYR LEU GLY ALA ASN
SEQRES 5 C 244 GLY LYS GLY LEU MET LEU ASN VAL THR ASP PRO ALA SER
SEQRES 6 C 244 ILE GLU SER VAL LEU GLU LYS ILE ARG ALA GLU PHE GLY
SEQRES 7 C 244 GLU VAL ASP ILE LEU VAL ASN ASN ALA GLY ILE THR ARG
SEQRES 8 C 244 ASP ASN LEU LEU MET ARG MET LYS ASP GLU GLU TRP ASN
SEQRES 9 C 244 ASP ILE ILE GLU THR ASN LEU SER SER VAL PHE ARG LEU
SEQRES 10 C 244 SER LYS ALA VAL MET ARG ALA MET MET LYS LYS ARG HIS
SEQRES 11 C 244 GLY ARG ILE ILE THR ILE GLY SER VAL VAL GLY THR MET
SEQRES 12 C 244 GLY ASN GLY GLY GLN ALA ASN TYR ALA ALA ALA LYS ALA
SEQRES 13 C 244 GLY LEU ILE GLY PHE SER LYS SER LEU ALA ARG GLU VAL
SEQRES 14 C 244 ALA SER ARG GLY ILE THR VAL ASN VAL VAL ALA PRO GLY
SEQRES 15 C 244 PHE ILE GLU THR ASP MET THR ARG ALA LEU SER ASP ASP
SEQRES 16 C 244 GLN ARG ALA GLY ILE LEU ALA GLN VAL PRO ALA GLY ARG
SEQRES 17 C 244 LEU GLY GLY ALA GLN GLU ILE ALA ASN ALA VAL ALA PHE
SEQRES 18 C 244 LEU ALA SER ASP GLU ALA ALA TYR ILE THR GLY GLU THR
SEQRES 19 C 244 LEU HIS VAL ASN GLY GLY MET TYR MET VAL
SEQRES 1 D 244 MET ASN PHE GLU GLY LYS ILE ALA LEU VAL THR GLY ALA
SEQRES 2 D 244 SER ARG GLY ILE GLY ARG ALA ILE ALA GLU THR LEU ALA
SEQRES 3 D 244 ALA ARG GLY ALA LYS VAL ILE GLY THR ALA THR SER GLU
SEQRES 4 D 244 ASN GLY ALA GLN ALA ILE SER ASP TYR LEU GLY ALA ASN
SEQRES 5 D 244 GLY LYS GLY LEU MET LEU ASN VAL THR ASP PRO ALA SER
SEQRES 6 D 244 ILE GLU SER VAL LEU GLU LYS ILE ARG ALA GLU PHE GLY
SEQRES 7 D 244 GLU VAL ASP ILE LEU VAL ASN ASN ALA GLY ILE THR ARG
SEQRES 8 D 244 ASP ASN LEU LEU MET ARG MET LYS ASP GLU GLU TRP ASN
SEQRES 9 D 244 ASP ILE ILE GLU THR ASN LEU SER SER VAL PHE ARG LEU
SEQRES 10 D 244 SER LYS ALA VAL MET ARG ALA MET MET LYS LYS ARG HIS
SEQRES 11 D 244 GLY ARG ILE ILE THR ILE GLY SER VAL VAL GLY THR MET
SEQRES 12 D 244 GLY ASN GLY GLY GLN ALA ASN TYR ALA ALA ALA LYS ALA
SEQRES 13 D 244 GLY LEU ILE GLY PHE SER LYS SER LEU ALA ARG GLU VAL
SEQRES 14 D 244 ALA SER ARG GLY ILE THR VAL ASN VAL VAL ALA PRO GLY
SEQRES 15 D 244 PHE ILE GLU THR ASP MET THR ARG ALA LEU SER ASP ASP
SEQRES 16 D 244 GLN ARG ALA GLY ILE LEU ALA GLN VAL PRO ALA GLY ARG
SEQRES 17 D 244 LEU GLY GLY ALA GLN GLU ILE ALA ASN ALA VAL ALA PHE
SEQRES 18 D 244 LEU ALA SER ASP GLU ALA ALA TYR ILE THR GLY GLU THR
SEQRES 19 D 244 LEU HIS VAL ASN GLY GLY MET TYR MET VAL
