HEADER ATP SYNTHASE 30-APR-98 1NBM
TITLE THE STRUCTURE OF BOVINE F1-ATPASE COVALENTLY INHIBITED WITH 4-CHLORO-
TITLE 2 7-NITROBENZOFURAZAN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: F1-ATPASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: BOVINE MITOCHONDRIAL F1-ATPASE;
COMPND 5 EC: 3.6.1.34;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: F1-ATPASE;
COMPND 8 CHAIN: D, F;
COMPND 9 SYNONYM: BOVINE MITOCHONDRIAL F1-ATPASE;
COMPND 10 EC: 3.6.1.34;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: F1-ATPASE;
COMPND 13 CHAIN: E;
COMPND 14 SYNONYM: BOVINE MITOCHONDRIAL F1-ATPASE;
COMPND 15 EC: 3.6.1.34;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: F1-ATPASE;
COMPND 18 CHAIN: G;
COMPND 19 SYNONYM: BOVINE MITOCHONDRIAL F1-ATPASE;
COMPND 20 EC: 3.6.1.34
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: HEART;
SOURCE 6 TISSUE: MUSCLE;
SOURCE 7 ORGANELLE: MITOCHONDRION;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 10 ORGANISM_COMMON: CATTLE;
SOURCE 11 ORGANISM_TAXID: 9913;
SOURCE 12 ORGAN: HEART;
SOURCE 13 TISSUE: MUSCLE;
SOURCE 14 ORGANELLE: MITOCHONDRION;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 17 ORGANISM_COMMON: CATTLE;
SOURCE 18 ORGANISM_TAXID: 9913;
SOURCE 19 ORGAN: HEART;
SOURCE 20 TISSUE: MUSCLE;
SOURCE 21 ORGANELLE: MITOCHONDRION;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 24 ORGANISM_COMMON: CATTLE;
SOURCE 25 ORGANISM_TAXID: 9913;
SOURCE 26 ORGAN: HEART;
SOURCE 27 TISSUE: MUSCLE;
SOURCE 28 ORGANELLE: MITOCHONDRION
KEYWDS ATP SYNTHASE, F1FO ATP SYNTHASE, F1-ATPASE, 4-CHLORO-7-
KEYWDS 2 NITROBENZOFURAZAN, INHIBITION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.L.ORRISS,A.G.W.LESLIE,K.BRAIG,J.E.WALKER
REVDAT 4 03-APR-24 1NBM 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1NBM 1 VERSN
REVDAT 2 01-APR-03 1NBM 1 JRNL
REVDAT 1 26-AUG-98 1NBM 0
JRNL AUTH G.L.ORRISS,A.G.LESLIE,K.BRAIG,J.E.WALKER
JRNL TITL BOVINE F1-ATPASE COVALENTLY INHIBITED WITH
JRNL TITL 2 4-CHLORO-7-NITROBENZOFURAZAN: THE STRUCTURE PROVIDES FURTHER
JRNL TITL 3 SUPPORT FOR A ROTARY CATALYTIC MECHANISM.
JRNL REF STRUCTURE V. 6 831 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9687365
JRNL DOI 10.1016/S0969-2126(98)00085-9
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.P.ABRAHAMS,A.G.LESLIE,R.LUTTER,J.E.WALKER
REMARK 1 TITL STRUCTURE AT 2.8 A RESOLUTION OF F1-ATPASE FROM BOVINE HEART
REMARK 1 TITL 2 MITOCHONDRIA
REMARK 1 REF NATURE V. 370 621 1994
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 66714
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE-R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.297
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3434
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.12
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.23
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6154
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 316
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 : 22732
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 161
REMARK 3 SOLVENT ATOMS : 164
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.67
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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 0.994
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.17
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : INDIVIDUAL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.500 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.000 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.500 ; 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : TYR.PAR
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TYR.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175220.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70240
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.30400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: ALUMINUM FLUORIDE INHIBITED FORM OF BOVINE
REMARK 200 MITOCHONDRIAL F1-ATPASE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS-HCL, PH7.5, 200MM SODIUM
REMARK 280 CHLORIDE, 20MM MAGNESIUM SULPHATE, 1MM EDTA, 0.002% (W/V) PHENYL
REMARK 280 METHYLSULPHONYL FLUORIDE, 0.02%(W/V) SODIUM AZIDE, 10.5% (W/V)
REMARK 280 PEG MME 5000, 250UM AMP-PNP AND 5UM ADP.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 140.50000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.40000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.40000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 140.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.30000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEPTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 36930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 101300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -211.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G
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 400
REMARK 400 COMPOUND
REMARK 400 THE F1-ATPASE MOLECULE HAS THREE COPIES OF THE
REMARK 400 NON-CATALYTIC ALPHA SUBUNIT AND THREE COPIES OF THE
REMARK 400 CATALYTIC BETA SUBUNIT. IN THE PRIMARY REFERENCE, THE BETA
REMARK 400 SUBUNITS WERE LABELLED ACCORDING TO THE BOUND NUCLEOTIDE,
REMARK 400 AS BETA(DP) (BINDS ADP), BETA(E) (NO BOUND NUCLEOTIDE) AND
REMARK 400 BETA(TP) (AMPPNP BOUND). THE ALPHA SUBUNITS
REMARK 400 (WHICH ALL BIND AMPPNP) CONTRIBUTE TO THE CATALYTIC SITES
REMARK 400 OF THE BETA SUBUNITS, AND HAVE BEEN LABELLED ACCORDINGLY.
REMARK 400 THUS ALPHA(DP) CONTRIBUTES TO THE CATALYTIC SITE ON
REMARK 400 BETA(DP), ALPHA(TP) TO THE SITE ON BETA(TP) AND ALPHA(E)
REMARK 400 TO THE SITE ON BETA(E). THE CORRESPONDENCE BETWEEN THE
REMARK 400 SUBUNIT NAMES AND THE CHAIN IDENTIFIERS IS GIVEN BELOW:
REMARK 400 CHAIN A: ALPHA(E) CHAIN B: ALPHA(TP) CHAIN C: ALPHA(DP)
REMARK 400 CHAIN D: BETA(DP) CHAIN E: BETA(E) CHAIN F: BETA(TP) CHAIN
REMARK 400 G IS THE GAMMA SUBUNIT.
