HEADER HYDROLASE, MEMBRANE PROTEIN 03-JAN-07 2OFG
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE ZINC(II) ATPASE
TITLE 2 ZIAA IN ITS APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC-TRANSPORTING ATPASE;
COMPND 3 CHAIN: X;
COMPND 4 FRAGMENT: RESIDUES 1-76;
COMPND 5 SYNONYM: ZN(2+)-TRANSLOCATING P-TYPE ATPASE;
COMPND 6 EC: 3.6.3.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 STRAIN: PCC 6803;
SOURCE 5 GENE: ZIAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET29A
KEYWDS FERREDOXIN-LIKE FOLD, BETA-ALPHA-BETA-BETA-ALPHA-BETA, STRUCTURAL
KEYWDS 2 GENOMICS, HYDROLASE, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,L.POGGI,N.J.ROBINSON,M.VANAROTTI
REVDAT 5 27-DEC-23 2OFG 1 REMARK
REVDAT 4 13-JUL-11 2OFG 1 VERSN
REVDAT 3 29-DEC-09 2OFG 1 JRNL
REVDAT 2 24-FEB-09 2OFG 1 VERSN
REVDAT 1 18-DEC-07 2OFG 0
JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,L.POGGI,M.VANAROTTI,
JRNL AUTH 2 S.TOTTEY,K.J.WALDRON,N.J.ROBINSON
JRNL TITL NMR STRUCTURAL ANALYSIS OF THE SOLUBLE DOMAIN OF ZIAA-ATPASE
JRNL TITL 2 AND THE BASIS OF SELECTIVE INTERACTIONS WITH COPPER
JRNL TITL 3 METALLOCHAPERONE ATX1.
JRNL REF J.BIOL.INORG.CHEM. V. 15 87 2010
JRNL REFN ISSN 0949-8257
JRNL PMID 19609573
JRNL DOI 10.1007/S00775-009-0568-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1, AMBER 8
REMARK 3 AUTHORS : GUENTERT, P., MUMENTHALER, C. WUETHRICH, K
REMARK 3 (CYANA), PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,
REMARK 3 FERGUSON (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OFG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041068.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM UNLABELED; 1.0 MM 15N
REMARK 210 -LABELED; 1.0MM 15N,13C LABELED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HNHA; HNCA-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 700 MHZ; 800
REMARK 210 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING IN TAD
REMARK 210 FOLLOWED BY RESTRAINED ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 1 MET X 1
REMARK 465 1 THR X 2
REMARK 465 1 GLN X 3
REMARK 465 1 SER X 4
REMARK 465 1 SER X 5
REMARK 465 2 LYS X 77
REMARK 465 2 SER X 78
REMARK 465 2 SER X 79
REMARK 465 2 VAL X 80
REMARK 465 2 THR X 81
REMARK 465 2 LEU X 82
REMARK 465 2 ASN X 83
REMARK 465 2 GLY X 84
REMARK 465 2 HIS X 85
REMARK 465 2 LYS X 86
REMARK 465 2 HIS X 87
REMARK 465 2 PRO X 88
REMARK 465 2 HIS X 89
REMARK 465 2 SER X 90
REMARK 465 2 HIS X 91
REMARK 465 2 ARG X 92
REMARK 465 2 GLU X 93
REMARK 465 2 GLU X 94
REMARK 465 2 GLY X 95
REMARK 465 2 HIS X 96
REMARK 465 2 SER X 97
REMARK 465 2 HIS X 98
REMARK 465 2 SER X 99
REMARK 465 2 HIS X 100
REMARK 465 2 GLY X 101
REMARK 465 2 ALA X 102
REMARK 465 2 GLY X 103
REMARK 465 2 GLU X 104
REMARK 465 2 PHE X 105
REMARK 465 2 ASN X 106
REMARK 465 2 LEU X 107
REMARK 465 2 LYS X 108
REMARK 465 2 GLN X 109