SEQRES 1 E 244 MET ASN PHE GLU GLY LYS ILE ALA LEU VAL THR GLY ALA
SEQRES 2 E 244 SER ARG GLY ILE GLY ARG ALA ILE ALA GLU THR LEU ALA
SEQRES 3 E 244 ALA ARG GLY ALA LYS VAL ILE GLY THR ALA THR SER GLU
SEQRES 4 E 244 ASN GLY ALA GLN ALA ILE SER ASP TYR LEU GLY ALA ASN
SEQRES 5 E 244 GLY LYS GLY LEU MET LEU ASN VAL THR ASP PRO ALA SER
SEQRES 6 E 244 ILE GLU SER VAL LEU GLU LYS ILE ARG ALA GLU PHE GLY
SEQRES 7 E 244 GLU VAL ASP ILE LEU VAL ASN ASN ALA GLY ILE THR ARG
SEQRES 8 E 244 ASP ASN LEU LEU MET ARG MET LYS ASP GLU GLU TRP ASN
SEQRES 9 E 244 ASP ILE ILE GLU THR ASN LEU SER SER VAL PHE ARG LEU
SEQRES 10 E 244 SER LYS ALA VAL MET ARG ALA MET MET LYS LYS ARG HIS
SEQRES 11 E 244 GLY ARG ILE ILE THR ILE GLY SER VAL VAL GLY THR MET
SEQRES 12 E 244 GLY ASN GLY GLY GLN ALA ASN TYR ALA ALA ALA LYS ALA
SEQRES 13 E 244 GLY LEU ILE GLY PHE SER LYS SER LEU ALA ARG GLU VAL
SEQRES 14 E 244 ALA SER ARG GLY ILE THR VAL ASN VAL VAL ALA PRO GLY
SEQRES 15 E 244 PHE ILE GLU THR ASP MET THR ARG ALA LEU SER ASP ASP
SEQRES 16 E 244 GLN ARG ALA GLY ILE LEU ALA GLN VAL PRO ALA GLY ARG
SEQRES 17 E 244 LEU GLY GLY ALA GLN GLU ILE ALA ASN ALA VAL ALA PHE
SEQRES 18 E 244 LEU ALA SER ASP GLU ALA ALA TYR ILE THR GLY GLU THR
SEQRES 19 E 244 LEU HIS VAL ASN GLY GLY MET TYR MET VAL
SEQRES 1 F 244 MET ASN PHE GLU GLY LYS ILE ALA LEU VAL THR GLY ALA
SEQRES 2 F 244 SER ARG GLY ILE GLY ARG ALA ILE ALA GLU THR LEU ALA
SEQRES 3 F 244 ALA ARG GLY ALA LYS VAL ILE GLY THR ALA THR SER GLU
SEQRES 4 F 244 ASN GLY ALA GLN ALA ILE SER ASP TYR LEU GLY ALA ASN
SEQRES 5 F 244 GLY LYS GLY LEU MET LEU ASN VAL THR ASP PRO ALA SER
SEQRES 6 F 244 ILE GLU SER VAL LEU GLU LYS ILE ARG ALA GLU PHE GLY
SEQRES 7 F 244 GLU VAL ASP ILE LEU VAL ASN ASN ALA GLY ILE THR ARG
SEQRES 8 F 244 ASP ASN LEU LEU MET ARG MET LYS ASP GLU GLU TRP ASN
SEQRES 9 F 244 ASP ILE ILE GLU THR ASN LEU SER SER VAL PHE ARG LEU
SEQRES 10 F 244 SER LYS ALA VAL MET ARG ALA MET MET LYS LYS ARG HIS
SEQRES 11 F 244 GLY ARG ILE ILE THR ILE GLY SER VAL VAL GLY THR MET
SEQRES 12 F 244 GLY ASN GLY GLY GLN ALA ASN TYR ALA ALA ALA LYS ALA
SEQRES 13 F 244 GLY LEU ILE GLY PHE SER LYS SER LEU ALA ARG GLU VAL
SEQRES 14 F 244 ALA SER ARG GLY ILE THR VAL ASN VAL VAL ALA PRO GLY