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 GLN A 1
REMARK 465 LYS A 2
REMARK 465 THR A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 465 VAL A 8
REMARK 465 SER A 9
REMARK 465 SER A 10
REMARK 465 ILE A 11
REMARK 465 LEU A 12
REMARK 465 GLU A 13
REMARK 465 GLU A 14
REMARK 465 ARG A 15
REMARK 465 ILE A 16
REMARK 465 LEU A 17
REMARK 465 GLY A 18
REMARK 465 ALA A 19
REMARK 465 ASP A 20
REMARK 465 THR A 21
REMARK 465 SER A 22
REMARK 465 VAL A 23
REMARK 465 GLN B 1
REMARK 465 LYS B 2
REMARK 465 THR B 3
REMARK 465 GLY B 4
REMARK 465 THR B 5
REMARK 465 ALA B 6
REMARK 465 GLU B 7
REMARK 465 VAL B 8
REMARK 465 SER B 9
REMARK 465 SER B 10
REMARK 465 ILE B 11
REMARK 465 LEU B 12
REMARK 465 GLU B 13
REMARK 465 GLU B 14
REMARK 465 ARG B 15
REMARK 465 ILE B 16
REMARK 465 LEU B 17
REMARK 465 GLY B 18
REMARK 465 ALA B 19
REMARK 465 ASP B 20
REMARK 465 THR B 21
REMARK 465 SER B 22
REMARK 465 VAL B 23
REMARK 465 GLN C 1
REMARK 465 LYS C 2
REMARK 465 THR C 3
REMARK 465 GLY C 4
REMARK 465 THR C 5
REMARK 465 ALA C 6
REMARK 465 GLU C 7
REMARK 465 VAL C 8
REMARK 465 SER C 9
REMARK 465 SER C 10
REMARK 465 ILE C 11
REMARK 465 LEU C 12
REMARK 465 GLU C 13
REMARK 465 GLU C 14
REMARK 465 ARG C 15
REMARK 465 ILE C 16
REMARK 465 LEU C 17
REMARK 465 GLY C 18
REMARK 465 ALA D -3
REMARK 465 ALA D -2
REMARK 465 GLN D -1
REMARK 465 ALA D 0
REMARK 465 SER D 1
REMARK 465 PRO D 2
REMARK 465 SER D 3
REMARK 465 PRO D 4
REMARK 465 LYS D 5
REMARK 465 ALA D 6
REMARK 465 GLY D 7
REMARK 465 ALA D 8
REMARK 465 GLU D 476
REMARK 465 ALA E -3
REMARK 465 ALA E -2
REMARK 465 GLN E -1
REMARK 465 ALA E 0
REMARK 465 SER E 1
REMARK 465 PRO E 2
REMARK 465 SER E 3
REMARK 465 PRO E 4
REMARK 465 LYS E 5
REMARK 465 ALA E 6
REMARK 465 GLY E 7
REMARK 465 ALA E 8
REMARK 465 GLU E 475
REMARK 465 GLU E 476
REMARK 465 ALA F -3
REMARK 465 ALA F -2
REMARK 465 GLN F -1
REMARK 465 ALA F 0
REMARK 465 SER F 1
REMARK 465 PRO F 2
REMARK 465 SER F 3
REMARK 465 PRO F 4
REMARK 465 LYS F 5
REMARK 465 ALA F 6
REMARK 465 GLY F 7
REMARK 465 ALA F 8
REMARK 465 GLU F 475
REMARK 465 GLU F 476
REMARK 465 GLY G 45
REMARK 465 VAL G 46
REMARK 465 GLY G 47
REMARK 465 SER G 48
REMARK 465 LEU G 49
REMARK 465 ALA G 50
REMARK 465 LEU G 51
REMARK 465 TYR G 52
REMARK 465 GLU G 53
REMARK 465 LYS G 54
REMARK 465 ALA G 55
REMARK 465 ASP G 56
REMARK 465 ILE G 57
REMARK 465 LYS G 58
REMARK 465 THR G 59
REMARK 465 PRO G 60
REMARK 465 GLU G 61
REMARK 465 ASP G 62
REMARK 465 LYS G 63
REMARK 465 LYS G 64
REMARK 465 LYS G 65
REMARK 465 HIS G 66
REMARK 465 LEU G 67
REMARK 465 ILE G 68
REMARK 465 ILE G 69
REMARK 465 GLY G 70
REMARK 465 VAL G 71
REMARK 465 SER G 72
REMARK 465 SER G 73
REMARK 465 ASP G 74
REMARK 465 ARG G 75
REMARK 465 GLY G 76
REMARK 465 SER G 91
REMARK 465 GLU G 92
REMARK 465 ALA G 93
REMARK 465 ALA G 94
REMARK 465 ASN G 95
REMARK 465 LEU G 96
REMARK 465 ALA G 97
REMARK 465 ALA G 98
REMARK 465 ALA G 99
REMARK 465 GLY G 100
REMARK 465 LYS G 101
REMARK 465 GLU G 102
REMARK 465 VAL G 103
REMARK 465 LYS G 104
REMARK 465 ILE G 105
REMARK 465 ILE G 106
REMARK 465 GLY G 107
REMARK 465 VAL G 108
REMARK 465 GLY G 109
REMARK 465 ASP G 110
REMARK 465 LYS G 111
REMARK 465 ILE G 112
REMARK 465 ARG G 113
REMARK 465 SER G 114
REMARK 465 ILE G 115
REMARK 465 LEU G 116
REMARK 465 HIS G 117
REMARK 465 ARG G 118
REMARK 465 THR G 119
REMARK 465 HIS G 120
REMARK 465 SER G 121
REMARK 465 ASP G 122
REMARK 465 GLN G 123
REMARK 465 PHE G 124
REMARK 465 LEU G 125
REMARK 465 VAL G 126
REMARK 465 THR G 127
REMARK 465 PHE G 128
REMARK 465 LYS G 129
REMARK 465 GLU G 130
REMARK 465 VAL G 131
REMARK 465 GLY G 132
REMARK 465 ARG G 133
REMARK 465 ARG G 134
REMARK 465 PRO G 135
REMARK 465 PRO G 136
REMARK 465 THR G 137
REMARK 465 PHE G 138
REMARK 465 GLY G 139
REMARK 465 ASP G 140
REMARK 465 ALA G 141
REMARK 465 SER G 142
REMARK 465 VAL G 143
REMARK 465 ILE G 144
REMARK 465 ALA G 145
REMARK 465 LEU G 146
REMARK 465 GLU G 147
REMARK 465 LEU G 148
REMARK 465 LEU G 149
REMARK 465 ASN G 150
REMARK 465 SER G 151
REMARK 465 GLY G 152
REMARK 465 TYR G 153
REMARK 465 GLU G 154
REMARK 465 PHE G 155
REMARK 465 ASP G 156
REMARK 465 GLU G 157
REMARK 465 GLY G 158
REMARK 465 SER G 159
REMARK 465 ILE G 160
REMARK 465 ILE G 161
REMARK 465 PHE G 162
REMARK 465 ASN G 163
REMARK 465 ARG G 164
REMARK 465 PHE G 165
REMARK 465 ARG G 166
REMARK 465 SER G 167
REMARK 465 VAL G 168
REMARK 465 ILE G 169
REMARK 465 SER G 170
REMARK 465 TYR G 171
REMARK 465 LYS G 172
REMARK 465 THR G 173
REMARK 465 GLU G 174
REMARK 465 GLU G 175
REMARK 465 LYS G 176
REMARK 465 PRO G 177
REMARK 465 ILE G 178
REMARK 465 PHE G 179
REMARK 465 SER G 180
REMARK 465 LEU G 181
REMARK 465 ASP G 182
REMARK 465 THR G 183
REMARK 465 ILE G 184
REMARK 465 SER G 185
REMARK 465 SER G 186
REMARK 465 ALA G 187
REMARK 465 GLU G 188
REMARK 465 SER G 189
REMARK 465 MET G 190
REMARK 465 SER G 191
REMARK 465 ILE G 192
REMARK 465 TYR G 193
REMARK 465 ASP G 194
REMARK 465 ASP G 195
REMARK 465 ILE G 196
REMARK 465 ASP G 197
REMARK 465 ALA G 198
REMARK 465 ASP G 199
REMARK 465 VAL G 200
REMARK 465 LEU G 201
REMARK 465 ARG G 202
REMARK 465 ASN G 203
REMARK 465 TYR G 204
REMARK 465 GLN G 205
REMARK 465 GLU G 206
REMARK 465 TYR G 207
REMARK 465 SER G 208
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ALA B 402
REMARK 475 PHE B 403
REMARK 475 ALA B 404
REMARK 475 GLN B 405
REMARK 475 PHE B 406
REMARK 475 GLY B 407
REMARK 475 SER B 408
REMARK 475 ASP B 409
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 25 81.82 -62.53
REMARK 500 GLU A 26 -67.09 -171.49
REMARK 500 ARG A 45 0.07 -68.46
REMARK 500 PHE A 76 54.74 -95.45
REMARK 500 LEU A 81 31.31 -87.17
REMARK 500 SER A 123 89.35 -64.75
REMARK 500 PRO A 138 12.27 -58.66
REMARK 500 ARG A 143 -62.32 -139.03
REMARK 500 ASN A 260 31.18 -82.18
REMARK 500 ALA A 293 -4.48 74.32
REMARK 500 PHE A 316 53.00 -109.04
REMARK 500 TYR A 337 -72.40 -49.09
REMARK 500 TYR A 452 32.28 -79.52
