HEADER OXIDOREDUCTASE 04-FEB-05 1YRL
TITLE ESCHERICHIA COLI KETOL-ACID REDUCTOISOMERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KETOL-ACID REDUCTOISOMERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ACETOHYDROXY-ACID ISOMEROREDUCTASE, ALPHA-KETO-BETA-
COMPND 5 HYDROXYLACIL REDUCTOISOMERASE;
COMPND 6 EC: 1.1.1.86;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ILVC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET30
KEYWDS BRANCHED-CHAIN AMINO ACID BIOSYNTHESIS, KNOTTED PROTEIN,
KEYWDS 2 REDUCTOISOMERASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.TYAGI,S.DUQUERROY,J.NAVAZA,L.W.GUDDAT,R.G.DUGGLEBY
REVDAT 5 25-OCT-23 1YRL 1 REMARK
REVDAT 4 11-OCT-17 1YRL 1 REMARK
REVDAT 3 24-FEB-09 1YRL 1 VERSN
REVDAT 2 24-JAN-06 1YRL 1 JRNL
REVDAT 1 11-OCT-05 1YRL 0
JRNL AUTH R.TYAGI,S.DUQUERROY,J.NAVAZA,L.W.GUDDAT,R.G.DUGGLEBY
JRNL TITL THE CRYSTAL STRUCTURE OF A BACTERIAL CLASS II KETOL-ACID
JRNL TITL 2 REDUCTOISOMERASE: DOMAIN CONSERVATION AND EVOLUTION
JRNL REF PROTEIN SCI. V. 14 3089 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 16322583
JRNL DOI 10.1110/PS.051791305
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 32.48
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) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 106858
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) : 0.223
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 10702
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3214
REMARK 3 BIN FREE R VALUE : 0.3527
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1341
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14443
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 45
REMARK 3 SOLVENT ATOMS : 416
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.53800
REMARK 3 B22 (A**2) : 3.53800
REMARK 3 B33 (A**2) : -7.07700
REMARK 3 B12 (A**2) : -6.85400
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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) : 1.220
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 1YRL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031850.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 9.0
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 FR-E
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : DOUBLE FOCUSSED MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR V.1.3.5
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR V. 1.35
REMARK 200 (MSC/RIGAKU)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106858
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 32.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.600
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.07400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.9000
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) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.30000
REMARK 200 R SYM FOR SHELL (I) : 0.30000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1QMG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM BICINE, PH
REMARK 280 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 59.42650
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 59.42650