SEQRES 15 F 244 PHE ILE GLU THR ASP MET THR ARG ALA LEU SER ASP ASP
SEQRES 16 F 244 GLN ARG ALA GLY ILE LEU ALA GLN VAL PRO ALA GLY ARG
SEQRES 17 F 244 LEU GLY GLY ALA GLN GLU ILE ALA ASN ALA VAL ALA PHE
SEQRES 18 F 244 LEU ALA SER ASP GLU ALA ALA TYR ILE THR GLY GLU THR
SEQRES 19 F 244 LEU HIS VAL ASN GLY GLY MET TYR MET VAL
SEQRES 1 G 244 MET ASN PHE GLU GLY LYS ILE ALA LEU VAL THR GLY ALA
SEQRES 2 G 244 SER ARG GLY ILE GLY ARG ALA ILE ALA GLU THR LEU ALA
SEQRES 3 G 244 ALA ARG GLY ALA LYS VAL ILE GLY THR ALA THR SER GLU
SEQRES 4 G 244 ASN GLY ALA GLN ALA ILE SER ASP TYR LEU GLY ALA ASN
SEQRES 5 G 244 GLY LYS GLY LEU MET LEU ASN VAL THR ASP PRO ALA SER
SEQRES 6 G 244 ILE GLU SER VAL LEU GLU LYS ILE ARG ALA GLU PHE GLY
SEQRES 7 G 244 GLU VAL ASP ILE LEU VAL ASN ASN ALA GLY ILE THR ARG
SEQRES 8 G 244 ASP ASN LEU LEU MET ARG MET LYS ASP GLU GLU TRP ASN
SEQRES 9 G 244 ASP ILE ILE GLU THR ASN LEU SER SER VAL PHE ARG LEU
SEQRES 10 G 244 SER LYS ALA VAL MET ARG ALA MET MET LYS LYS ARG HIS
SEQRES 11 G 244 GLY ARG ILE ILE THR ILE GLY SER VAL VAL GLY THR MET
SEQRES 12 G 244 GLY ASN GLY GLY GLN ALA ASN TYR ALA ALA ALA LYS ALA
SEQRES 13 G 244 GLY LEU ILE GLY PHE SER LYS SER LEU ALA ARG GLU VAL
SEQRES 14 G 244 ALA SER ARG GLY ILE THR VAL ASN VAL VAL ALA PRO GLY
SEQRES 15 G 244 PHE ILE GLU THR ASP MET THR ARG ALA LEU SER ASP ASP
SEQRES 16 G 244 GLN ARG ALA GLY ILE LEU ALA GLN VAL PRO ALA GLY ARG
SEQRES 17 G 244 LEU GLY GLY ALA GLN GLU ILE ALA ASN ALA VAL ALA PHE
SEQRES 18 G 244 LEU ALA SER ASP GLU ALA ALA TYR ILE THR GLY GLU THR
SEQRES 19 G 244 LEU HIS VAL ASN GLY GLY MET TYR MET VAL
SEQRES 1 H 244 MET ASN PHE GLU GLY LYS ILE ALA LEU VAL THR GLY ALA
SEQRES 2 H 244 SER ARG GLY ILE GLY ARG ALA ILE ALA GLU THR LEU ALA
SEQRES 3 H 244 ALA ARG GLY ALA LYS VAL ILE GLY THR ALA THR SER GLU
SEQRES 4 H 244 ASN GLY ALA GLN ALA ILE SER ASP TYR LEU GLY ALA ASN
SEQRES 5 H 244 GLY LYS GLY LEU MET LEU ASN VAL THR ASP PRO ALA SER
SEQRES 6 H 244 ILE GLU SER VAL LEU GLU LYS ILE ARG ALA GLU PHE GLY
SEQRES 7 H 244 GLU VAL ASP ILE LEU VAL ASN ASN ALA GLY ILE THR ARG
SEQRES 8 H 244 ASP ASN LEU LEU MET ARG MET LYS ASP GLU GLU TRP ASN
SEQRES 9 H 244 ASP ILE ILE GLU THR ASN LEU SER SER VAL PHE ARG LEU
SEQRES 10 H 244 SER LYS ALA VAL MET ARG ALA MET MET LYS LYS ARG HIS