REMARK 500 LEU A 453 -2.68 -153.48
REMARK 500 SER A 474 -88.85 -91.40
REMARK 500 GLN A 475 30.73 -79.50
REMARK 500 HIS A 476 31.71 -160.24
REMARK 500 GLU A 509 77.59 -109.88
REMARK 500 ASN B 46 35.81 -86.22
REMARK 500 GLU B 50 32.14 73.02
REMARK 500 PRO B 68 29.13 -69.13
REMARK 500 ASP B 69 -18.18 -170.51
REMARK 500 PHE B 76 51.87 -94.21
REMARK 500 ASN B 78 85.65 -66.91
REMARK 500 LYS B 118 55.05 -148.11
REMARK 500 ILE B 121 90.93 47.45
REMARK 500 ARG B 143 -38.37 -157.18
REMARK 500 ASP B 191 35.55 -96.85
REMARK 500 SER B 237 -34.62 -162.98
REMARK 500 ASP B 297 11.89 -144.68
REMARK 500 PHE B 316 47.82 -102.68
REMARK 500 VAL B 386 -55.41 -129.00
REMARK 500 LEU B 410 -145.46 -143.13
REMARK 500 ASP B 411 104.87 74.44
REMARK 500 LYS B 455 55.87 -96.41
REMARK 500 ASN B 466 49.66 -79.84
REMARK 500 ALA B 467 -52.03 -168.48
REMARK 500 SER B 474 -78.99 -74.25
REMARK 500 GLN B 475 23.66 -75.23
REMARK 500 HIS B 476 35.26 -156.88
REMARK 500 THR C 21 33.53 -140.26
REMARK 500 LEU C 25 5.20 -56.88
REMARK 500 PHE C 76 42.02 -89.98
REMARK 500 LYS C 118 40.79 -82.69
REMARK 500 ARG C 143 -35.95 -136.59
REMARK 500 ASP C 194 94.62 -65.52
REMARK 500 ALA C 293 -13.57 71.42
REMARK 500 PHE C 316 39.21 -96.33
REMARK 500 ASP C 347 45.80 -95.20
REMARK 500 ALA C 364 43.66 -82.00
REMARK 500
REMARK 500 THIS ENTRY HAS 130 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 176 OG1
REMARK 620 2 GLN A 208 OE1 121.7
REMARK 620 3 ATP A 600 O2G 121.0 117.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 176 OG1
REMARK 620 2 GLN B 208 OE1 113.6
REMARK 620 3 ATP B 600 O2G 138.1 108.3
REMARK 620 4 ATP B 600 O2B 72.3 172.9 65.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 176 OG1
REMARK 620 2 ATP C 600 O2G 135.8
REMARK 620 3 ATP C 600 O2B 71.1 64.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 163 OG1
REMARK 620 2 ADP D 600 O2B 107.7
REMARK 620 3 HOH D 603 O 107.9 124.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 163 OG1
REMARK 620 2 ATP F 600 O2G 155.7
REMARK 620 3 ATP F 600 O2B 84.5 72.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: PL1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE RESIDUE LISTED IS THE LYSINE WITHIN THE P
REMARK 800 -LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
REMARK 800
REMARK 800 SITE_IDENTIFIER: PL2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE RESIDUE LISTED IS THE LYSINE WITHIN THE P
REMARK 800 -LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
REMARK 800
REMARK 800 SITE_IDENTIFIER: PL3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE RESIDUE LISTED IS THE LYSINE WITHIN THE P
REMARK 800 -LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
REMARK 800
REMARK 800 SITE_IDENTIFIER: PL4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE RESIDUE LISTED IS THE LYSINE WITHIN THE P
REMARK 800 -LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
REMARK 800
REMARK 800 SITE_IDENTIFIER: PL5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE RESIDUE LISTED IS THE LYSINE WITHIN THE P
REMARK 800 -LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
REMARK 800
REMARK 800 SITE_IDENTIFIER: PL6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE RESIDUE LISTED IS THE LYSINE WITHIN THE P
REMARK 800 -LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID
REMARK 800 RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE
REMARK 800 ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE
REMARK 800 ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT)
REMARK 800 COULD HELP TO STABLISE THE NEGATIVE CHARGE THAT DEVELOPS ON THE
REMARK 800 TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION
REMARK 800 STATE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID
REMARK 800 RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE
REMARK 800 ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE
REMARK 800 ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT)
REMARK 800 COULD HELP TO STABLISE THE NEGATIVE CHARGE THAT DEVELOPS ON THE
REMARK 800 TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION
REMARK 800 STATE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID
REMARK 800 RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE
REMARK 800 ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE
REMARK 800 ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT)
REMARK 800 COULD HELP TO STABLISE THE NEGATIVE CHARGE THAT DEVELOPS ON THE
REMARK 800 TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION
REMARK 800 STATE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP F 600
DBREF 1NBM A 1 510 UNP P19483 ATPA1_BOVIN 44 553
DBREF 1NBM B 1 510 UNP P19483 ATPA1_BOVIN 44 553
DBREF 1NBM C 1 510 UNP P19483 ATPA1_BOVIN 44 553
DBREF 1NBM D -3 476 UNP P00829 ATPB_BOVIN 47 526
DBREF 1NBM E -3 476 UNP P00829 ATPB_BOVIN 47 526
DBREF 1NBM F -3 476 UNP P00829 ATPB_BOVIN 47 526
DBREF 1NBM G 1 272 UNP P05631 ATPG_BOVIN 26 297
SEQADV 1NBM GLY A 481 UNP P19483 SER 524 CONFLICT
SEQADV 1NBM GLY B 481 UNP P19483 SER 524 CONFLICT
SEQADV 1NBM GLY C 481 UNP P19483 SER 524 CONFLICT
SEQADV 1NBM TYN E 311 UNP P00829 TYR 361 MODIFIED RESIDUE
SEQRES 1 A 510 GLN LYS THR GLY THR ALA GLU VAL SER SER ILE LEU GLU
SEQRES 2 A 510 GLU ARG ILE LEU GLY ALA ASP THR SER VAL ASP LEU GLU
SEQRES 3 A 510 GLU THR GLY ARG VAL LEU SER ILE GLY ASP GLY ILE ALA
SEQRES 4 A 510 ARG VAL HIS GLY LEU ARG ASN VAL GLN ALA GLU GLU MET
SEQRES 5 A 510 VAL GLU PHE SER SER GLY LEU LYS GLY MET SER LEU ASN
SEQRES 6 A 510 LEU GLU PRO ASP ASN VAL GLY VAL VAL VAL PHE GLY ASN
SEQRES 7 A 510 ASP LYS LEU ILE LYS GLU GLY ASP ILE VAL LYS ARG THR
SEQRES 8 A 510 GLY ALA ILE VAL ASP VAL PRO VAL GLY GLU GLU LEU LEU
SEQRES 9 A 510 GLY ARG VAL VAL ASP ALA LEU GLY ASN ALA ILE ASP GLY
SEQRES 10 A 510 LYS GLY PRO ILE GLY SER LYS ALA ARG ARG ARG VAL GLY
SEQRES 11 A 510 LEU LYS ALA PRO GLY ILE ILE PRO ARG ILE SER VAL ARG