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.42650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE TETRAMER CAN BE ASSEMBLED BY COMBINATION OF THE A AND D
REMARK 300 CHAINS WITH THE B AND C CHAINS GENERATED BY THE SYMMETRY OPERATOR 1-
REMARK 300 Y,1+X-Y,Z.
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 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 490
REMARK 465 GLY A 491
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLY B 37
REMARK 465 LYS B 38
REMARK 465 LYS B 39
REMARK 465 VAL B 40
REMARK 465 VAL B 41
REMARK 465 ILE B 42
REMARK 465 VAL B 43
REMARK 465 GLY B 44
REMARK 465 CYS B 45
REMARK 465 GLY B 46
REMARK 465 ALA B 47
REMARK 465 GLN B 48
REMARK 465 GLY B 49
REMARK 465 LEU B 50
REMARK 465 ASN B 51
REMARK 465 GLN B 52
REMARK 465 GLY B 53
REMARK 465 LEU B 54
REMARK 465 ASN B 55
REMARK 465 MET B 56
REMARK 465 ARG B 57
REMARK 465 ASP B 58
REMARK 465 SER B 59
REMARK 465 GLY B 60
REMARK 465 LEU B 61
REMARK 465 ASP B 62
REMARK 465 ILE B 63
REMARK 465 SER B 64
REMARK 465 TYR B 65
REMARK 465 ALA B 66
REMARK 465 LEU B 67
REMARK 465 ARG B 68
REMARK 465 LYS B 69
REMARK 465 GLU B 70
REMARK 465 ALA B 71
REMARK 465 ILE B 72
REMARK 465 ALA B 73
REMARK 465 GLU B 74
REMARK 465 LYS B 75
REMARK 465 ARG B 76
REMARK 465 ALA B 77
REMARK 465 SER B 78
REMARK 465 TRP B 79
REMARK 465 ARG B 80
REMARK 465 LYS B 81
REMARK 465 ALA B 82
REMARK 465 THR B 83
REMARK 465 GLU B 84
REMARK 465 ASN B 85
REMARK 465 GLY B 86
REMARK 465 PHE B 87
REMARK 465 LYS B 88
REMARK 465 VAL B 89
REMARK 465 GLY B 90
REMARK 465 THR B 91
REMARK 465 VAL B 489
REMARK 465 ALA B 490
REMARK 465 GLY B 491
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 ALA C 490
REMARK 465 GLY C 491
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLY D 44
REMARK 465 CYS D 45
REMARK 465 GLY D 46
REMARK 465 ALA D 47
REMARK 465 GLN D 48
REMARK 465 GLY D 49
REMARK 465 LYS D 75
REMARK 465 ARG D 76
REMARK 465 ALA D 77
REMARK 465 SER D 78
REMARK 465 TRP D 79
REMARK 465 ARG D 80
REMARK 465 LYS D 81
REMARK 465 ALA D 82
REMARK 465 THR D 83
REMARK 465 GLU D 84
REMARK 465 ASN D 85
REMARK 465 ALA D 490
REMARK 465 GLY D 491
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 LYS A 145 CG CD CE NZ
REMARK 470 GLU B 93 CG CD OE1 OE2
REMARK 470 GLU B 94 CG CD OE1 OE2
REMARK 470 LEU B 95 CG CD1 CD2
REMARK 470 ILE B 96 CG1 CG2 CD1
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 GLU B 163 CG CD OE1 OE2
REMARK 470 PHE B 169 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 25 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 69 CG CD CE NZ
REMARK 470 LYS C 81 CG CD CE NZ
REMARK 470 LYS C 145 CG CD CE NZ
REMARK 470 ARG D 25 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 55 CG OD1 ND2
REMARK 470 SER D 59 OG
REMARK 470 LEU D 67 CG CD1 CD2
REMARK 470 ARG D 68 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 69 CG CD CE NZ
REMARK 470 ILE D 72 CG1 CG2 CD1
REMARK 470 LYS D 88 CG CD CE NZ
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 CYS A 20 94.86 -167.24
REMARK 500 CYS A 45 68.05 -104.57
REMARK 500 LYS A 123 -172.74 -67.14
REMARK 500 PHE A 169 -147.20 -117.73
REMARK 500 SER A 208 -149.33 -117.43
REMARK 500 THR A 223 -79.99 -119.79
REMARK 500 CYS A 226 -51.31 -133.92