SEQRES 11 H 244 GLY ARG ILE ILE THR ILE GLY SER VAL VAL GLY THR MET
SEQRES 12 H 244 GLY ASN GLY GLY GLN ALA ASN TYR ALA ALA ALA LYS ALA
SEQRES 13 H 244 GLY LEU ILE GLY PHE SER LYS SER LEU ALA ARG GLU VAL
SEQRES 14 H 244 ALA SER ARG GLY ILE THR VAL ASN VAL VAL ALA PRO GLY
SEQRES 15 H 244 PHE ILE GLU THR ASP MET THR ARG ALA LEU SER ASP ASP
SEQRES 16 H 244 GLN ARG ALA GLY ILE LEU ALA GLN VAL PRO ALA GLY ARG
SEQRES 17 H 244 LEU GLY GLY ALA GLN GLU ILE ALA ASN ALA VAL ALA PHE
SEQRES 18 H 244 LEU ALA SER ASP GLU ALA ALA TYR ILE THR GLY GLU THR
SEQRES 19 H 244 LEU HIS VAL ASN GLY GLY MET TYR MET VAL
FORMUL 9 HOH *349(H2 O)
HELIX 1 1 ARG A 15 ARG A 28 1 14
HELIX 2 2 SER A 38 GLY A 50 1 13
HELIX 3 3 ASP A 62 PHE A 77 1 16
HELIX 4 4 LYS A 99 LEU A 111 1 13
HELIX 5 5 LEU A 111 ARG A 129 1 19
HELIX 6 6 ALA A 152 ALA A 170 1 19
HELIX 7 7 THR A 186 ALA A 191 1 6
HELIX 8 8 SER A 193 ALA A 202 1 10
HELIX 9 9 GLY A 211 SER A 224 1 14
HELIX 10 10 ASP A 225 ALA A 228 5 4
HELIX 11 11 ARG B 15 ARG B 28 1 14
HELIX 12 12 SER B 38 GLY B 50 1 13
HELIX 13 13 ASP B 62 PHE B 77 1 16
HELIX 14 14 LEU B 94 MET B 98 5 5
HELIX 15 15 LYS B 99 LEU B 111 1 13
HELIX 16 16 LEU B 111 ARG B 129 1 19
HELIX 17 17 GLN B 148 ALA B 170 1 23
HELIX 18 18 SER B 193 ALA B 202 1 10
HELIX 19 19 GLY B 211 SER B 224 1 14
HELIX 20 20 ASP B 225 ALA B 228 5 4
HELIX 21 21 ARG C 15 ARG C 28 1 14
HELIX 22 22 SER C 38 GLY C 50 1 13
HELIX 23 23 SER C 65 PHE C 77 1 13
HELIX 24 24 LEU C 94 MET C 98 5 5
HELIX 25 25 LYS C 99 LEU C 111 1 13
HELIX 26 26 LEU C 111 ARG C 129 1 19
HELIX 27 27 TYR C 151 ALA C 170 1 20
HELIX 28 28 ARG C 197 ALA C 202 1 6
HELIX 29 29 GLY C 211 SER C 224 1 14
HELIX 30 30 ASP C 225 ALA C 228 5 4
HELIX 31 31 ARG D 15 ARG D 28 1 14
HELIX 32 32 SER D 38 GLY D 50 1 13
HELIX 33 33 ASP D 62 PHE D 77 1 16
HELIX 34 34 LEU D 94 MET D 98 5 5
HELIX 35 35 LYS D 99 LEU D 111 1 13
HELIX 36 36 LEU D 111 ARG D 129 1 19
HELIX 37 37 TYR D 151 ALA D 170 1 20
HELIX 38 38 SER D 193 ALA D 202 1 10
HELIX 39 39 GLY D 211 SER D 224 1 14
HELIX 40 40 ASP D 225 ALA D 228 5 4
HELIX 41 41 ARG E 15 ARG E 28 1 14
HELIX 42 42 SER E 38 GLY E 50 1 13
HELIX 43 43 ASP E 62 PHE E 77 1 16
HELIX 44 44 LEU E 94 MET E 98 5 5
HELIX 45 45 LYS E 99 LEU E 111 1 13
HELIX 46 46 LEU E 111 ARG E 129 1 19
HELIX 47 47 TYR E 151 ALA E 170 1 20