SEQRES 12 A 510 GLU PRO MET GLN THR GLY ILE LYS ALA VAL ASP SER LEU
SEQRES 13 A 510 VAL PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES 14 A 510 ASP ARG GLN THR GLY LYS THR SER ILE ALA ILE ASP THR
SEQRES 15 A 510 ILE ILE ASN GLN LYS ARG PHE ASN ASP GLY THR ASP GLU
SEQRES 16 A 510 LYS LYS LYS LEU TYR CYS ILE TYR VAL ALA ILE GLY GLN
SEQRES 17 A 510 LYS ARG SER THR VAL ALA GLN LEU VAL LYS ARG LEU THR
SEQRES 18 A 510 ASP ALA ASP ALA MET LYS TYR THR ILE VAL VAL SER ALA
SEQRES 19 A 510 THR ALA SER ASP ALA ALA PRO LEU GLN TYR LEU ALA PRO
SEQRES 20 A 510 TYR SER GLY CYS SER MET GLY GLU TYR PHE ARG ASP ASN
SEQRES 21 A 510 GLY LYS HIS ALA LEU ILE ILE TYR ASP ASP LEU SER LYS
SEQRES 22 A 510 GLN ALA VAL ALA TYR ARG GLN MET SER LEU LEU LEU ARG
SEQRES 23 A 510 ARG PRO PRO GLY ARG GLU ALA TYR PRO GLY ASP VAL PHE
SEQRES 24 A 510 TYR LEU HIS SER ARG LEU LEU GLU ARG ALA ALA LYS MET
SEQRES 25 A 510 ASN ASP ALA PHE GLY GLY GLY SER LEU THR ALA LEU PRO
SEQRES 26 A 510 VAL ILE GLU THR GLN ALA GLY ASP VAL SER ALA TYR ILE
SEQRES 27 A 510 PRO THR ASN VAL ILE SER ILE THR ASP GLY GLN ILE PHE
SEQRES 28 A 510 LEU GLU THR GLU LEU PHE TYR LYS GLY ILE ARG PRO ALA
SEQRES 29 A 510 ILE ASN VAL GLY LEU SER VAL SER ARG VAL GLY SER ALA
SEQRES 30 A 510 ALA GLN THR ARG ALA MET LYS GLN VAL ALA GLY THR MET
SEQRES 31 A 510 LYS LEU GLU LEU ALA GLN TYR ARG GLU VAL ALA ALA PHE
SEQRES 32 A 510 ALA GLN PHE GLY SER ASP LEU ASP ALA ALA THR GLN GLN
SEQRES 33 A 510 LEU LEU SER ARG GLY VAL ARG LEU THR GLU LEU LEU LYS
SEQRES 34 A 510 GLN GLY GLN TYR SER PRO MET ALA ILE GLU GLU GLN VAL
SEQRES 35 A 510 ALA VAL ILE TYR ALA GLY VAL ARG GLY TYR LEU ASP LYS
SEQRES 36 A 510 LEU GLU PRO SER LYS ILE THR LYS PHE GLU ASN ALA PHE
SEQRES 37 A 510 LEU SER HIS VAL ILE SER GLN HIS GLN ALA LEU LEU GLY
SEQRES 38 A 510 LYS ILE ARG THR ASP GLY LYS ILE SER GLU GLU SER ASP
SEQRES 39 A 510 ALA LYS LEU LYS GLU ILE VAL THR ASN PHE LEU ALA GLY
SEQRES 40 A 510 PHE GLU ALA
SEQRES 1 B 510 GLN LYS THR GLY THR ALA GLU VAL SER SER ILE LEU GLU
SEQRES 2 B 510 GLU ARG ILE LEU GLY ALA ASP THR SER VAL ASP LEU GLU
SEQRES 3 B 510 GLU THR GLY ARG VAL LEU SER ILE GLY ASP GLY ILE ALA
SEQRES 4 B 510 ARG VAL HIS GLY LEU ARG ASN VAL GLN ALA GLU GLU MET
SEQRES 5 B 510 VAL GLU PHE SER SER GLY LEU LYS GLY MET SER LEU ASN
SEQRES 6 B 510 LEU GLU PRO ASP ASN VAL GLY VAL VAL VAL PHE GLY ASN
SEQRES 7 B 510 ASP LYS LEU ILE LYS GLU GLY ASP ILE VAL LYS ARG THR
SEQRES 8 B 510 GLY ALA ILE VAL ASP VAL PRO VAL GLY GLU GLU LEU LEU
SEQRES 9 B 510 GLY ARG VAL VAL ASP ALA LEU GLY ASN ALA ILE ASP GLY
SEQRES 10 B 510 LYS GLY PRO ILE GLY SER LYS ALA ARG ARG ARG VAL GLY
SEQRES 11 B 510 LEU LYS ALA PRO GLY ILE ILE PRO ARG ILE SER VAL ARG
SEQRES 12 B 510 GLU PRO MET GLN THR GLY ILE LYS ALA VAL ASP SER LEU
SEQRES 13 B 510 VAL PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES 14 B 510 ASP ARG GLN THR GLY LYS THR SER ILE ALA ILE ASP THR
SEQRES 15 B 510 ILE ILE ASN GLN LYS ARG PHE ASN ASP GLY THR ASP GLU
SEQRES 16 B 510 LYS LYS LYS LEU TYR CYS ILE TYR VAL ALA ILE GLY GLN
SEQRES 17 B 510 LYS ARG SER THR VAL ALA GLN LEU VAL LYS ARG LEU THR
SEQRES 18 B 510 ASP ALA ASP ALA MET LYS TYR THR ILE VAL VAL SER ALA
SEQRES 19 B 510 THR ALA SER ASP ALA ALA PRO LEU GLN TYR LEU ALA PRO
SEQRES 20 B 510 TYR SER GLY CYS SER MET GLY GLU TYR PHE ARG ASP ASN
SEQRES 21 B 510 GLY LYS HIS ALA LEU ILE ILE TYR ASP ASP LEU SER LYS
SEQRES 22 B 510 GLN ALA VAL ALA TYR ARG GLN MET SER LEU LEU LEU ARG
SEQRES 23 B 510 ARG PRO PRO GLY ARG GLU ALA TYR PRO GLY ASP VAL PHE
SEQRES 24 B 510 TYR LEU HIS SER ARG LEU LEU GLU ARG ALA ALA LYS MET
SEQRES 25 B 510 ASN ASP ALA PHE GLY GLY GLY SER LEU THR ALA LEU PRO
SEQRES 26 B 510 VAL ILE GLU THR GLN ALA GLY ASP VAL SER ALA TYR ILE
SEQRES 27 B 510 PRO THR ASN VAL ILE SER ILE THR ASP GLY GLN ILE PHE
SEQRES 28 B 510 LEU GLU THR GLU LEU PHE TYR LYS GLY ILE ARG PRO ALA
SEQRES 29 B 510 ILE ASN VAL GLY LEU SER VAL SER ARG VAL GLY SER ALA
SEQRES 30 B 510 ALA GLN THR ARG ALA MET LYS GLN VAL ALA GLY THR MET
SEQRES 31 B 510 LYS LEU GLU LEU ALA GLN TYR ARG GLU VAL ALA ALA PHE
SEQRES 32 B 510 ALA GLN PHE GLY SER ASP LEU ASP ALA ALA THR GLN GLN
SEQRES 33 B 510 LEU LEU SER ARG GLY VAL ARG LEU THR GLU LEU LEU LYS
SEQRES 34 B 510 GLN GLY GLN TYR SER PRO MET ALA ILE GLU GLU GLN VAL
SEQRES 35 B 510 ALA VAL ILE TYR ALA GLY VAL ARG GLY TYR LEU ASP LYS
SEQRES 36 B 510 LEU GLU PRO SER LYS ILE THR LYS PHE GLU ASN ALA PHE
SEQRES 37 B 510 LEU SER HIS VAL ILE SER GLN HIS GLN ALA LEU LEU GLY
SEQRES 38 B 510 LYS ILE ARG THR ASP GLY LYS ILE SER GLU GLU SER ASP
SEQRES 39 B 510 ALA LYS LEU LYS GLU ILE VAL THR ASN PHE LEU ALA GLY
SEQRES 40 B 510 PHE GLU ALA
SEQRES 1 C 510 GLN LYS THR GLY THR ALA GLU VAL SER SER ILE LEU GLU
SEQRES 2 C 510 GLU ARG ILE LEU GLY ALA ASP THR SER VAL ASP LEU GLU
SEQRES 3 C 510 GLU THR GLY ARG VAL LEU SER ILE GLY ASP GLY ILE ALA
SEQRES 4 C 510 ARG VAL HIS GLY LEU ARG ASN VAL GLN ALA GLU GLU MET
SEQRES 5 C 510 VAL GLU PHE SER SER GLY LEU LYS GLY MET SER LEU ASN
SEQRES 6 C 510 LEU GLU PRO ASP ASN VAL GLY VAL VAL VAL PHE GLY ASN
SEQRES 7 C 510 ASP LYS LEU ILE LYS GLU GLY ASP ILE VAL LYS ARG THR
SEQRES 8 C 510 GLY ALA ILE VAL ASP VAL PRO VAL GLY GLU GLU LEU LEU
SEQRES 9 C 510 GLY ARG VAL VAL ASP ALA LEU GLY ASN ALA ILE ASP GLY
SEQRES 10 C 510 LYS GLY PRO ILE GLY SER LYS ALA ARG ARG ARG VAL GLY
SEQRES 11 C 510 LEU LYS ALA PRO GLY ILE ILE PRO ARG ILE SER VAL ARG
SEQRES 12 C 510 GLU PRO MET GLN THR GLY ILE LYS ALA VAL ASP SER LEU
SEQRES 13 C 510 VAL PRO ILE GLY ARG GLY GLN ARG GLU LEU ILE ILE GLY
SEQRES 14 C 510 ASP ARG GLN THR GLY LYS THR SER ILE ALA ILE ASP THR
SEQRES 15 C 510 ILE ILE ASN GLN LYS ARG PHE ASN ASP GLY THR ASP GLU
SEQRES 16 C 510 LYS LYS LYS LEU TYR CYS ILE TYR VAL ALA ILE GLY GLN
SEQRES 17 C 510 LYS ARG SER THR VAL ALA GLN LEU VAL LYS ARG LEU THR
SEQRES 18 C 510 ASP ALA ASP ALA MET LYS TYR THR ILE VAL VAL SER ALA
SEQRES 19 C 510 THR ALA SER ASP ALA ALA PRO LEU GLN TYR LEU ALA PRO