REMARK 465 2 GLU X 110
REMARK 465 2 LEU X 111
REMARK 465 3 MET X 1
REMARK 465 3 THR X 2
REMARK 465 3 GLN X 3
REMARK 465 3 SER X 4
REMARK 465 3 SER X 5
REMARK 465 3 LYS X 77
REMARK 465 3 SER X 78
REMARK 465 3 SER X 79
REMARK 465 3 VAL X 80
REMARK 465 3 THR X 81
REMARK 465 3 LEU X 82
REMARK 465 3 ASN X 83
REMARK 465 3 GLY X 84
REMARK 465 3 HIS X 85
REMARK 465 3 LYS X 86
REMARK 465 3 HIS X 87
REMARK 465 3 PRO X 88
REMARK 465 3 HIS X 89
REMARK 465 3 SER X 90
REMARK 465 3 HIS X 91
REMARK 465 3 ARG X 92
REMARK 465 3 GLU X 93
REMARK 465 3 GLU X 94
REMARK 465 3 GLY X 95
REMARK 465 3 HIS X 96
REMARK 465 3 SER X 97
REMARK 465 3 HIS X 98
REMARK 465 3 SER X 99
REMARK 465 3 HIS X 100
REMARK 465 3 GLY X 101
REMARK 465 3 ALA X 102
REMARK 465 3 GLY X 103
REMARK 465 3 GLU X 104
REMARK 465 3 PHE X 105
REMARK 465 3 ASN X 106
REMARK 465 3 LEU X 107
REMARK 465 3 LYS X 108
REMARK 465 3 GLN X 109
REMARK 465 3 GLU X 110
REMARK 465 3 LEU X 111
REMARK 465 4 MET X 1
REMARK 465 4 THR X 2
REMARK 465 4 GLN X 3
REMARK 465 4 SER X 4
REMARK 465 4 SER X 5
REMARK 465 4 LYS X 77
REMARK 465 4 SER X 78
REMARK 465 4 SER X 79
REMARK 465 4 VAL X 80
REMARK 465 4 THR X 81
REMARK 465 4 LEU X 82
REMARK 465 4 ASN X 83
REMARK 465 4 GLY X 84
REMARK 465 4 HIS X 85
REMARK 465 4 LYS X 86
REMARK 465 4 HIS X 87
REMARK 465 4 PRO X 88
REMARK 465 4 HIS X 89
REMARK 465 4 SER X 90
REMARK 465 4 HIS X 91
REMARK 465 4 ARG X 92
REMARK 465 4 GLU X 93
REMARK 465 4 GLU X 94
REMARK 465 4 GLY X 95
REMARK 465 4 HIS X 96
REMARK 465 4 SER X 97
REMARK 465 4 HIS X 98
REMARK 465 4 SER X 99
REMARK 465 4 HIS X 100
REMARK 465 4 GLY X 101
REMARK 465 4 ALA X 102
REMARK 465 4 GLY X 103
REMARK 465 4 GLU X 104
REMARK 465 4 PHE X 105
REMARK 465 4 ASN X 106
REMARK 465 4 LEU X 107
REMARK 465 4 LYS X 108
REMARK 465 4 GLN X 109
REMARK 465 4 GLU X 110
REMARK 465 4 LEU X 111
REMARK 465 5 MET X 1
REMARK 465 5 THR X 2
REMARK 465 5 GLN X 3
REMARK 465 5 SER X 4
REMARK 465 5 SER X 5
REMARK 465 5 LYS X 77
REMARK 465 5 SER X 78
REMARK 465 5 SER X 79
REMARK 465 5 VAL X 80
REMARK 465 5 THR X 81
REMARK 465 5 LEU X 82
REMARK 465 5 ASN X 83
REMARK 465 5 GLY X 84
REMARK 465 5 HIS X 85
REMARK 465 5 LYS X 86
REMARK 465 5 HIS X 87
REMARK 465 5 PRO X 88
REMARK 465 5 HIS X 89
REMARK 465 5 SER X 90
REMARK 465 5 HIS X 91
REMARK 465 5 ARG X 92
REMARK 465 5 GLU X 93
REMARK 465 5 GLU X 94
REMARK 465 5 GLY X 95
REMARK 465 5 HIS X 96
REMARK 465 5 SER X 97
REMARK 465 5 HIS X 98
REMARK 465 5 SER X 99
REMARK 465 5 HIS X 100
REMARK 465 5 GLY X 101
REMARK 465 5 ALA X 102
REMARK 465 5 GLY X 103
REMARK 465 5 GLU X 104
REMARK 465 5 PHE X 105
REMARK 465 5 ASN X 106
REMARK 465 5 LEU X 107
REMARK 465 5 LYS X 108
REMARK 465 5 GLN X 109
REMARK 465 5 GLU X 110
REMARK 465 5 LEU X 111
REMARK 465 6 MET X 1
REMARK 465 6 THR X 2
REMARK 465 6 GLN X 3
REMARK 465 6 SER X 4
REMARK 465 6 SER X 5