REMARK 500 SER A 390 11.65 -140.42
REMARK 500 LEU A 391 -50.06 -161.50
REMARK 500 LYS A 404 52.30 -157.40
REMARK 500 ARG A 405 -158.70 52.01
REMARK 500 TYR A 426 1.08 -67.12
REMARK 500 ALA A 488 71.52 -113.67
REMARK 500 CYS B 20 109.05 -169.80
REMARK 500 GLU B 27 9.45 -69.54
REMARK 500 LYS B 123 -171.65 -67.29
REMARK 500 PHE B 169 -139.01 -79.44
REMARK 500 PRO B 179 -72.86 -50.42
REMARK 500 GLU B 180 27.10 -70.05
REMARK 500 ASN B 181 56.25 -148.57
REMARK 500 ASP B 182 59.91 -153.38
REMARK 500 SER B 208 -148.63 -116.10
REMARK 500 THR B 223 -81.61 -125.76
REMARK 500 CYS B 226 -54.70 -131.57
REMARK 500 THR B 245 125.13 -15.28
REMARK 500 ASP B 324 30.13 39.53
REMARK 500 LYS B 325 -73.56 -43.84
REMARK 500 THR B 341 68.52 -118.17
REMARK 500 LEU B 391 -50.62 -163.16
REMARK 500 LYS B 404 53.92 -157.79
REMARK 500 ARG B 405 -157.96 50.23
REMARK 500 SER B 414 170.20 -59.21
REMARK 500 LEU B 439 175.92 -52.80
REMARK 500 LEU C 10 -68.23 -25.26
REMARK 500 CYS C 20 84.96 175.74
REMARK 500 PHE C 28 53.09 -119.16
REMARK 500 LYS C 75 62.40 24.03
REMARK 500 ARG C 76 -177.39 -59.64
REMARK 500 ALA C 82 -70.02 -63.50
REMARK 500 LEU C 105 65.24 -101.34
REMARK 500 ARG C 116 16.01 -69.44
REMARK 500 THR C 117 -22.77 -143.84
REMARK 500 LYS C 123 -171.69 -66.67
REMARK 500 HIS C 132 133.81 -177.79
REMARK 500 PHE C 169 -152.17 -120.00
REMARK 500 PRO C 183 -81.99 -46.21
REMARK 500 LYS C 184 13.20 -64.95
REMARK 500 SER C 208 -149.49 -117.34
REMARK 500 THR C 223 -129.16 -107.31
REMARK 500 CYS C 226 -57.75 -131.20
REMARK 500
REMARK 500 THIS ENTRY HAS 85 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 SO4 A 4121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4122
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 4123
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 4124
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 4125
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4126
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4127
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4128
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 4129
DBREF 1YRL A 1 491 UNP P05793 ILVC_ECOLI 0 490
DBREF 1YRL B 1 491 UNP P05793 ILVC_ECOLI 0 490
DBREF 1YRL C 1 491 UNP P05793 ILVC_ECOLI 0 490
DBREF 1YRL D 1 491 UNP P05793 ILVC_ECOLI 0 490
SEQRES 1 A 491 MET ALA ASN TYR PHE ASN THR LEU ASN LEU ARG GLN GLN
SEQRES 2 A 491 LEU ALA GLN LEU GLY LYS CYS ARG PHE MET GLY ARG ASP
SEQRES 3 A 491 GLU PHE ALA ASP GLY ALA SER TYR LEU GLN GLY LYS LYS
SEQRES 4 A 491 VAL VAL ILE VAL GLY CYS GLY ALA GLN GLY LEU ASN GLN
SEQRES 5 A 491 GLY LEU ASN MET ARG ASP SER GLY LEU ASP ILE SER TYR
SEQRES 6 A 491 ALA LEU ARG LYS GLU ALA ILE ALA GLU LYS ARG ALA SER
SEQRES 7 A 491 TRP ARG LYS ALA THR GLU ASN GLY PHE LYS VAL GLY THR
SEQRES 8 A 491 TYR GLU GLU LEU ILE PRO GLN ALA ASP LEU VAL ILE ASN
SEQRES 9 A 491 LEU THR PRO ASP LYS GLN HIS SER ASP VAL VAL ARG THR
SEQRES 10 A 491 VAL GLN PRO LEU MET LYS ASP GLY ALA ALA LEU GLY TYR
SEQRES 11 A 491 SER HIS GLY PHE ASN ILE VAL GLU VAL GLY GLU GLN ILE
SEQRES 12 A 491 ARG LYS ASP ILE THR VAL VAL MET VAL ALA PRO LYS CYS
SEQRES 13 A 491 PRO GLY THR GLU VAL ARG GLU GLU TYR LYS ARG GLY PHE