SEQRES 20 C 510 TYR SER GLY CYS SER MET GLY GLU TYR PHE ARG ASP ASN
SEQRES 21 C 510 GLY LYS HIS ALA LEU ILE ILE TYR ASP ASP LEU SER LYS
SEQRES 22 C 510 GLN ALA VAL ALA TYR ARG GLN MET SER LEU LEU LEU ARG
SEQRES 23 C 510 ARG PRO PRO GLY ARG GLU ALA TYR PRO GLY ASP VAL PHE
SEQRES 24 C 510 TYR LEU HIS SER ARG LEU LEU GLU ARG ALA ALA LYS MET
SEQRES 25 C 510 ASN ASP ALA PHE GLY GLY GLY SER LEU THR ALA LEU PRO
SEQRES 26 C 510 VAL ILE GLU THR GLN ALA GLY ASP VAL SER ALA TYR ILE
SEQRES 27 C 510 PRO THR ASN VAL ILE SER ILE THR ASP GLY GLN ILE PHE
SEQRES 28 C 510 LEU GLU THR GLU LEU PHE TYR LYS GLY ILE ARG PRO ALA
SEQRES 29 C 510 ILE ASN VAL GLY LEU SER VAL SER ARG VAL GLY SER ALA
SEQRES 30 C 510 ALA GLN THR ARG ALA MET LYS GLN VAL ALA GLY THR MET
SEQRES 31 C 510 LYS LEU GLU LEU ALA GLN TYR ARG GLU VAL ALA ALA PHE
SEQRES 32 C 510 ALA GLN PHE GLY SER ASP LEU ASP ALA ALA THR GLN GLN
SEQRES 33 C 510 LEU LEU SER ARG GLY VAL ARG LEU THR GLU LEU LEU LYS
SEQRES 34 C 510 GLN GLY GLN TYR SER PRO MET ALA ILE GLU GLU GLN VAL
SEQRES 35 C 510 ALA VAL ILE TYR ALA GLY VAL ARG GLY TYR LEU ASP LYS
SEQRES 36 C 510 LEU GLU PRO SER LYS ILE THR LYS PHE GLU ASN ALA PHE
SEQRES 37 C 510 LEU SER HIS VAL ILE SER GLN HIS GLN ALA LEU LEU GLY
SEQRES 38 C 510 LYS ILE ARG THR ASP GLY LYS ILE SER GLU GLU SER ASP
SEQRES 39 C 510 ALA LYS LEU LYS GLU ILE VAL THR ASN PHE LEU ALA GLY
SEQRES 40 C 510 PHE GLU ALA
SEQRES 1 D 480 ALA ALA GLN ALA SER PRO SER PRO LYS ALA GLY ALA THR
SEQRES 2 D 480 THR GLY ARG ILE VAL ALA VAL ILE GLY ALA VAL VAL ASP
SEQRES 3 D 480 VAL GLN PHE ASP GLU GLY LEU PRO PRO ILE LEU ASN ALA
SEQRES 4 D 480 LEU GLU VAL GLN GLY ARG GLU THR ARG LEU VAL LEU GLU
SEQRES 5 D 480 VAL ALA GLN HIS LEU GLY GLU SER THR VAL ARG THR ILE
SEQRES 6 D 480 ALA MET ASP GLY THR GLU GLY LEU VAL ARG GLY GLN LYS
SEQRES 7 D 480 VAL LEU ASP SER GLY ALA PRO ILE ARG ILE PRO VAL GLY
SEQRES 8 D 480 PRO GLU THR LEU GLY ARG ILE MET ASN VAL ILE GLY GLU
SEQRES 9 D 480 PRO ILE ASP GLU ARG GLY PRO ILE LYS THR LYS GLN PHE
SEQRES 10 D 480 ALA ALA ILE HIS ALA GLU ALA PRO GLU PHE VAL GLU MET
SEQRES 11 D 480 SER VAL GLU GLN GLU ILE LEU VAL THR GLY ILE LYS VAL
SEQRES 12 D 480 VAL ASP LEU LEU ALA PRO TYR ALA LYS GLY GLY LYS ILE
SEQRES 13 D 480 GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR VAL LEU
SEQRES 14 D 480 ILE MET GLU LEU ILE ASN ASN VAL ALA LYS ALA HIS GLY
SEQRES 15 D 480 GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG THR ARG
SEQRES 16 D 480 GLU GLY ASN ASP LEU TYR HIS GLU MET ILE GLU SER GLY
SEQRES 17 D 480 VAL ILE ASN LEU LYS ASP ALA THR SER LYS VAL ALA LEU
SEQRES 18 D 480 VAL TYR GLY GLN MET ASN GLU PRO PRO GLY ALA ARG ALA
SEQRES 19 D 480 ARG VAL ALA LEU THR GLY LEU THR VAL ALA GLU TYR PHE
SEQRES 20 D 480 ARG ASP GLN GLU GLY GLN ASP VAL LEU LEU PHE ILE ASP
SEQRES 21 D 480 ASN ILE PHE ARG PHE THR GLN ALA GLY SER GLU VAL SER
SEQRES 22 D 480 ALA LEU LEU GLY ARG ILE PRO SER ALA VAL GLY TYR GLN
SEQRES 23 D 480 PRO THR LEU ALA THR ASP MET GLY THR MET GLN GLU ARG
SEQRES 24 D 480 ILE THR THR THR LYS LYS GLY SER ILE THR SER VAL GLN
SEQRES 25 D 480 ALA ILE TYR VAL PRO ALA ASP ASP LEU THR ASP PRO ALA
SEQRES 26 D 480 PRO ALA THR THR PHE ALA HIS LEU ASP ALA THR THR VAL
SEQRES 27 D 480 LEU SER ARG ALA ILE ALA GLU LEU GLY ILE TYR PRO ALA
SEQRES 28 D 480 VAL ASP PRO LEU ASP SER THR SER ARG ILE MET ASP PRO
SEQRES 29 D 480 ASN ILE VAL GLY SER GLU HIS TYR ASP VAL ALA ARG GLY
SEQRES 30 D 480 VAL GLN LYS ILE LEU GLN ASP TYR LYS SER LEU GLN ASP
SEQRES 31 D 480 ILE ILE ALA ILE LEU GLY MET ASP GLU LEU SER GLU GLU
SEQRES 32 D 480 ASP LYS LEU THR VAL SER ARG ALA ARG LYS ILE GLN ARG
SEQRES 33 D 480 PHE LEU SER GLN PRO PHE GLN VAL ALA GLU VAL PHE THR
SEQRES 34 D 480 GLY HIS LEU GLY LYS LEU VAL PRO LEU LYS GLU THR ILE
SEQRES 35 D 480 LYS GLY PHE GLN GLN ILE LEU ALA GLY GLU TYR ASP HIS
SEQRES 36 D 480 LEU PRO GLU GLN ALA PHE TYR MET VAL GLY PRO ILE GLU
SEQRES 37 D 480 GLU ALA VAL ALA LYS ALA ASP LYS LEU ALA GLU GLU
SEQRES 1 E 480 ALA ALA GLN ALA SER PRO SER PRO LYS ALA GLY ALA THR
SEQRES 2 E 480 THR GLY ARG ILE VAL ALA VAL ILE GLY ALA VAL VAL ASP
SEQRES 3 E 480 VAL GLN PHE ASP GLU GLY LEU PRO PRO ILE LEU ASN ALA
SEQRES 4 E 480 LEU GLU VAL GLN GLY ARG GLU THR ARG LEU VAL LEU GLU
SEQRES 5 E 480 VAL ALA GLN HIS LEU GLY GLU SER THR VAL ARG THR ILE
SEQRES 6 E 480 ALA MET ASP GLY THR GLU GLY LEU VAL ARG GLY GLN LYS
SEQRES 7 E 480 VAL LEU ASP SER GLY ALA PRO ILE ARG ILE PRO VAL GLY
SEQRES 8 E 480 PRO GLU THR LEU GLY ARG ILE MET ASN VAL ILE GLY GLU
SEQRES 9 E 480 PRO ILE ASP GLU ARG GLY PRO ILE LYS THR LYS GLN PHE
SEQRES 10 E 480 ALA ALA ILE HIS ALA GLU ALA PRO GLU PHE VAL GLU MET
SEQRES 11 E 480 SER VAL GLU GLN GLU ILE LEU VAL THR GLY ILE LYS VAL
SEQRES 12 E 480 VAL ASP LEU LEU ALA PRO TYR ALA LYS GLY GLY LYS ILE
SEQRES 13 E 480 GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR VAL LEU
SEQRES 14 E 480 ILE MET GLU LEU ILE ASN ASN VAL ALA LYS ALA HIS GLY
SEQRES 15 E 480 GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG THR ARG
SEQRES 16 E 480 GLU GLY ASN ASP LEU TYR HIS GLU MET ILE GLU SER GLY
SEQRES 17 E 480 VAL ILE ASN LEU LYS ASP ALA THR SER LYS VAL ALA LEU
SEQRES 18 E 480 VAL TYR GLY GLN MET ASN GLU PRO PRO GLY ALA ARG ALA
SEQRES 19 E 480 ARG VAL ALA LEU THR GLY LEU THR VAL ALA GLU TYR PHE
SEQRES 20 E 480 ARG ASP GLN GLU GLY GLN ASP VAL LEU LEU PHE ILE ASP
SEQRES 21 E 480 ASN ILE PHE ARG PHE THR GLN ALA GLY SER GLU VAL SER
SEQRES 22 E 480 ALA LEU LEU GLY ARG ILE PRO SER ALA VAL GLY TYR GLN
SEQRES 23 E 480 PRO THR LEU ALA THR ASP MET GLY THR MET GLN GLU ARG
SEQRES 24 E 480 ILE THR THR THR LYS LYS GLY SER ILE THR SER VAL GLN
SEQRES 25 E 480 ALA ILE TYN VAL PRO ALA ASP ASP LEU THR ASP PRO ALA
SEQRES 26 E 480 PRO ALA THR THR PHE ALA HIS LEU ASP ALA THR THR VAL
SEQRES 27 E 480 LEU SER ARG ALA ILE ALA GLU LEU GLY ILE TYR PRO ALA
SEQRES 28 E 480 VAL ASP PRO LEU ASP SER THR SER ARG ILE MET ASP PRO