REMARK 465 6 LYS X 77
REMARK 465 6 SER X 78
REMARK 465 6 SER X 79
REMARK 465 6 VAL X 80
REMARK 465 6 THR X 81
REMARK 465 6 LEU X 82
REMARK 465 6 ASN X 83
REMARK 465 6 GLY X 84
REMARK 465 6 HIS X 85
REMARK 465 6 LYS X 86
REMARK 465 6 HIS X 87
REMARK 465 6 PRO X 88
REMARK 465 6 HIS X 89
REMARK 465 6 SER X 90
REMARK 465 6 HIS X 91
REMARK 465 6 ARG X 92
REMARK 465 6 GLU X 93
REMARK 465 6 GLU X 94
REMARK 465 6 GLY X 95
REMARK 465 6 HIS X 96
REMARK 465 6 SER X 97
REMARK 465 6 HIS X 98
REMARK 465 6 SER X 99
REMARK 465 6 HIS X 100
REMARK 465 6 GLY X 101
REMARK 465 6 ALA X 102
REMARK 465 6 GLY X 103
REMARK 465 6 GLU X 104
REMARK 465 6 PHE X 105
REMARK 465 6 ASN X 106
REMARK 465 6 LEU X 107
REMARK 465 6 LYS X 108
REMARK 465 6 GLN X 109
REMARK 465 6 GLU X 110
REMARK 465 6 LEU X 111
REMARK 465 7 MET X 1
REMARK 465 7 THR X 2
REMARK 465 7 GLN X 3
REMARK 465 7 SER X 4
REMARK 465 7 SER X 5
REMARK 465 7 LYS X 77
REMARK 465 7 SER X 78
REMARK 465 7 SER X 79
REMARK 465 7 VAL X 80
REMARK 465 7 THR X 81
REMARK 465 7 LEU X 82
REMARK 465 7 ASN X 83
REMARK 465 7 GLY X 84
REMARK 465 7 HIS X 85
REMARK 465 7 LYS X 86
REMARK 465 7 HIS X 87
REMARK 465 7 PRO X 88
REMARK 465 7 HIS X 89
REMARK 465 7 SER X 90
REMARK 465 7 HIS X 91
REMARK 465 7 ARG X 92
REMARK 465 7 GLU X 93
REMARK 465 7 GLU X 94
REMARK 465 7 GLY X 95
REMARK 465 7 HIS X 96
REMARK 465 7 SER X 97
REMARK 465 7 HIS X 98
REMARK 465 7 SER X 99
REMARK 465 7 HIS X 100
REMARK 465 7 GLY X 101
REMARK 465 7 ALA X 102
REMARK 465 7 GLY X 103
REMARK 465 7 GLU X 104
REMARK 465 7 PHE X 105
REMARK 465 7 ASN X 106
REMARK 465 7 LEU X 107
REMARK 465 7 LYS X 108
REMARK 465 7 GLN X 109
REMARK 465 7 GLU X 110
REMARK 465 7 LEU X 111
REMARK 465 8 MET X 1
REMARK 465 8 THR X 2
REMARK 465 8 GLN X 3
REMARK 465 8 SER X 4
REMARK 465 8 SER X 5
REMARK 465 8 LYS X 77
REMARK 465 8 SER X 78
REMARK 465 8 SER X 79
REMARK 465 8 VAL X 80
REMARK 465 8 THR X 81
REMARK 465 8 LEU X 82
REMARK 465 8 ASN X 83
REMARK 465 8 GLY X 84
REMARK 465 8 HIS X 85
REMARK 465 8 LYS X 86
REMARK 465 8 HIS X 87
REMARK 465 8 PRO X 88
REMARK 465 8 HIS X 89
REMARK 465 8 SER X 90
REMARK 465 8 HIS X 91
REMARK 465 8 ARG X 92
REMARK 465 8 GLU X 93
REMARK 465 8 GLU X 94
REMARK 465 8 GLY X 95
REMARK 465 8 HIS X 96
REMARK 465 8 SER X 97
REMARK 465 8 HIS X 98
REMARK 465 8 SER X 99
REMARK 465 8 HIS X 100
REMARK 465 8 GLY X 101
REMARK 465 8 ALA X 102
REMARK 465 8 GLY X 103
REMARK 465 8 GLU X 104
REMARK 465 8 PHE X 105
REMARK 465 8 ASN X 106
REMARK 465 8 LEU X 107
REMARK 465 8 LYS X 108
REMARK 465 8 GLN X 109
REMARK 465 8 GLU X 110
REMARK 465 8 LEU X 111
REMARK 465 9 MET X 1
REMARK 465 9 THR X 2
REMARK 465 9 GLN X 3
REMARK 465 9 SER X 4
REMARK 465 9 SER X 5
REMARK 465 9 LYS X 77
REMARK 465 9 SER X 78
REMARK 465 9 SER X 79
REMARK 465 9 VAL X 80
REMARK 465 9 THR X 81
REMARK 465 9 LEU X 82
REMARK 465 9 ASN X 83