SEQRES 14 A 491 GLY VAL PRO THR LEU ILE ALA VAL HIS PRO GLU ASN ASP
SEQRES 15 A 491 PRO LYS GLY GLU GLY MET ALA ILE ALA LYS ALA TRP ALA
SEQRES 16 A 491 ALA ALA THR GLY GLY HIS ARG ALA GLY VAL LEU GLU SER
SEQRES 17 A 491 SER PHE VAL ALA GLU VAL LYS SER ASP LEU MET GLY GLU
SEQRES 18 A 491 GLN THR ILE LEU CYS GLY MET LEU GLN ALA GLY SER LEU
SEQRES 19 A 491 LEU CYS PHE ASP LYS LEU VAL GLU GLU GLY THR ASP PRO
SEQRES 20 A 491 ALA TYR ALA GLU LYS LEU ILE GLN PHE GLY TRP GLU THR
SEQRES 21 A 491 ILE THR GLU ALA LEU LYS GLN GLY GLY ILE THR LEU MET
SEQRES 22 A 491 MET ASP ARG LEU SER ASN PRO ALA LYS LEU ARG ALA TYR
SEQRES 23 A 491 ALA LEU SER GLU GLN LEU LYS GLU ILE MET ALA PRO LEU
SEQRES 24 A 491 PHE GLN LYS HIS MET ASP ASP ILE ILE SER GLY GLU PHE
SEQRES 25 A 491 SER SER GLY MET MET ALA ASP TRP ALA ASN ASP ASP LYS
SEQRES 26 A 491 LYS LEU LEU THR TRP ARG GLU GLU THR GLY LYS THR ALA
SEQRES 27 A 491 PHE GLU THR ALA PRO GLN TYR GLU GLY LYS ILE GLY GLU
SEQRES 28 A 491 GLN GLU TYR PHE ASP LYS GLY VAL LEU MET ILE ALA MET
SEQRES 29 A 491 VAL LYS ALA GLY VAL GLU LEU ALA PHE GLU THR MET VAL
SEQRES 30 A 491 ASP SER GLY ILE ILE GLU GLU SER ALA TYR TYR GLU SER
SEQRES 31 A 491 LEU HIS GLU LEU PRO LEU ILE ALA ASN THR ILE ALA ARG
SEQRES 32 A 491 LYS ARG LEU TYR GLU MET ASN VAL VAL ILE SER ASP THR
SEQRES 33 A 491 ALA GLU TYR GLY ASN TYR LEU PHE SER TYR ALA CYS VAL
SEQRES 34 A 491 PRO LEU LEU LYS PRO PHE MET ALA GLU LEU GLN PRO GLY
SEQRES 35 A 491 ASP LEU GLY LYS ALA ILE PRO GLU GLY ALA VAL ASP ASN
SEQRES 36 A 491 GLY GLN LEU ARG ASP VAL ASN GLU ALA ILE ARG SER HIS
SEQRES 37 A 491 ALA ILE GLU GLN VAL GLY LYS LYS LEU ARG GLY TYR MET
SEQRES 38 A 491 THR ASP MET LYS ARG ILE ALA VAL ALA GLY
SEQRES 1 B 491 MET ALA ASN TYR PHE ASN THR LEU ASN LEU ARG GLN GLN
SEQRES 2 B 491 LEU ALA GLN LEU GLY LYS CYS ARG PHE MET GLY ARG ASP
SEQRES 3 B 491 GLU PHE ALA ASP GLY ALA SER TYR LEU GLN GLY LYS LYS
SEQRES 4 B 491 VAL VAL ILE VAL GLY CYS GLY ALA GLN GLY LEU ASN GLN
SEQRES 5 B 491 GLY LEU ASN MET ARG ASP SER GLY LEU ASP ILE SER TYR
SEQRES 6 B 491 ALA LEU ARG LYS GLU ALA ILE ALA GLU LYS ARG ALA SER
SEQRES 7 B 491 TRP ARG LYS ALA THR GLU ASN GLY PHE LYS VAL GLY THR
SEQRES 8 B 491 TYR GLU GLU LEU ILE PRO GLN ALA ASP LEU VAL ILE ASN
SEQRES 9 B 491 LEU THR PRO ASP LYS GLN HIS SER ASP VAL VAL ARG THR
SEQRES 10 B 491 VAL GLN PRO LEU MET LYS ASP GLY ALA ALA LEU GLY TYR
SEQRES 11 B 491 SER HIS GLY PHE ASN ILE VAL GLU VAL GLY GLU GLN ILE
SEQRES 12 B 491 ARG LYS ASP ILE THR VAL VAL MET VAL ALA PRO LYS CYS
SEQRES 13 B 491 PRO GLY THR GLU VAL ARG GLU GLU TYR LYS ARG GLY PHE
SEQRES 14 B 491 GLY VAL PRO THR LEU ILE ALA VAL HIS PRO GLU ASN ASP
SEQRES 15 B 491 PRO LYS GLY GLU GLY MET ALA ILE ALA LYS ALA TRP ALA
SEQRES 16 B 491 ALA ALA THR GLY GLY HIS ARG ALA GLY VAL LEU GLU SER
SEQRES 17 B 491 SER PHE VAL ALA GLU VAL LYS SER ASP LEU MET GLY GLU
SEQRES 18 B 491 GLN THR ILE LEU CYS GLY MET LEU GLN ALA GLY SER LEU
SEQRES 19 B 491 LEU CYS PHE ASP LYS LEU VAL GLU GLU GLY THR ASP PRO
SEQRES 20 B 491 ALA TYR ALA GLU LYS LEU ILE GLN PHE GLY TRP GLU THR
SEQRES 21 B 491 ILE THR GLU ALA LEU LYS GLN GLY GLY ILE THR LEU MET
SEQRES 22 B 491 MET ASP ARG LEU SER ASN PRO ALA LYS LEU ARG ALA TYR