SEQRES 29 E 480 ASN ILE VAL GLY SER GLU HIS TYR ASP VAL ALA ARG GLY
SEQRES 30 E 480 VAL GLN LYS ILE LEU GLN ASP TYR LYS SER LEU GLN ASP
SEQRES 31 E 480 ILE ILE ALA ILE LEU GLY MET ASP GLU LEU SER GLU GLU
SEQRES 32 E 480 ASP LYS LEU THR VAL SER ARG ALA ARG LYS ILE GLN ARG
SEQRES 33 E 480 PHE LEU SER GLN PRO PHE GLN VAL ALA GLU VAL PHE THR
SEQRES 34 E 480 GLY HIS LEU GLY LYS LEU VAL PRO LEU LYS GLU THR ILE
SEQRES 35 E 480 LYS GLY PHE GLN GLN ILE LEU ALA GLY GLU TYR ASP HIS
SEQRES 36 E 480 LEU PRO GLU GLN ALA PHE TYR MET VAL GLY PRO ILE GLU
SEQRES 37 E 480 GLU ALA VAL ALA LYS ALA ASP LYS LEU ALA GLU GLU
SEQRES 1 F 480 ALA ALA GLN ALA SER PRO SER PRO LYS ALA GLY ALA THR
SEQRES 2 F 480 THR GLY ARG ILE VAL ALA VAL ILE GLY ALA VAL VAL ASP
SEQRES 3 F 480 VAL GLN PHE ASP GLU GLY LEU PRO PRO ILE LEU ASN ALA
SEQRES 4 F 480 LEU GLU VAL GLN GLY ARG GLU THR ARG LEU VAL LEU GLU
SEQRES 5 F 480 VAL ALA GLN HIS LEU GLY GLU SER THR VAL ARG THR ILE
SEQRES 6 F 480 ALA MET ASP GLY THR GLU GLY LEU VAL ARG GLY GLN LYS
SEQRES 7 F 480 VAL LEU ASP SER GLY ALA PRO ILE ARG ILE PRO VAL GLY
SEQRES 8 F 480 PRO GLU THR LEU GLY ARG ILE MET ASN VAL ILE GLY GLU
SEQRES 9 F 480 PRO ILE ASP GLU ARG GLY PRO ILE LYS THR LYS GLN PHE
SEQRES 10 F 480 ALA ALA ILE HIS ALA GLU ALA PRO GLU PHE VAL GLU MET
SEQRES 11 F 480 SER VAL GLU GLN GLU ILE LEU VAL THR GLY ILE LYS VAL
SEQRES 12 F 480 VAL ASP LEU LEU ALA PRO TYR ALA LYS GLY GLY LYS ILE
SEQRES 13 F 480 GLY LEU PHE GLY GLY ALA GLY VAL GLY LYS THR VAL LEU
SEQRES 14 F 480 ILE MET GLU LEU ILE ASN ASN VAL ALA LYS ALA HIS GLY
SEQRES 15 F 480 GLY TYR SER VAL PHE ALA GLY VAL GLY GLU ARG THR ARG
SEQRES 16 F 480 GLU GLY ASN ASP LEU TYR HIS GLU MET ILE GLU SER GLY
SEQRES 17 F 480 VAL ILE ASN LEU LYS ASP ALA THR SER LYS VAL ALA LEU
SEQRES 18 F 480 VAL TYR GLY GLN MET ASN GLU PRO PRO GLY ALA ARG ALA
SEQRES 19 F 480 ARG VAL ALA LEU THR GLY LEU THR VAL ALA GLU TYR PHE
SEQRES 20 F 480 ARG ASP GLN GLU GLY GLN ASP VAL LEU LEU PHE ILE ASP
SEQRES 21 F 480 ASN ILE PHE ARG PHE THR GLN ALA GLY SER GLU VAL SER
SEQRES 22 F 480 ALA LEU LEU GLY ARG ILE PRO SER ALA VAL GLY TYR GLN
SEQRES 23 F 480 PRO THR LEU ALA THR ASP MET GLY THR MET GLN GLU ARG
SEQRES 24 F 480 ILE THR THR THR LYS LYS GLY SER ILE THR SER VAL GLN
SEQRES 25 F 480 ALA ILE TYR VAL PRO ALA ASP ASP LEU THR ASP PRO ALA
SEQRES 26 F 480 PRO ALA THR THR PHE ALA HIS LEU ASP ALA THR THR VAL
SEQRES 27 F 480 LEU SER ARG ALA ILE ALA GLU LEU GLY ILE TYR PRO ALA
SEQRES 28 F 480 VAL ASP PRO LEU ASP SER THR SER ARG ILE MET ASP PRO
SEQRES 29 F 480 ASN ILE VAL GLY SER GLU HIS TYR ASP VAL ALA ARG GLY
SEQRES 30 F 480 VAL GLN LYS ILE LEU GLN ASP TYR LYS SER LEU GLN ASP
SEQRES 31 F 480 ILE ILE ALA ILE LEU GLY MET ASP GLU LEU SER GLU GLU
SEQRES 32 F 480 ASP LYS LEU THR VAL SER ARG ALA ARG LYS ILE GLN ARG
SEQRES 33 F 480 PHE LEU SER GLN PRO PHE GLN VAL ALA GLU VAL PHE THR
SEQRES 34 F 480 GLY HIS LEU GLY LYS LEU VAL PRO LEU LYS GLU THR ILE
SEQRES 35 F 480 LYS GLY PHE GLN GLN ILE LEU ALA GLY GLU TYR ASP HIS
SEQRES 36 F 480 LEU PRO GLU GLN ALA PHE TYR MET VAL GLY PRO ILE GLU
SEQRES 37 F 480 GLU ALA VAL ALA LYS ALA ASP LYS LEU ALA GLU GLU
SEQRES 1 G 272 ALA THR LEU LYS ASP ILE THR ARG ARG LEU LYS SER ILE
SEQRES 2 G 272 LYS ASN ILE GLN LYS ILE THR LYS SER MET LYS MET VAL
SEQRES 3 G 272 ALA ALA ALA LYS TYR ALA ARG ALA GLU ARG GLU LEU LYS
SEQRES 4 G 272 PRO ALA ARG VAL TYR GLY VAL GLY SER LEU ALA LEU TYR
SEQRES 5 G 272 GLU LYS ALA ASP ILE LYS THR PRO GLU ASP LYS LYS LYS
SEQRES 6 G 272 HIS LEU ILE ILE GLY VAL SER SER ASP ARG GLY LEU CYS
SEQRES 7 G 272 GLY ALA ILE HIS SER SER VAL ALA LYS GLN MET LYS SER
SEQRES 8 G 272 GLU ALA ALA ASN LEU ALA ALA ALA GLY LYS GLU VAL LYS
SEQRES 9 G 272 ILE ILE GLY VAL GLY ASP LYS ILE ARG SER ILE LEU HIS
SEQRES 10 G 272 ARG THR HIS SER ASP GLN PHE LEU VAL THR PHE LYS GLU
SEQRES 11 G 272 VAL GLY ARG ARG PRO PRO THR PHE GLY ASP ALA SER VAL
SEQRES 12 G 272 ILE ALA LEU GLU LEU LEU ASN SER GLY TYR GLU PHE ASP
SEQRES 13 G 272 GLU GLY SER ILE ILE PHE ASN ARG PHE ARG SER VAL ILE
SEQRES 14 G 272 SER TYR LYS THR GLU GLU LYS PRO ILE PHE SER LEU ASP
SEQRES 15 G 272 THR ILE SER SER ALA GLU SER MET SER ILE TYR ASP ASP
SEQRES 16 G 272 ILE ASP ALA ASP VAL LEU ARG ASN TYR GLN GLU TYR SER
SEQRES 17 G 272 LEU ALA ASN ILE ILE TYR TYR SER LEU LYS GLU SER THR
SEQRES 18 G 272 THR SER GLU GLN SER ALA ARG MET THR ALA MET ASP ASN
SEQRES 19 G 272 ALA SER LYS ASN ALA SER GLU MET ILE ASP LYS LEU THR
SEQRES 20 G 272 LEU THR PHE ASN ARG THR ARG GLN ALA VAL ILE THR LYS
SEQRES 21 G 272 GLU LEU ILE GLU ILE ILE SER GLY ALA ALA ALA LEU
MODRES 1NBM TYN E 311 TYR AMINOBENZOFURAZAN-O-TYROSINE
HET TYN E 311 22
HET MG A 601 1
HET ATP A 600 31
HET MG B 601 1
HET ATP B 600 31
HET MG C 601 1
HET ATP C 600 31
HET MG D 601 1
HET ADP D 600 27
HET PO4 E 602 5
HET MG F 601 1
HET ATP F 600 31
HETNAM TYN AMINOBENZOFURAZAN-O-TYROSINE
HETNAM MG MAGNESIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM PO4 PHOSPHATE ION
FORMUL 5 TYN C15 H16 N4 O4
FORMUL 8 MG 5(MG 2+)
FORMUL 9 ATP 4(C10 H16 N5 O13 P3)
FORMUL 15 ADP C10 H15 N5 O10 P2
FORMUL 16 PO4 O4 P 3-
FORMUL 19 HOH *164(H2 O)
HELIX 1 1 ASP A 79 LEU A 81 5 3
HELIX 2 2 GLU A 101 LEU A 103 5 3
HELIX 3 3 LYS A 151 LEU A 156 1 6
HELIX 4 4 LYS A 175 ASP A 191 1 17
HELIX 5 5 ARG A 210 ASP A 222 1 13
HELIX 6 6 ALA A 225 TYR A 228 5 4
HELIX 7 7 ALA A 240 ASP A 259 1 20
HELIX 8 8 LEU A 271 LEU A 284 1 14
HELIX 9 9 ARG A 291 ALA A 293 5 3
HELIX 10 10 VAL A 298 ARG A 308 1 11
HELIX 11 11 ASP A 314 PHE A 316 5 3
HELIX 12 12 TYR A 337 ILE A 345 1 9
HELIX 13 13 THR A 354 LYS A 359 1 6
HELIX 14 14 GLY A 375 ALA A 378 5 4
HELIX 15 15 ARG A 381 ALA A 404 1 24
HELIX 16 16 ALA A 412 LEU A 427 1 16
HELIX 17 17 ILE A 438 VAL A 449 1 12
HELIX 18 18 PRO A 458 GLN A 475 1 18
HELIX 19 19 GLN A 477 ASP A 486 1 10
HELIX 20 20 GLU A 491 PHE A 508 1 18
HELIX 21 21 ASP B 79 LEU B 81 5 3
HELIX 22 22 GLU B 101 LEU B 103 5 3
HELIX 23 23 LYS B 151 LEU B 156 1 6