REMARK 465 9 GLY X 84
REMARK 465 9 HIS X 85
REMARK 465 9 LYS X 86
REMARK 465 9 HIS X 87
REMARK 465 9 PRO X 88
REMARK 465 9 HIS X 89
REMARK 465 9 SER X 90
REMARK 465 9 HIS X 91
REMARK 465 9 ARG X 92
REMARK 465 9 GLU X 93
REMARK 465 9 GLU X 94
REMARK 465 9 GLY X 95
REMARK 465 9 HIS X 96
REMARK 465 9 SER X 97
REMARK 465 9 HIS X 98
REMARK 465 9 SER X 99
REMARK 465 9 HIS X 100
REMARK 465 9 GLY X 101
REMARK 465 9 ALA X 102
REMARK 465 9 GLY X 103
REMARK 465 9 GLU X 104
REMARK 465 9 PHE X 105
REMARK 465 9 ASN X 106
REMARK 465 9 LEU X 107
REMARK 465 9 LYS X 108
REMARK 465 9 GLN X 109
REMARK 465 9 GLU X 110
REMARK 465 9 LEU X 111
REMARK 465 10 MET X 1
REMARK 465 10 THR X 2
REMARK 465 10 GLN X 3
REMARK 465 10 SER X 4
REMARK 465 10 SER X 5
REMARK 465 10 LYS X 77
REMARK 465 10 SER X 78
REMARK 465 10 SER X 79
REMARK 465 10 VAL X 80
REMARK 465 10 THR X 81
REMARK 465 10 LEU X 82
REMARK 465 10 ASN X 83
REMARK 465 10 GLY X 84
REMARK 465 10 HIS X 85
REMARK 465 10 LYS X 86
REMARK 465 10 HIS X 87
REMARK 465 10 PRO X 88
REMARK 465 10 HIS X 89
REMARK 465 10 SER X 90
REMARK 465 10 HIS X 91
REMARK 465 10 ARG X 92
REMARK 465 10 GLU X 93
REMARK 465 10 GLU X 94
REMARK 465 10 GLY X 95
REMARK 465 10 HIS X 96
REMARK 465 10 SER X 97
REMARK 465 10 HIS X 98
REMARK 465 10 SER X 99
REMARK 465 10 HIS X 100
REMARK 465 10 GLY X 101
REMARK 465 10 ALA X 102
REMARK 465 10 GLY X 103
REMARK 465 10 GLU X 104
REMARK 465 10 PHE X 105
REMARK 465 10 ASN X 106
REMARK 465 10 LEU X 107
REMARK 465 10 LYS X 108
REMARK 465 10 GLN X 109
REMARK 465 10 GLU X 110
REMARK 465 10 LEU X 111
REMARK 465 11 MET X 1
REMARK 465 11 THR X 2
REMARK 465 11 GLN X 3
REMARK 465 11 SER X 4
REMARK 465 11 SER X 5
REMARK 465 11 LYS X 77
REMARK 465 11 SER X 78
REMARK 465 11 SER X 79
REMARK 465 11 VAL X 80
REMARK 465 11 THR X 81
REMARK 465 11 LEU X 82
REMARK 465 11 ASN X 83
REMARK 465 11 GLY X 84
REMARK 465 11 HIS X 85
REMARK 465 11 LYS X 86
REMARK 465 11 HIS X 87
REMARK 465 11 PRO X 88
REMARK 465 11 HIS X 89
REMARK 465 11 SER X 90
REMARK 465 11 HIS X 91
REMARK 465 11 ARG X 92
REMARK 465 11 GLU X 93
REMARK 465 11 GLU X 94
REMARK 465 11 GLY X 95
REMARK 465 11 HIS X 96
REMARK 465 11 SER X 97
REMARK 465 11 HIS X 98
REMARK 465 11 SER X 99
REMARK 465 11 HIS X 100
REMARK 465 11 GLY X 101
REMARK 465 11 ALA X 102
REMARK 465 11 GLY X 103
REMARK 465 11 GLU X 104
REMARK 465 11 PHE X 105
REMARK 465 11 ASN X 106
REMARK 465 11 LEU X 107
REMARK 465 11 LYS X 108
REMARK 465 11 GLN X 109
REMARK 465 11 GLU X 110
REMARK 465 11 LEU X 111
REMARK 465 12 MET X 1
REMARK 465 12 THR X 2
REMARK 465 12 GLN X 3
REMARK 465 12 SER X 4
REMARK 465 12 SER X 5
REMARK 465 12 LYS X 77
REMARK 465 12 SER X 78
REMARK 465 12 SER X 79
REMARK 465 12 VAL X 80
REMARK 465 12 THR X 81
REMARK 465 12 LEU X 82
REMARK 465 12 ASN X 83
REMARK 465 12 GLY X 84
REMARK 465 12 HIS X 85
REMARK 465 12 LYS X 86