SEQRES 23 B 491 ALA LEU SER GLU GLN LEU LYS GLU ILE MET ALA PRO LEU
SEQRES 24 B 491 PHE GLN LYS HIS MET ASP ASP ILE ILE SER GLY GLU PHE
SEQRES 25 B 491 SER SER GLY MET MET ALA ASP TRP ALA ASN ASP ASP LYS
SEQRES 26 B 491 LYS LEU LEU THR TRP ARG GLU GLU THR GLY LYS THR ALA
SEQRES 27 B 491 PHE GLU THR ALA PRO GLN TYR GLU GLY LYS ILE GLY GLU
SEQRES 28 B 491 GLN GLU TYR PHE ASP LYS GLY VAL LEU MET ILE ALA MET
SEQRES 29 B 491 VAL LYS ALA GLY VAL GLU LEU ALA PHE GLU THR MET VAL
SEQRES 30 B 491 ASP SER GLY ILE ILE GLU GLU SER ALA TYR TYR GLU SER
SEQRES 31 B 491 LEU HIS GLU LEU PRO LEU ILE ALA ASN THR ILE ALA ARG
SEQRES 32 B 491 LYS ARG LEU TYR GLU MET ASN VAL VAL ILE SER ASP THR
SEQRES 33 B 491 ALA GLU TYR GLY ASN TYR LEU PHE SER TYR ALA CYS VAL
SEQRES 34 B 491 PRO LEU LEU LYS PRO PHE MET ALA GLU LEU GLN PRO GLY
SEQRES 35 B 491 ASP LEU GLY LYS ALA ILE PRO GLU GLY ALA VAL ASP ASN
SEQRES 36 B 491 GLY GLN LEU ARG ASP VAL ASN GLU ALA ILE ARG SER HIS
SEQRES 37 B 491 ALA ILE GLU GLN VAL GLY LYS LYS LEU ARG GLY TYR MET
SEQRES 38 B 491 THR ASP MET LYS ARG ILE ALA VAL ALA GLY
SEQRES 1 C 491 MET ALA ASN TYR PHE ASN THR LEU ASN LEU ARG GLN GLN
SEQRES 2 C 491 LEU ALA GLN LEU GLY LYS CYS ARG PHE MET GLY ARG ASP
SEQRES 3 C 491 GLU PHE ALA ASP GLY ALA SER TYR LEU GLN GLY LYS LYS
SEQRES 4 C 491 VAL VAL ILE VAL GLY CYS GLY ALA GLN GLY LEU ASN GLN
SEQRES 5 C 491 GLY LEU ASN MET ARG ASP SER GLY LEU ASP ILE SER TYR
SEQRES 6 C 491 ALA LEU ARG LYS GLU ALA ILE ALA GLU LYS ARG ALA SER
SEQRES 7 C 491 TRP ARG LYS ALA THR GLU ASN GLY PHE LYS VAL GLY THR
SEQRES 8 C 491 TYR GLU GLU LEU ILE PRO GLN ALA ASP LEU VAL ILE ASN
SEQRES 9 C 491 LEU THR PRO ASP LYS GLN HIS SER ASP VAL VAL ARG THR
SEQRES 10 C 491 VAL GLN PRO LEU MET LYS ASP GLY ALA ALA LEU GLY TYR
SEQRES 11 C 491 SER HIS GLY PHE ASN ILE VAL GLU VAL GLY GLU GLN ILE
SEQRES 12 C 491 ARG LYS ASP ILE THR VAL VAL MET VAL ALA PRO LYS CYS
SEQRES 13 C 491 PRO GLY THR GLU VAL ARG GLU GLU TYR LYS ARG GLY PHE
SEQRES 14 C 491 GLY VAL PRO THR LEU ILE ALA VAL HIS PRO GLU ASN ASP
SEQRES 15 C 491 PRO LYS GLY GLU GLY MET ALA ILE ALA LYS ALA TRP ALA
SEQRES 16 C 491 ALA ALA THR GLY GLY HIS ARG ALA GLY VAL LEU GLU SER
SEQRES 17 C 491 SER PHE VAL ALA GLU VAL LYS SER ASP LEU MET GLY GLU
SEQRES 18 C 491 GLN THR ILE LEU CYS GLY MET LEU GLN ALA GLY SER LEU
SEQRES 19 C 491 LEU CYS PHE ASP LYS LEU VAL GLU GLU GLY THR ASP PRO
SEQRES 20 C 491 ALA TYR ALA GLU LYS LEU ILE GLN PHE GLY TRP GLU THR
SEQRES 21 C 491 ILE THR GLU ALA LEU LYS GLN GLY GLY ILE THR LEU MET
SEQRES 22 C 491 MET ASP ARG LEU SER ASN PRO ALA LYS LEU ARG ALA TYR
SEQRES 23 C 491 ALA LEU SER GLU GLN LEU LYS GLU ILE MET ALA PRO LEU
SEQRES 24 C 491 PHE GLN LYS HIS MET ASP ASP ILE ILE SER GLY GLU PHE
SEQRES 25 C 491 SER SER GLY MET MET ALA ASP TRP ALA ASN ASP ASP LYS
SEQRES 26 C 491 LYS LEU LEU THR TRP ARG GLU GLU THR GLY LYS THR ALA
SEQRES 27 C 491 PHE GLU THR ALA PRO GLN TYR GLU GLY LYS ILE GLY GLU
SEQRES 28 C 491 GLN GLU TYR PHE ASP LYS GLY VAL LEU MET ILE ALA MET
SEQRES 29 C 491 VAL LYS ALA GLY VAL GLU LEU ALA PHE GLU THR MET VAL
SEQRES 30 C 491 ASP SER GLY ILE ILE GLU GLU SER ALA TYR TYR GLU SER
SEQRES 31 C 491 LEU HIS GLU LEU PRO LEU ILE ALA ASN THR ILE ALA ARG