HELIX 48 48 THR E 186 LEU E 192 1 7
HELIX 49 49 SER E 193 ALA E 202 1 10
HELIX 50 50 GLY E 211 SER E 224 1 14
HELIX 51 51 ASP E 225 ALA E 228 5 4
HELIX 52 52 GLY F 16 ARG F 28 1 13
HELIX 53 53 SER F 38 GLY F 50 1 13
HELIX 54 54 ASP F 62 PHE F 77 1 16
HELIX 55 55 LEU F 94 MET F 98 5 5
HELIX 56 56 LYS F 99 LEU F 111 1 13
HELIX 57 57 LEU F 111 ARG F 129 1 19
HELIX 58 58 ALA F 152 ALA F 170 1 19
HELIX 59 59 THR F 186 ALA F 191 1 6
HELIX 60 60 SER F 193 ALA F 202 1 10
HELIX 61 61 GLY F 211 SER F 224 1 14
HELIX 62 62 ASP F 225 ALA F 228 5 4
HELIX 63 63 ARG G 15 ARG G 28 1 14
HELIX 64 64 SER G 38 GLY G 50 1 13
HELIX 65 65 ASP G 62 PHE G 77 1 16
HELIX 66 66 LEU G 94 MET G 98 5 5
HELIX 67 67 LYS G 99 LEU G 111 1 13
HELIX 68 68 LEU G 111 ARG G 129 1 19
HELIX 69 69 TYR G 151 ALA G 170 1 20
HELIX 70 70 THR G 186 LEU G 192 1 7
HELIX 71 71 SER G 193 ALA G 202 1 10
HELIX 72 72 GLY G 211 SER G 224 1 14
HELIX 73 73 ASP G 225 ALA G 228 5 4
HELIX 74 74 ARG H 15 ARG H 28 1 14
HELIX 75 75 SER H 38 GLY H 50 1 13
HELIX 76 76 ASP H 62 PHE H 77 1 16
HELIX 77 77 LEU H 94 MET H 98 5 5
HELIX 78 78 LYS H 99 LEU H 111 1 13
HELIX 79 79 LEU H 111 ARG H 129 1 19
HELIX 80 80 TYR H 151 ALA H 170 1 20
HELIX 81 81 THR H 186 LEU H 192 1 7
HELIX 82 82 GLN H 196 ALA H 202 1 7
HELIX 83 83 GLY H 211 SER H 224 1 14
HELIX 84 84 ASP H 225 ALA H 228 5 4
SHEET 1 A 7 GLY A 53 MET A 57 0
SHEET 2 A 7 LYS A 31 ALA A 36 1 O VAL A 32 N LYS A 54
SHEET 3 A 7 ILE A 7 VAL A 10 1 N ALA A 8 O LYS A 31
SHEET 4 A 7 ILE A 82 ASN A 86 1 O ILE A 82 N LEU A 9
SHEET 5 A 7 GLY A 131 ILE A 136 1 O ARG A 132 N LEU A 83
SHEET 6 A 7 ILE A 174 PRO A 181 1 O THR A 175 N ILE A 133
SHEET 7 A 7 THR A 234 VAL A 237 1 N LEU A 235 O VAL A 178
SHEET 1 B 7 GLY B 53 MET B 57 0
SHEET 2 B 7 LYS B 31 ALA B 36 1 O VAL B 32 N LYS B 54
SHEET 3 B 7 ILE B 7 VAL B 10 1 O ALA B 8 N ILE B 33
SHEET 4 B 7 ILE B 82 ASN B 86 1 O ILE B 82 N LEU B 9
SHEET 5 B 7 GLY B 131 ILE B 136 1 O ARG B 132 N LEU B 83
SHEET 6 B 7 ILE B 174 PRO B 181 1 O THR B 175 N ILE B 133
SHEET 7 B 7 THR B 234 VAL B 237 1 N LEU B 235 O VAL B 178
SHEET 1 C 7 GLY C 53 MET C 57 0
SHEET 2 C 7 LYS C 31 ALA C 36 1 O VAL C 32 N LYS C 54
SHEET 3 C 7 ILE C 7 VAL C 10 1 O ALA C 8 N ILE C 33
SHEET 4 C 7 ILE C 82 ASN C 85 1 O ILE C 82 N LEU C 9