HELIX 24 24 LYS B 175 ASN B 190 1 16
HELIX 25 25 ARG B 210 ASP B 222 1 13
HELIX 26 26 ALA B 225 TYR B 228 5 4
HELIX 27 27 ALA B 240 ASN B 260 1 21
HELIX 28 28 LEU B 271 LEU B 284 1 14
HELIX 29 29 ARG B 291 ALA B 293 5 3
HELIX 30 30 VAL B 298 ARG B 308 1 11
HELIX 31 31 ASP B 314 PHE B 316 5 3
HELIX 32 32 TYR B 337 ILE B 343 1 7
HELIX 33 33 THR B 354 TYR B 358 1 5
HELIX 34 34 SER B 376 ALA B 378 5 3
HELIX 35 35 ARG B 381 LYS B 384 1 4
HELIX 36 36 ALA B 387 GLU B 399 1 13
HELIX 37 37 ALA B 412 LEU B 428 1 17
HELIX 38 38 ILE B 438 ARG B 450 1 13
HELIX 39 39 PRO B 458 SER B 474 1 17
HELIX 40 40 GLN B 477 ASP B 486 1 10
HELIX 41 41 GLU B 491 GLY B 507 1 17
HELIX 42 42 ASP C 79 LEU C 81 5 3
HELIX 43 43 GLU C 101 LEU C 103 5 3
HELIX 44 44 LYS C 151 LEU C 156 1 6
HELIX 45 45 LYS C 175 ASN C 190 1 16
HELIX 46 46 GLU C 195 LYS C 197 5 3
HELIX 47 47 ARG C 210 ASP C 222 1 13
HELIX 48 48 MET C 226 TYR C 228 5 3
HELIX 49 49 ALA C 240 ASN C 260 1 21
HELIX 50 50 LEU C 271 LEU C 284 1 14
HELIX 51 51 ARG C 291 ALA C 293 5 3
HELIX 52 52 VAL C 298 ARG C 308 1 11
HELIX 53 53 ASP C 314 PHE C 316 5 3
HELIX 54 54 TYR C 337 SER C 344 1 8
HELIX 55 55 THR C 354 TYR C 358 1 5
HELIX 56 56 VAL C 367 LEU C 369 5 3
HELIX 57 57 GLY C 375 ALA C 378 5 4
HELIX 58 58 ARG C 381 VAL C 386 1 6
HELIX 59 59 MET C 390 PHE C 403 1 14
HELIX 60 60 ALA C 412 LEU C 428 1 17
HELIX 61 61 ILE C 438 VAL C 449 1 12
HELIX 62 62 PRO C 458 SER C 474 1 17
HELIX 63 63 GLN C 477 ASP C 486 1 10
HELIX 64 64 GLU C 491 PHE C 508 1 18
HELIX 65 65 PRO D 88 THR D 90 5 3
HELIX 66 66 PHE D 123 GLU D 125 5 3
HELIX 67 67 LYS D 138 LEU D 143 1 6
HELIX 68 68 LYS D 162 VAL D 173 1 12
HELIX 69 69 THR D 190 GLU D 202 1 13
HELIX 70 70 PRO D 226 ARG D 244 1 19
HELIX 71 71 ILE D 258 LEU D 272 5 15
HELIX 72 72 ALA D 278 GLY D 280 5 3
HELIX 73 73 LEU D 285 ARG D 295 1 11
HELIX 74 74 PRO D 313 ASP D 315 5 3
HELIX 75 75 PRO D 320 HIS D 328 1 9
HELIX 76 76 ARG D 337 LEU D 342 1 6
HELIX 77 77 SER D 365 ILE D 388 1 24
HELIX 78 78 GLU D 398 LEU D 414 1 17
HELIX 79 79 VAL D 420 THR D 425 5 6
HELIX 80 80 LEU D 434 LEU D 445 1 12
HELIX 81 81 GLU D 454 ALA D 456 5 3
HELIX 82 82 ILE D 463 LYS D 472 1 10
HELIX 83 83 PRO E 88 THR E 90 5 3
HELIX 84 84 PHE E 123 GLU E 125 5 3
HELIX 85 85 LYS E 138 LEU E 143 1 6
HELIX 86 86 LYS E 162 HIS E 177 1 16
HELIX 87 87 THR E 190 SER E 203 1 14
HELIX 88 88 PRO E 226 GLU E 247 1 22
HELIX 89 89 PHE E 259 LEU E 271 1 13
HELIX 90 90 ALA E 278 GLY E 280 5 3
HELIX 91 91 PRO E 283 ARG E 295 5 13
HELIX 92 92 PRO E 313 ASP E 315 5 3
HELIX 93 93 PRO E 320 HIS E 328 1 9
HELIX 94 94 ARG E 337 GLU E 341 1 5
HELIX 95 95 PRO E 360 VAL E 363 1 4
HELIX 96 96 SER E 365 ILE E 388 1 24
HELIX 97 97 GLU E 398 LEU E 414 1 17
HELIX 98 98 GLN E 419 THR E 425 5 7
HELIX 99 99 LEU E 434 ALA E 446 1 13
HELIX 100 100 GLU E 454 PHE E 457 5 4
HELIX 101 101 ILE E 463 LEU E 473 1 11
HELIX 102 102 LYS F 138 LEU F 143 1 6
HELIX 103 103 LYS F 162 ASN F 172 1 11
HELIX 104 104 THR F 190 SER F 203 1 14
HELIX 105 105 PRO F 226 GLN F 246 1 21
HELIX 106 106 ILE F 258 LEU F 272 5 15
HELIX 107 107 ALA F 278 GLY F 280 5 3
HELIX 108 108 LEU F 285 ARG F 295 1 11
HELIX 109 109 PRO F 313 ASP F 315 5 3
HELIX 110 110 PRO F 320 HIS F 328 1 9
HELIX 111 111 ARG F 337 LEU F 342 1 6
HELIX 112 112 PRO F 360 VAL F 363 1 4
HELIX 113 113 SER F 365 LEU F 391 1 27
HELIX 114 114 GLU F 398 PHE F 413 1 16
HELIX 115 115 GLN F 419 THR F 425 5 7
HELIX 116 116 LEU F 434 LEU F 445 1 12
HELIX 117 117 GLU F 454 PHE F 457 5 4
HELIX 118 118 ILE F 463 LEU F 473 1 11
HELIX 119 119 LEU G 3 VAL G 43 1 41
HELIX 120 120 HIS G 82 MET G 89 1 8
HELIX 121 121 ALA G 210 ALA G 269 1 60
SHEET 1 A 6 ILE A 87 LYS A 89 0
SHEET 2 A 6 THR A 28 GLY A 35 -1 N GLY A 29 O VAL A 88
SHEET 3 A 6 ILE A 38 GLY A 43 -1 N HIS A 42 O ARG A 30
SHEET 4 A 6 ASN A 70 VAL A 75 -1 N VAL A 73 O ALA A 39
SHEET 5 A 6 LYS A 60 GLU A 67 -1 N GLU A 67 O ASN A 70
SHEET 6 A 6 GLU A 51 GLU A 54 -1 N VAL A 53 O GLY A 61
SHEET 1 B 2 ASP A 96 VAL A 99 0
SHEET 2 B 2 ALA A 125 ARG A 128 -1 N ARG A 127 O VAL A 97
SHEET 1 C 5 VAL A 107 ASP A 109 0
SHEET 2 C 5 THR A 229 ALA A 234 1 N VAL A 231 O VAL A 108
SHEET 3 C 5 TYR A 200 ILE A 206 1 N CYS A 201 O ILE A 230
SHEET 4 C 5 HIS A 263 ASP A 269 1 N LEU A 265 O TYR A 200
SHEET 5 C 5 SER A 320 PRO A 325 1 N SER A 320 O ALA A 264
SHEET 1 D 3 GLN A 349 LEU A 352 0
SHEET 2 D 3 LEU A 166 GLY A 169 1 N LEU A 166 O ILE A 350
SHEET 3 D 3 VAL A 326 GLU A 328 1 N ILE A 327 O ILE A 167
SHEET 1 E 7 THR B 28 ARG B 30 0
SHEET 2 E 7 ILE B 87 ARG B 90 -1 N VAL B 88 O GLY B 29
SHEET 3 E 7 MET B 52 PHE B 55 -1 N GLU B 54 O LYS B 89
SHEET 4 E 7 LYS B 60 LEU B 66 -1 N GLY B 61 O VAL B 53
SHEET 5 E 7 VAL B 71 VAL B 75 -1 N VAL B 74 O MET B 62
SHEET 6 E 7 ILE B 38 GLY B 43 -1 N VAL B 41 O VAL B 71
SHEET 7 E 7 GLY B 29 GLY B 35 -1 N GLY B 35 O ILE B 38
SHEET 1 F 2 ASP B 96 VAL B 99 0
SHEET 2 F 2 ALA B 125 ARG B 128 -1 N ARG B 127 O VAL B 97
SHEET 1 G 5 VAL B 107 ASP B 109 0
SHEET 2 G 5 THR B 229 ALA B 234 1 N VAL B 231 O VAL B 108
SHEET 3 G 5 TYR B 200 ILE B 206 1 N CYS B 201 O ILE B 230
SHEET 4 G 5 HIS B 263 ASP B 269 1 N LEU B 265 O TYR B 200
SHEET 5 G 5 SER B 320 PRO B 325 1 N SER B 320 O ALA B 264
SHEET 1 H 3 GLN B 349 LEU B 352 0
SHEET 2 H 3 LEU B 166 GLY B 169 1 N LEU B 166 O ILE B 350
SHEET 3 H 3 VAL B 326 GLU B 328 1 N ILE B 327 O ILE B 167
SHEET 1 I 7 THR C 28 ARG C 30 0
SHEET 2 I 7 ILE C 87 ARG C 90 -1 N VAL C 88 O GLY C 29
SHEET 3 I 7 MET C 52 PHE C 55 -1 N GLU C 54 O LYS C 89
SHEET 4 I 7 LYS C 60 LEU C 66 -1 N GLY C 61 O VAL C 53
SHEET 5 I 7 VAL C 71 VAL C 75 -1 N VAL C 74 O MET C 62
SHEET 6 I 7 ILE C 38 GLY C 43 -1 N VAL C 41 O VAL C 71
SHEET 7 I 7 GLY C 29 GLY C 35 -1 N GLY C 35 O ILE C 38
SHEET 1 J 2 ASP C 96 VAL C 99 0
SHEET 2 J 2 ALA C 125 ARG C 128 -1 N ARG C 127 O VAL C 97
SHEET 1 K 7 VAL C 107 ASP C 109 0
SHEET 2 K 7 THR C 229 ALA C 234 1 N VAL C 231 O VAL C 108