SEQRES 32 C 491 LYS ARG LEU TYR GLU MET ASN VAL VAL ILE SER ASP THR
SEQRES 33 C 491 ALA GLU TYR GLY ASN TYR LEU PHE SER TYR ALA CYS VAL
SEQRES 34 C 491 PRO LEU LEU LYS PRO PHE MET ALA GLU LEU GLN PRO GLY
SEQRES 35 C 491 ASP LEU GLY LYS ALA ILE PRO GLU GLY ALA VAL ASP ASN
SEQRES 36 C 491 GLY GLN LEU ARG ASP VAL ASN GLU ALA ILE ARG SER HIS
SEQRES 37 C 491 ALA ILE GLU GLN VAL GLY LYS LYS LEU ARG GLY TYR MET
SEQRES 38 C 491 THR ASP MET LYS ARG ILE ALA VAL ALA GLY
SEQRES 1 D 491 MET ALA ASN TYR PHE ASN THR LEU ASN LEU ARG GLN GLN
SEQRES 2 D 491 LEU ALA GLN LEU GLY LYS CYS ARG PHE MET GLY ARG ASP
SEQRES 3 D 491 GLU PHE ALA ASP GLY ALA SER TYR LEU GLN GLY LYS LYS
SEQRES 4 D 491 VAL VAL ILE VAL GLY CYS GLY ALA GLN GLY LEU ASN GLN
SEQRES 5 D 491 GLY LEU ASN MET ARG ASP SER GLY LEU ASP ILE SER TYR
SEQRES 6 D 491 ALA LEU ARG LYS GLU ALA ILE ALA GLU LYS ARG ALA SER
SEQRES 7 D 491 TRP ARG LYS ALA THR GLU ASN GLY PHE LYS VAL GLY THR
SEQRES 8 D 491 TYR GLU GLU LEU ILE PRO GLN ALA ASP LEU VAL ILE ASN
SEQRES 9 D 491 LEU THR PRO ASP LYS GLN HIS SER ASP VAL VAL ARG THR
SEQRES 10 D 491 VAL GLN PRO LEU MET LYS ASP GLY ALA ALA LEU GLY TYR
SEQRES 11 D 491 SER HIS GLY PHE ASN ILE VAL GLU VAL GLY GLU GLN ILE
SEQRES 12 D 491 ARG LYS ASP ILE THR VAL VAL MET VAL ALA PRO LYS CYS
SEQRES 13 D 491 PRO GLY THR GLU VAL ARG GLU GLU TYR LYS ARG GLY PHE
SEQRES 14 D 491 GLY VAL PRO THR LEU ILE ALA VAL HIS PRO GLU ASN ASP
SEQRES 15 D 491 PRO LYS GLY GLU GLY MET ALA ILE ALA LYS ALA TRP ALA
SEQRES 16 D 491 ALA ALA THR GLY GLY HIS ARG ALA GLY VAL LEU GLU SER
SEQRES 17 D 491 SER PHE VAL ALA GLU VAL LYS SER ASP LEU MET GLY GLU
SEQRES 18 D 491 GLN THR ILE LEU CYS GLY MET LEU GLN ALA GLY SER LEU
SEQRES 19 D 491 LEU CYS PHE ASP LYS LEU VAL GLU GLU GLY THR ASP PRO
SEQRES 20 D 491 ALA TYR ALA GLU LYS LEU ILE GLN PHE GLY TRP GLU THR
SEQRES 21 D 491 ILE THR GLU ALA LEU LYS GLN GLY GLY ILE THR LEU MET
SEQRES 22 D 491 MET ASP ARG LEU SER ASN PRO ALA LYS LEU ARG ALA TYR
SEQRES 23 D 491 ALA LEU SER GLU GLN LEU LYS GLU ILE MET ALA PRO LEU
SEQRES 24 D 491 PHE GLN LYS HIS MET ASP ASP ILE ILE SER GLY GLU PHE
SEQRES 25 D 491 SER SER GLY MET MET ALA ASP TRP ALA ASN ASP ASP LYS
SEQRES 26 D 491 LYS LEU LEU THR TRP ARG GLU GLU THR GLY LYS THR ALA
SEQRES 27 D 491 PHE GLU THR ALA PRO GLN TYR GLU GLY LYS ILE GLY GLU
SEQRES 28 D 491 GLN GLU TYR PHE ASP LYS GLY VAL LEU MET ILE ALA MET
SEQRES 29 D 491 VAL LYS ALA GLY VAL GLU LEU ALA PHE GLU THR MET VAL
SEQRES 30 D 491 ASP SER GLY ILE ILE GLU GLU SER ALA TYR TYR GLU SER
SEQRES 31 D 491 LEU HIS GLU LEU PRO LEU ILE ALA ASN THR ILE ALA ARG
SEQRES 32 D 491 LYS ARG LEU TYR GLU MET ASN VAL VAL ILE SER ASP THR
SEQRES 33 D 491 ALA GLU TYR GLY ASN TYR LEU PHE SER TYR ALA CYS VAL
SEQRES 34 D 491 PRO LEU LEU LYS PRO PHE MET ALA GLU LEU GLN PRO GLY
SEQRES 35 D 491 ASP LEU GLY LYS ALA ILE PRO GLU GLY ALA VAL ASP ASN
SEQRES 36 D 491 GLY GLN LEU ARG ASP VAL ASN GLU ALA ILE ARG SER HIS
SEQRES 37 D 491 ALA ILE GLU GLN VAL GLY LYS LYS LEU ARG GLY TYR MET
SEQRES 38 D 491 THR ASP MET LYS ARG ILE ALA VAL ALA GLY
HET SO4 A4121 5
HET SO4 A4122 5
HET SO4 A4127 5
HET SO4 A4128 5
HET SO4 B4126 5
HET SO4 C4125 5
HET SO4 D4123 5