SHEET 5 C 7 GLY C 131 ILE C 136 1 O ARG C 132 N LEU C 83
SHEET 6 C 7 ILE C 174 PRO C 181 1 O THR C 175 N ILE C 133
SHEET 7 C 7 THR C 234 VAL C 237 1 N LEU C 235 O VAL C 178
SHEET 1 D 7 GLY D 53 MET D 57 0
SHEET 2 D 7 LYS D 31 ALA D 36 1 O VAL D 32 N LYS D 54
SHEET 3 D 7 ILE D 7 VAL D 10 1 N ALA D 8 O LYS D 31
SHEET 4 D 7 ILE D 82 ASN D 85 1 O ILE D 82 N LEU D 9
SHEET 5 D 7 GLY D 131 ILE D 136 1 O ARG D 132 N LEU D 83
SHEET 6 D 7 ILE D 174 PRO D 181 1 O THR D 175 N ILE D 133
SHEET 7 D 7 THR D 234 VAL D 237 1 N LEU D 235 O VAL D 178
SHEET 1 E 7 GLY E 53 MET E 57 0
SHEET 2 E 7 LYS E 31 ALA E 36 1 O VAL E 32 N LYS E 54
SHEET 3 E 7 ILE E 7 VAL E 10 1 N ALA E 8 O LYS E 31
SHEET 4 E 7 ILE E 82 ASN E 86 1 O ILE E 82 N LEU E 9
SHEET 5 E 7 GLY E 131 ILE E 136 1 O ARG E 132 N LEU E 83
SHEET 6 E 7 ILE E 174 PRO E 181 1 O THR E 175 N ILE E 133
SHEET 7 E 7 THR E 234 VAL E 237 1 N LEU E 235 O VAL E 178
SHEET 1 F 7 GLY F 53 MET F 57 0
SHEET 2 F 7 LYS F 31 ALA F 36 1 O VAL F 32 N LYS F 54
SHEET 3 F 7 ILE F 7 VAL F 10 1 N ALA F 8 O LYS F 31
SHEET 4 F 7 ILE F 82 ASN F 86 1 O ILE F 82 N LEU F 9
SHEET 5 F 7 GLY F 131 ILE F 136 1 O ARG F 132 N LEU F 83
SHEET 6 F 7 ILE F 174 PRO F 181 1 O THR F 175 N ILE F 133
SHEET 7 F 7 THR F 234 VAL F 237 1 N LEU F 235 O VAL F 178
SHEET 1 G 7 GLY G 53 MET G 57 0
SHEET 2 G 7 LYS G 31 ALA G 36 1 O VAL G 32 N LYS G 54
SHEET 3 G 7 ILE G 7 VAL G 10 1 N ALA G 8 O LYS G 31
SHEET 4 G 7 ILE G 82 ASN G 86 1 O ILE G 82 N LEU G 9
SHEET 5 G 7 GLY G 131 ILE G 136 1 O ARG G 132 N LEU G 83
SHEET 6 G 7 ILE G 174 PRO G 181 1 O THR G 175 N ILE G 133
SHEET 7 G 7 THR G 234 VAL G 237 1 N LEU G 235 O VAL G 178
SHEET 1 H 7 GLY H 53 MET H 57 0
SHEET 2 H 7 LYS H 31 ALA H 36 1 O VAL H 32 N LYS H 54
SHEET 3 H 7 ILE H 7 VAL H 10 1 O ALA H 8 N ILE H 33
SHEET 4 H 7 ILE H 82 ASN H 86 1 O ILE H 82 N LEU H 9
SHEET 5 H 7 GLY H 131 ILE H 136 1 O ARG H 132 N LEU H 83
SHEET 6 H 7 ILE H 174 PRO H 181 1 O THR H 175 N ILE H 133
SHEET 7 H 7 THR H 234 VAL H 237 1 N LEU H 235 O VAL H 178
CRYST1 61.700 120.100 131.100 90.00 90.50 90.00 P 1 21 1 16
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 0.016207 0.000000 0.000141 0.00000
SCALE2 0.000000 0.008326 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007628 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