SHEET 3 K 7 TYR C 200 ILE C 206 1 N CYS C 201 O ILE C 230
SHEET 4 K 7 HIS C 263 ASP C 269 1 N LEU C 265 O TYR C 200
SHEET 5 K 7 SER C 320 GLU C 328 1 N SER C 320 O ALA C 264
SHEET 6 K 7 ARG C 164 GLY C 169 1 N GLU C 165 O ALA C 323
SHEET 7 K 7 GLN C 349 LEU C 352 1 N ILE C 350 O LEU C 166
SHEET 1 L 7 THR D 10 ARG D 12 0
SHEET 2 L 7 LYS D 74 ASP D 77 -1 N VAL D 75 O GLY D 11
SHEET 3 L 7 ALA D 35 VAL D 38 -1 N GLU D 37 O LEU D 76
SHEET 4 L 7 VAL D 46 GLN D 51 -1 N LEU D 47 O LEU D 36
SHEET 5 L 7 THR D 57 ALA D 62 -1 N ILE D 61 O GLU D 48
SHEET 6 L 7 VAL D 20 PHE D 25 -1 N VAL D 23 O VAL D 58
SHEET 7 L 7 GLY D 11 ILE D 17 -1 N ILE D 17 O VAL D 20
SHEET 1 M 2 ARG D 83 PRO D 85 0
SHEET 2 M 2 PHE D 113 ALA D 115 -1 N ALA D 114 O ILE D 84
SHEET 1 N 6 ALA D 331 VAL D 334 0
SHEET 2 N 6 ILE D 152 GLY D 156 1 N GLY D 153 O ALA D 331
SHEET 3 N 6 ILE D 304 TYR D 311 1 N GLN D 308 O ILE D 152
SHEET 4 N 6 VAL D 251 ASP D 256 1 N VAL D 251 O THR D 305
SHEET 5 N 6 SER D 181 VAL D 186 1 N VAL D 182 O LEU D 252
SHEET 6 N 6 VAL D 215 GLY D 220 1 N ALA D 216 O SER D 181
SHEET 1 O 7 THR E 10 ARG E 12 0
SHEET 2 O 7 LYS E 74 ASP E 77 -1 N VAL E 75 O GLY E 11
SHEET 3 O 7 ALA E 35 VAL E 38 -1 N GLU E 37 O LEU E 76
SHEET 4 O 7 VAL E 46 GLN E 51 -1 N LEU E 47 O LEU E 36
SHEET 5 O 7 THR E 57 ALA E 62 -1 N ILE E 61 O GLU E 48
SHEET 6 O 7 VAL E 20 GLN E 24 -1 N VAL E 23 O VAL E 58
SHEET 7 O 7 ARG E 12 ILE E 17 -1 N ILE E 17 O VAL E 20
SHEET 1 P 2 ARG E 83 VAL E 86 0
SHEET 2 P 2 GLN E 112 ALA E 115 -1 N ALA E 114 O ILE E 84
SHEET 1 Q 6 ALA E 331 VAL E 334 0
SHEET 2 Q 6 LYS E 151 PHE E 155 1 N GLY E 153 O ALA E 331
SHEET 3 Q 6 SER E 303 ALA E 309 1 N SER E 306 O ILE E 152
SHEET 4 Q 6 ASP E 250 ILE E 255 1 N VAL E 251 O SER E 303
SHEET 5 Q 6 SER E 181 GLU E 188 1 N VAL E 182 O LEU E 252
SHEET 6 Q 6 VAL E 215 GLN E 221 1 N ALA E 216 O SER E 181
SHEET 1 R 7 THR F 10 ARG F 12 0
SHEET 2 R 7 LYS F 74 ASP F 77 -1 N VAL F 75 O GLY F 11
SHEET 3 R 7 ALA F 35 VAL F 38 -1 N GLU F 37 O LEU F 76
SHEET 4 R 7 VAL F 46 HIS F 52 -1 N LEU F 47 O LEU F 36
SHEET 5 R 7 THR F 57 ALA F 62 -1 N ILE F 61 O GLU F 48
SHEET 6 R 7 VAL F 20 GLN F 24 -1 N VAL F 23 O VAL F 58
SHEET 7 R 7 ARG F 12 ILE F 17 -1 N ILE F 17 O VAL F 20
SHEET 1 S 2 ARG F 83 VAL F 86 0
SHEET 2 S 2 GLN F 112 ALA F 115 -1 N ALA F 114 O ILE F 84
SHEET 1 T 6 ALA F 331 VAL F 334 0
SHEET 2 T 6 LYS F 151 GLY F 156 1 N GLY F 153 O ALA F 331
SHEET 3 T 6 ILE F 304 TYR F 311 1 N SER F 306 O ILE F 152
SHEET 4 T 6 VAL F 251 ASP F 256 1 N VAL F 251 O THR F 305
SHEET 5 T 6 SER F 181 VAL F 186 1 N VAL F 182 O LEU F 252
SHEET 6 T 6 VAL F 215 GLY F 220 1 N ALA F 216 O SER F 181
LINK C ILE E 310 N TYN E 311 1555 1555 1.33
LINK C TYN E 311 N VAL E 312 1555 1555 1.33
LINK OG1 THR A 176 MG MG A 601 1555 1555 1.65
LINK OE1 GLN A 208 MG MG A 601 1555 1555 2.85
LINK O2G ATP A 600 MG MG A 601 1555 1555 1.86
LINK OG1 THR B 176 MG MG B 601 1555 1555 1.66
LINK OE1 GLN B 208 MG MG B 601 1555 1555 3.09
LINK O2G ATP B 600 MG MG B 601 1555 1555 2.09
LINK O2B ATP B 600 MG MG B 601 1555 1555 2.61
LINK OG1 THR C 176 MG MG C 601 1555 1555 1.62
LINK O2G ATP C 600 MG MG C 601 1555 1555 1.76
LINK O2B ATP C 600 MG MG C 601 1555 1555 2.79
LINK OG1 THR D 163 MG MG D 601 1555 1555 1.64
LINK O2B ADP D 600 MG MG D 601 1555 1555 1.70
LINK MG MG D 601 O HOH D 603 1555 1555 1.67
LINK OG1 THR F 163 MG MG F 601 1555 1555 1.62
LINK O2G ATP F 600 MG MG F 601 1555 1555 1.86
LINK O2B ATP F 600 MG MG F 601 1555 1555 2.26
CISPEP 1 ASP A 269 ASP A 270 0 -0.57
CISPEP 2 ARG A 362 PRO A 363 0 -0.54
CISPEP 3 ASP B 269 ASP B 270 0 0.59
CISPEP 4 ARG B 362 PRO B 363 0 0.01
CISPEP 5 ASP C 269 ASP C 270 0 1.68
CISPEP 6 ARG C 362 PRO C 363 0 0.22
CISPEP 7 ASP D 256 ASN D 257 0 -0.09
CISPEP 8 TYR D 345 PRO D 346 0 -0.09
CISPEP 9 ASP E 256 ASN E 257 0 -0.82
CISPEP 10 TYR E 345 PRO E 346 0 -0.27
CISPEP 11 ASP F 256 ASN F 257 0 -0.25
CISPEP 12 TYR F 345 PRO F 346 0 -0.81
SITE 1 PL1 1 LYS A 175
SITE 1 PL2 1 LYS B 175
SITE 1 PL3 1 LYS C 175
SITE 1 PL4 1 LYS D 162
SITE 1 PL5 1 LYS E 162
SITE 1 PL6 1 LYS F 162
SITE 1 CA1 2 GLU D 188 ARG C 373
SITE 1 CA2 2 GLU E 188 ARG A 373
SITE 1 CA3 2 GLU F 188 ARG B 373
SITE 1 AC1 4 THR A 176 GLN A 208 ASP A 269 ATP A 600
SITE 1 AC2 4 THR B 176 GLN B 208 ASP B 269 ATP B 600
SITE 1 AC3 3 THR C 176 ASP C 269 ATP C 600
SITE 1 AC4 3 THR D 163 ADP D 600 HOH D 603
SITE 1 AC5 6 ALA E 158 GLY E 159 VAL E 160 GLY E 161
SITE 2 AC5 6 LYS E 162 THR E 163
SITE 1 AC6 4 THR F 163 GLU F 188 GLU F 192 ATP F 600
SITE 1 AC7 13 GLN A 172 THR A 173 GLY A 174 LYS A 175
SITE 2 AC7 13 THR A 176 SER A 177 PHE A 357 ARG A 362
SITE 3 AC7 13 GLN A 430 GLN A 432 MG A 601 HOH A 606
SITE 4 AC7 13 ARG D 372
SITE 1 AC8 16 ASP B 170 ARG B 171 GLN B 172 THR B 173
SITE 2 AC8 16 GLY B 174 LYS B 175 THR B 176 SER B 177
SITE 3 AC8 16 PHE B 357 ARG B 362 GLN B 430 GLN B 432
SITE 4 AC8 16 MG B 601 HOH B 610 HOH B 615 ASP E 359
SITE 1 AC9 14 GLN C 172 THR C 173 GLY C 174 LYS C 175
SITE 2 AC9 14 THR C 176 SER C 177 PHE C 357 PRO C 363
SITE 3 AC9 14 GLN C 430 GLY C 431 GLN C 432 MG C 601
SITE 4 AC9 14 HOH C 602 HOH C 611
SITE 1 BC1 18 SER C 372 ARG C 373 GLY D 157 ALA D 158
SITE 2 BC1 18 GLY D 159 VAL D 160 GLY D 161 LYS D 162
SITE 3 BC1 18 THR D 163 VAL D 164 TYR D 345 PHE D 418
SITE 4 BC1 18 ALA D 421 PHE D 424 THR D 425 MG D 601
SITE 5 BC1 18 HOH D 603 HOH D 610
SITE 1 BC2 19 SER B 344 VAL B 371 ARG B 373 GLY F 157
SITE 2 BC2 19 GLY F 159 VAL F 160 GLY F 161 LYS F 162
SITE 3 BC2 19 THR F 163 VAL F 164 GLU F 188 ARG F 189
SITE 4 BC2 19 TYR F 345 PHE F 418 ALA F 421 PHE F 424
SITE 5 BC2 19 THR F 425 MG F 601 HOH F 609
CRYST1 281.000 106.600 138.800 90.00 90.00 90.00 P 21 21 21 12
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 0.003559 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009381 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007205 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