REMARK 465 12 HIS X 87
REMARK 465 12 PRO X 88
REMARK 465 12 HIS X 89
REMARK 465 12 SER X 90
REMARK 465 12 HIS X 91
REMARK 465 12 ARG X 92
REMARK 465 12 GLU X 93
REMARK 465 12 GLU X 94
REMARK 465 12 GLY X 95
REMARK 465 12 HIS X 96
REMARK 465 12 SER X 97
REMARK 465 12 HIS X 98
REMARK 465 12 SER X 99
REMARK 465 12 HIS X 100
REMARK 465 12 GLY X 101
REMARK 465 12 ALA X 102
REMARK 465 12 GLY X 103
REMARK 465 12 GLU X 104
REMARK 465 12 PHE X 105
REMARK 465 12 ASN X 106
REMARK 465 12 LEU X 107
REMARK 465 12 LYS X 108
REMARK 465 12 GLN X 109
REMARK 465 12 GLU X 110
REMARK 465 12 LEU X 111
REMARK 465 13 MET X 1
REMARK 465 13 THR X 2
REMARK 465 13 GLN X 3
REMARK 465 13 SER X 4
REMARK 465 13 SER X 5
REMARK 465 13 LYS X 77
REMARK 465 13 SER X 78
REMARK 465 13 SER X 79
REMARK 465 13 VAL X 80
REMARK 465 13 THR X 81
REMARK 465 13 LEU X 82
REMARK 465 13 ASN X 83
REMARK 465 13 GLY X 84
REMARK 465 13 HIS X 85
REMARK 465 13 LYS X 86
REMARK 465 13 HIS X 87
REMARK 465 13 PRO X 88
REMARK 465 13 HIS X 89
REMARK 465 13 SER X 90
REMARK 465 13 HIS X 91
REMARK 465 13 ARG X 92
REMARK 465 13 GLU X 93
REMARK 465 13 GLU X 94
REMARK 465 13 GLY X 95
REMARK 465 13 HIS X 96
REMARK 465 13 SER X 97
REMARK 465 13 HIS X 98
REMARK 465 13 SER X 99
REMARK 465 13 HIS X 100
REMARK 465 13 GLY X 101
REMARK 465 13 ALA X 102
REMARK 465 13 GLY X 103
REMARK 465 13 GLU X 104
REMARK 465 13 PHE X 105
REMARK 465 13 ASN X 106
REMARK 465 13 LEU X 107
REMARK 465 13 LYS X 108
REMARK 465 13 GLN X 109
REMARK 465 13 GLU X 110
REMARK 465 13 LEU X 111
REMARK 465 14 MET X 1
REMARK 465 14 THR X 2
REMARK 465 14 GLN X 3
REMARK 465 14 SER X 4
REMARK 465 14 SER X 5
REMARK 465 14 LYS X 77
REMARK 465 14 SER X 78
REMARK 465 14 SER X 79
REMARK 465 14 VAL X 80
REMARK 465 14 THR X 81
REMARK 465 14 LEU X 82
REMARK 465 14 ASN X 83
REMARK 465 14 GLY X 84
REMARK 465 14 HIS X 85
REMARK 465 14 LYS X 86
REMARK 465 14 HIS X 87
REMARK 465 14 PRO X 88
REMARK 465 14 HIS X 89
REMARK 465 14 SER X 90
REMARK 465 14 HIS X 91
REMARK 465 14 ARG X 92
REMARK 465 14 GLU X 93
REMARK 465 14 GLU X 94
REMARK 465 14 GLY X 95
REMARK 465 14 HIS X 96
REMARK 465 14 SER X 97
REMARK 465 14 HIS X 98
REMARK 465 14 SER X 99
REMARK 465 14 HIS X 100
REMARK 465 14 GLY X 101
REMARK 465 14 ALA X 102
REMARK 465 14 GLY X 103
REMARK 465 14 GLU X 104
REMARK 465 14 PHE X 105
REMARK 465 14 ASN X 106
REMARK 465 14 LEU X 107
REMARK 465 14 LYS X 108
REMARK 465 14 GLN X 109
REMARK 465 14 GLU X 110
REMARK 465 14 LEU X 111
REMARK 465 15 MET X 1
REMARK 465 15 THR X 2
REMARK 465 15 GLN X 3
REMARK 465 15 SER X 4
REMARK 465 15 SER X 5
REMARK 465 15 LYS X 77
REMARK 465 15 SER X 78
REMARK 465 15 SER X 79
REMARK 465 15 VAL X 80
REMARK 465 15 THR X 81
REMARK 465 15 LEU X 82
REMARK 465 15 ASN X 83
REMARK 465 15 GLY X 84
REMARK 465 15 HIS X 85
REMARK 465 15 LYS X 86
REMARK 465 15 HIS X 87