HET SO4 D4124 5
HET SO4 D4129 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 9(O4 S 2-)
FORMUL 14 HOH *416(H2 O)
HELIX 1 1 TYR A 4 LEU A 8 5 5
HELIX 2 2 ASN A 9 GLY A 18 1 10
HELIX 3 3 GLY A 24 ALA A 29 5 6
HELIX 4 4 ALA A 32 GLN A 36 5 5
HELIX 5 5 GLY A 46 SER A 59 1 14
HELIX 6 6 ARG A 68 GLU A 74 1 7
HELIX 7 7 ARG A 76 ASN A 85 1 10
HELIX 8 8 TYR A 92 ILE A 96 1 5
HELIX 9 9 PRO A 97 ALA A 99 5 3
HELIX 10 10 PRO A 107 MET A 122 1 16
HELIX 11 11 GLY A 133 GLU A 138 1 6
HELIX 12 12 THR A 159 ARG A 167 1 9
HELIX 13 13 PRO A 179 ASP A 182 5 4
HELIX 14 14 GLU A 186 GLY A 199 1 14
HELIX 15 15 GLY A 199 GLY A 204 1 6
HELIX 16 16 SER A 209 THR A 223 1 15
HELIX 17 17 CYS A 226 GLU A 243 1 18
HELIX 18 18 ASP A 246 ARG A 276 1 31
HELIX 19 19 SER A 278 SER A 309 1 32
HELIX 20 20 GLY A 310 ALA A 321 1 12
HELIX 21 21 ASP A 324 GLY A 335 1 12
HELIX 22 22 THR A 337 ALA A 342 1 6
HELIX 23 23 GLY A 350 LYS A 357 1 8
HELIX 24 24 GLY A 358 ASP A 378 1 21
HELIX 25 25 ILE A 382 SER A 390 1 9
HELIX 26 26 GLU A 393 ILE A 413 1 21
HELIX 27 27 SER A 414 GLU A 438 1 25
HELIX 28 28 ASP A 454 HIS A 468 1 15
HELIX 29 29 HIS A 468 ILE A 487 1 20
HELIX 30 30 TYR B 4 LEU B 8 5 5
HELIX 31 31 ASN B 9 GLY B 18 1 10
HELIX 32 32 GLY B 24 ALA B 29 5 6
HELIX 33 33 ASP B 30 GLN B 36 5 7
HELIX 34 34 HIS B 111 MET B 122 1 12
HELIX 35 35 GLY B 133 GLU B 138 1 6
HELIX 36 36 THR B 159 GLY B 168 1 10
HELIX 37 37 GLU B 186 ALA B 197 1 12
HELIX 38 38 THR B 198 ALA B 203 5 6
HELIX 39 39 SER B 209 GLN B 222 1 14
HELIX 40 40 CYS B 226 GLU B 243 1 18
HELIX 41 41 ASP B 246 ARG B 276 1 31
HELIX 42 42 SER B 278 GLY B 310 1 33
HELIX 43 43 GLY B 310 TRP B 320 1 11
HELIX 44 44 ASP B 324 LYS B 336 1 13
HELIX 45 45 THR B 337 ALA B 342 5 6
HELIX 46 46 GLY B 350 LYS B 357 1 8
HELIX 47 47 GLY B 358 ASP B 378 1 21
HELIX 48 48 ILE B 382 TYR B 388 1 7
HELIX 49 49 GLU B 393 ILE B 413 1 21
HELIX 50 50 SER B 414 GLU B 438 1 25
HELIX 51 51 ASP B 454 SER B 467 1 14
HELIX 52 52 HIS B 468 ILE B 487 1 20
HELIX 53 53 TYR C 4 LEU C 8 5 5
HELIX 54 54 ASN C 9 GLY C 18 1 10
HELIX 55 55 GLY C 24 ALA C 29 5 6
HELIX 56 56 GLY C 46 LEU C 61 1 16
HELIX 57 57 ARG C 68 GLU C 74 1 7
HELIX 58 58 ARG C 76 ASN C 85 1 10
HELIX 59 59 TYR C 92 ILE C 96 1 5
HELIX 60 60 PRO C 107 MET C 122 1 16
HELIX 61 61 GLY C 133 VAL C 139 1 7
HELIX 62 62 THR C 159 ARG C 167 1 9
HELIX 63 63 PRO C 179 ASP C 182 5 4
HELIX 64 64 GLU C 186 THR C 198 1 13
HELIX 65 65 GLY C 199 ALA C 203 5 5
HELIX 66 66 SER C 209 THR C 223 1 15
HELIX 67 67 CYS C 226 GLU C 243 1 18
HELIX 68 68 ASP C 246 ARG C 276 1 31
HELIX 69 69 SER C 278 GLY C 310 1 33
HELIX 70 70 GLY C 310 ASN C 322 1 13
HELIX 71 71 ASP C 324 GLY C 335 1 12
HELIX 72 72 THR C 337 ALA C 342 1 6
HELIX 73 73 GLY C 350 LYS C 357 1 8
HELIX 74 74 GLY C 358 ASP C 378 1 21
HELIX 75 75 ILE C 382 SER C 390 1 9
HELIX 76 76 GLU C 393 ILE C 413 1 21
HELIX 77 77 SER C 414 LEU C 432 1 19
HELIX 78 78 LEU C 432 ALA C 437 1 6
HELIX 79 79 ASP C 454 SER C 467 1 14
HELIX 80 80 HIS C 468 ILE C 487 1 20
HELIX 81 81 TYR D 4 LEU D 8 5 5
HELIX 82 82 ASN D 9 GLY D 18 1 10
HELIX 83 83 GLY D 24 ALA D 29 5 6
HELIX 84 84 ALA D 32 GLN D 36 5 5
HELIX 85 85 LEU D 50 ASP D 58 1 9
HELIX 86 86 GLU D 70 GLU D 74 5 5