REMARK 465 15 PRO X 88
REMARK 465 15 HIS X 89
REMARK 465 15 SER X 90
REMARK 465 15 HIS X 91
REMARK 465 15 ARG X 92
REMARK 465 15 GLU X 93
REMARK 465 15 GLU X 94
REMARK 465 15 GLY X 95
REMARK 465 15 HIS X 96
REMARK 465 15 SER X 97
REMARK 465 15 HIS X 98
REMARK 465 15 SER X 99
REMARK 465 15 HIS X 100
REMARK 465 15 GLY X 101
REMARK 465 15 ALA X 102
REMARK 465 15 GLY X 103
REMARK 465 15 GLU X 104
REMARK 465 15 PHE X 105
REMARK 465 15 ASN X 106
REMARK 465 15 LEU X 107
REMARK 465 15 LYS X 108
REMARK 465 15 GLN X 109
REMARK 465 15 GLU X 110
REMARK 465 15 LEU X 111
REMARK 465 16 MET X 1
REMARK 465 16 THR X 2
REMARK 465 16 GLN X 3
REMARK 465 16 SER X 4
REMARK 465 16 SER X 5
REMARK 465 16 LYS X 77
REMARK 465 16 SER X 78
REMARK 465 16 SER X 79
REMARK 465 16 VAL X 80
REMARK 465 16 THR X 81
REMARK 465 16 LEU X 82
REMARK 465 16 ASN X 83
REMARK 465 16 GLY X 84
REMARK 465 16 HIS X 85
REMARK 465 16 LYS X 86
REMARK 465 16 HIS X 87
REMARK 465 16 PRO X 88
REMARK 465 16 HIS X 89
REMARK 465 16 SER X 90
REMARK 465 16 HIS X 91
REMARK 465 16 ARG X 92
REMARK 465 16 GLU X 93
REMARK 465 16 GLU X 94
REMARK 465 16 GLY X 95
REMARK 465 16 HIS X 96
REMARK 465 16 SER X 97
REMARK 465 16 HIS X 98
REMARK 465 16 SER X 99
REMARK 465 16 HIS X 100
REMARK 465 16 GLY X 101
REMARK 465 16 ALA X 102
REMARK 465 16 GLY X 103
REMARK 465 16 GLU X 104
REMARK 465 16 PHE X 105
REMARK 465 16 ASN X 106
REMARK 465 16 LEU X 107
REMARK 465 16 LYS X 108
REMARK 465 16 GLN X 109
REMARK 465 16 GLU X 110
REMARK 465 16 LEU X 111
REMARK 465 17 MET X 1
REMARK 465 17 THR X 2
REMARK 465 17 GLN X 3
REMARK 465 17 SER X 4
REMARK 465 17 SER X 5
REMARK 465 17 LYS X 77
REMARK 465 17 SER X 78
REMARK 465 17 SER X 79
REMARK 465 17 VAL X 80
REMARK 465 17 THR X 81
REMARK 465 17 LEU X 82
REMARK 465 17 ASN X 83
REMARK 465 17 GLY X 84
REMARK 465 17 HIS X 85
REMARK 465 17 LYS X 86
REMARK 465 17 HIS X 87
REMARK 465 17 PRO X 88
REMARK 465 17 HIS X 89
REMARK 465 17 SER X 90
REMARK 465 17 HIS X 91
REMARK 465 17 ARG X 92
REMARK 465 17 GLU X 93
REMARK 465 17 GLU X 94
REMARK 465 17 GLY X 95
REMARK 465 17 HIS X 96
REMARK 465 17 SER X 97
REMARK 465 17 HIS X 98
REMARK 465 17 SER X 99
REMARK 465 17 HIS X 100
REMARK 465 17 GLY X 101
REMARK 465 17 ALA X 102
REMARK 465 17 GLY X 103
REMARK 465 17 GLU X 104
REMARK 465 17 PHE X 105
REMARK 465 17 ASN X 106
REMARK 465 17 LEU X 107
REMARK 465 17 LYS X 108
REMARK 465 17 GLN X 109
REMARK 465 17 GLU X 110
REMARK 465 17 LEU X 111
REMARK 465 18 MET X 1
REMARK 465 18 THR X 2
REMARK 465 18 GLN X 3
REMARK 465 18 SER X 4
REMARK 465 18 SER X 5
REMARK 465 18 LYS X 77
REMARK 465 18 SER X 78
REMARK 465 18 SER X 79
REMARK 465 18 VAL X 80
REMARK 465 18 THR X 81
REMARK 465 18 LEU X 82
REMARK 465 18 ASN X 83
REMARK 465 18 GLY X 84
REMARK 465 18 HIS X 85
REMARK 465 18 LYS X 86
REMARK 465 18 HIS X 87
REMARK 465 18 PRO X 88
REMARK 465 18 HIS X 89
REMARK 465 18 SER X 90
REMARK 465 18 HIS X 91
REMARK 465 18 ARG X 92
REMARK 465 18 GLU X 93
REMARK 465 18 GLU X 94
REMARK 465 18 GLY X 95
REMARK 465 18 HIS X 96
REMARK 465 18 SER X 97
REMARK 465 18 HIS X 98
REMARK 465 18 SER X 99
REMARK 465 18 HIS X 100
REMARK 465 18 GLY X 101
REMARK 465 18 ALA X 102
REMARK 465 18 GLY X 103
REMARK 465 18 GLU X 104
REMARK 465 18 PHE X 105
REMARK 465 18 ASN X 106
REMARK 465 18 LEU X 107
REMARK 465 18 LYS X 108
REMARK 465 18 GLN X 109
REMARK 465 18 GLU X 110
REMARK 465 18 LEU X 111
REMARK 465 19 MET X 1
REMARK 465 19 THR X 2
REMARK 465 19 GLN X 3
REMARK 465 19 SER X 4
REMARK 465 19 SER X 5
REMARK 465 19 LYS X 77
REMARK 465 19 SER X 78
REMARK 465 19 SER X 79
REMARK 465 19 VAL X 80
REMARK 465 19 THR X 81
REMARK 465 19 LEU X 82
REMARK 465 19 ASN X 83
REMARK 465 19 GLY X 84
REMARK 465 19 HIS X 85
REMARK 465 19 LYS X 86
REMARK 465 19 HIS X 87
REMARK 465 19 PRO X 88
REMARK 465 19 HIS X 89
REMARK 465 19 SER X 90
REMARK 465 19 HIS X 91
REMARK 465 19 ARG X 92
REMARK 465 19 GLU X 93
REMARK 465 19 GLU X 94
REMARK 465 19 GLY X 95
REMARK 465 19 HIS X 96
REMARK 465 19 SER X 97
REMARK 465 19 HIS X 98
REMARK 465 19 SER X 99
REMARK 465 19 HIS X 100
REMARK 465 19 GLY X 101
REMARK 465 19 ALA X 102
REMARK 465 19 GLY X 103
REMARK 465 19 GLU X 104
REMARK 465 19 PHE X 105
REMARK 465 19 ASN X 106
REMARK 465 19 LEU X 107
REMARK 465 19 LYS X 108
REMARK 465 19 GLN X 109
REMARK 465 19 GLU X 110
REMARK 465 19 LEU X 111
REMARK 465 20 MET X 1
REMARK 465 20 THR X 2
REMARK 465 20 GLN X 3
REMARK 465 20 SER X 4
REMARK 465 20 SER X 5
REMARK 465 20 LYS X 77
REMARK 465 20 SER X 78
REMARK 465 20 SER X 79
REMARK 465 20 VAL X 80
REMARK 465 20 THR X 81
REMARK 465 20 LEU X 82
REMARK 465 20 ASN X 83
REMARK 465 20 GLY X 84
REMARK 465 20 HIS X 85
REMARK 465 20 LYS X 86
REMARK 465 20 HIS X 87
REMARK 465 20 PRO X 88
REMARK 465 20 HIS X 89
REMARK 465 20 SER X 90
REMARK 465 20 HIS X 91
REMARK 465 20 ARG X 92
REMARK 465 20 GLU X 93
REMARK 465 20 GLU X 94
REMARK 465 20 GLY X 95
REMARK 465 20 HIS X 96
REMARK 465 20 SER X 97
REMARK 465 20 HIS X 98
REMARK 465 20 SER X 99
REMARK 465 20 HIS X 100
REMARK 465 20 GLY X 101
REMARK 465 20 ALA X 102
REMARK 465 20 GLY X 103
REMARK 465 20 GLU X 104
REMARK 465 20 PHE X 105
REMARK 465 20 ASN X 106
REMARK 465 20 LEU X 107
REMARK 465 20 LYS X 108
REMARK 465 20 GLN X 109
REMARK 465 20 GLU X 110
REMARK 465 20 LEU X 111
REMARK 465 21 MET X 1
REMARK 465 21 THR X 2
REMARK 465 21 GLN X 3
REMARK 465 21 SER X 4
REMARK 465 21 SER X 5
REMARK 465 21 LYS X 77
REMARK 465 21 SER X 78
REMARK 465 21 SER X 79
REMARK 465 21 VAL X 80
REMARK 465 21 THR X 81
REMARK 465 21 LEU X 82
REMARK 465 21 ASN X 83
REMARK 465 21 GLY X 84
REMARK 465 21 HIS X 85
REMARK 465 21 LYS X 86
REMARK 465 21 HIS X 87
REMARK 465 21 PRO X 88
REMARK 465 21 HIS X 89
REMARK 465 21 SER X 90