HELIX 87 87 PRO D 107 LYS D 109 5 3
HELIX 88 88 GLN D 110 MET D 122 1 13
HELIX 89 89 GLY D 133 GLU D 138 1 6
HELIX 90 90 THR D 159 ARG D 167 1 9
HELIX 91 91 PRO D 179 ASP D 182 5 4
HELIX 92 92 GLU D 186 THR D 198 1 13
HELIX 93 93 GLY D 199 GLY D 204 1 6
HELIX 94 94 SER D 209 ILE D 224 1 16
HELIX 95 95 CYS D 226 GLU D 243 1 18
HELIX 96 96 ASP D 246 ASP D 275 1 30
HELIX 97 97 SER D 278 SER D 309 1 32
HELIX 98 98 GLY D 310 ALA D 321 1 12
HELIX 99 99 ASP D 324 LYS D 336 1 13
HELIX 100 100 GLY D 350 LYS D 357 1 8
HELIX 101 101 GLY D 358 ASP D 378 1 21
HELIX 102 102 ILE D 382 LEU D 391 1 10
HELIX 103 103 GLU D 393 ILE D 413 1 21
HELIX 104 104 SER D 414 LEU D 432 1 19
HELIX 105 105 LEU D 432 ALA D 437 1 6
HELIX 106 106 ASP D 454 SER D 467 1 14
HELIX 107 107 HIS D 468 ILE D 487 1 20
SHEET 1 A 9 CYS A 20 PHE A 22 0
SHEET 2 A 9 VAL A 205 SER A 208 -1 O GLU A 207 N ARG A 21
SHEET 3 A 9 THR A 173 VAL A 177 1 N THR A 173 O LEU A 206
SHEET 4 A 9 THR A 148 PRO A 154 -1 N ALA A 153 O LEU A 174
SHEET 5 A 9 ALA A 127 TYR A 130 1 N LEU A 128 O THR A 148
SHEET 6 A 9 LEU A 101 ASN A 104 1 N VAL A 102 O GLY A 129
SHEET 7 A 9 VAL A 40 VAL A 43 1 N VAL A 43 O ILE A 103
SHEET 8 A 9 ILE A 63 LEU A 67 1 O ALA A 66 N ILE A 42
SHEET 9 A 9 LYS A 88 THR A 91 1 O GLY A 90 N TYR A 65
SHEET 1 B 6 CYS B 20 PHE B 22 0
SHEET 2 B 6 VAL B 205 SER B 208 -1 O GLU B 207 N ARG B 21
SHEET 3 B 6 THR B 173 VAL B 177 1 N ILE B 175 O LEU B 206
SHEET 4 B 6 THR B 148 PRO B 154 -1 N ALA B 153 O LEU B 174
SHEET 5 B 6 ALA B 127 TYR B 130 1 N LEU B 128 O VAL B 150
SHEET 6 B 6 LEU B 101 ILE B 103 1 N VAL B 102 O ALA B 127
SHEET 1 C 9 CYS C 20 PHE C 22 0
SHEET 2 C 9 VAL C 205 SER C 208 -1 O GLU C 207 N ARG C 21
SHEET 3 C 9 THR C 173 VAL C 177 1 N THR C 173 O LEU C 206
SHEET 4 C 9 THR C 148 PRO C 154 -1 N ALA C 153 O LEU C 174
SHEET 5 C 9 ALA C 127 GLY C 129 1 N LEU C 128 O THR C 148
SHEET 6 C 9 LEU C 101 ASN C 104 1 N VAL C 102 O ALA C 127
SHEET 7 C 9 VAL C 40 VAL C 43 1 N VAL C 41 O ILE C 103
SHEET 8 C 9 ILE C 63 LEU C 67 1 O SER C 64 N ILE C 42
SHEET 9 C 9 LYS C 88 THR C 91 1 O LYS C 88 N TYR C 65
SHEET 1 D 8 ARG D 21 PHE D 22 0
SHEET 2 D 8 VAL D 205 GLU D 207 -1 O GLU D 207 N ARG D 21
SHEET 3 D 8 THR D 173 VAL D 177 1 N THR D 173 O LEU D 206
SHEET 4 D 8 THR D 148 PRO D 154 -1 N ALA D 153 O LEU D 174
SHEET 5 D 8 ALA D 127 TYR D 130 1 N LEU D 128 O THR D 148
SHEET 6 D 8 LEU D 101 ILE D 103 1 N VAL D 102 O GLY D 129
SHEET 7 D 8 LYS D 39 ILE D 42 1 N VAL D 41 O LEU D 101
SHEET 8 D 8 ASP D 62 TYR D 65 1 O ASP D 62 N VAL D 40
SITE 1 AC1 4 ASN A 3 ASN A 6 HOH A4183 HOH A4282
SITE 1 AC2 2 ARG A 11 GLN A 12
SITE 1 AC3 2 ASN D 3 ASN D 6
SITE 1 AC4 3 GLN A 301 ARG D 11 GLN D 12
SITE 1 AC5 2 ARG C 11 GLN C 12
SITE 1 AC6 2 ARG B 11 GLN B 12
SITE 1 AC7 5 ALA A 71 ARG A 76 SER A 78 HOH A4156
SITE 2 AC7 5 HOH A4163
SITE 1 AC8 2 HIS A 201 ARG A 202
SITE 1 AC9 2 HIS D 201 ARG D 202
CRYST1 226.882 226.882 118.853 90.00 90.00 120.00 P 63 24
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 0.004408 0.002545 0.000000 0.00000
SCALE2 0.000000 0.005089 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008414 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