REMARK 465 21 HIS X 91
REMARK 465 21 ARG X 92
REMARK 465 21 GLU X 93
REMARK 465 21 GLU X 94
REMARK 465 21 GLY X 95
REMARK 465 21 HIS X 96
REMARK 465 21 SER X 97
REMARK 465 21 HIS X 98
REMARK 465 21 SER X 99
REMARK 465 21 HIS X 100
REMARK 465 21 GLY X 101
REMARK 465 21 ALA X 102
REMARK 465 21 GLY X 103
REMARK 465 21 GLU X 104
REMARK 465 21 PHE X 105
REMARK 465 21 ASN X 106
REMARK 465 21 LEU X 107
REMARK 465 21 LYS X 108
REMARK 465 21 GLN X 109
REMARK 465 21 GLU X 110
REMARK 465 21 LEU X 111
REMARK 465 22 MET X 1
REMARK 465 22 THR X 2
REMARK 465 22 GLN X 3
REMARK 465 22 SER X 4
REMARK 465 22 SER X 5
REMARK 465 22 LYS X 77
REMARK 465 22 SER X 78
REMARK 465 22 SER X 79
REMARK 465 22 VAL X 80
REMARK 465 22 THR X 81
REMARK 465 22 LEU X 82
REMARK 465 22 ASN X 83
REMARK 465 22 GLY X 84
REMARK 465 22 HIS X 85
REMARK 465 22 LYS X 86
REMARK 465 22 HIS X 87
REMARK 465 22 PRO X 88
REMARK 465 22 HIS X 89
REMARK 465 22 SER X 90
REMARK 465 22 HIS X 91
REMARK 465 22 ARG X 92
REMARK 465 22 GLU X 93
REMARK 465 22 GLU X 94
REMARK 465 22 GLY X 95
REMARK 465 22 HIS X 96
REMARK 465 22 SER X 97
REMARK 465 22 HIS X 98
REMARK 465 22 SER X 99
REMARK 465 22 HIS X 100
REMARK 465 22 GLY X 101
REMARK 465 22 ALA X 102
REMARK 465 22 GLY X 103
REMARK 465 22 GLU X 104
REMARK 465 22 PHE X 105
REMARK 465 22 ASN X 106
REMARK 465 22 LEU X 107
REMARK 465 22 LYS X 108
REMARK 465 22 GLN X 109
REMARK 465 22 GLU X 110
REMARK 465 22 LEU X 111
REMARK 465 23 MET X 1
REMARK 465 23 THR X 2
REMARK 465 23 GLN X 3
REMARK 465 23 SER X 4
REMARK 465 23 SER X 5
REMARK 465 23 LYS X 77
REMARK 465 23 SER X 78
REMARK 465 23 SER X 79
REMARK 465 23 VAL X 80
REMARK 465 23 THR X 81
REMARK 465 23 LEU X 82
REMARK 465 23 ASN X 83
REMARK 465 23 GLY X 84
REMARK 465 23 HIS X 85
REMARK 465 23 LYS X 86
REMARK 465 23 HIS X 87
REMARK 465 23 PRO X 88
REMARK 465 23 HIS X 89
REMARK 465 23 SER X 90
REMARK 465 23 HIS X 91
REMARK 465 23 ARG X 92
REMARK 465 23 GLU X 93
REMARK 465 23 GLU X 94
REMARK 465 23 GLY X 95
REMARK 465 23 HIS X 96
REMARK 465 23 SER X 97
REMARK 465 23 HIS X 98
REMARK 465 23 SER X 99
REMARK 465 23 HIS X 100
REMARK 465 23 GLY X 101
REMARK 465 23 ALA X 102
REMARK 465 23 GLY X 103
REMARK 465 23 GLU X 104
REMARK 465 23 PHE X 105
REMARK 465 23 ASN X 106
REMARK 465 23 LEU X 107
REMARK 465 23 LYS X 108
REMARK 465 23 GLN X 109
REMARK 465 23 GLU X 110
REMARK 465 23 LEU X 111
REMARK 465 24 MET X 1
REMARK 465 24 THR X 2
REMARK 465 24 GLN X 3
REMARK 465 24 SER X 4
REMARK 465 24 SER X 5
REMARK 465 24 LYS X 77
REMARK 465 24 SER X 78
REMARK 465 24 SER X 79
REMARK 465 24 VAL X 80
REMARK 465 24 THR X 81
REMARK 465 24 LEU X 82
REMARK 465 24 ASN X 83
REMARK 465 24 GLY X 84
REMARK 465 24 HIS X 85
REMARK 465 24 LYS X 86
REMARK 465 24 HIS X 87
REMARK 465 24 PRO X 88
REMARK 465 24 HIS X 89
REMARK 465 24 SER X 90
REMARK 465 24 HIS X 91
REMARK 465 24 ARG X 92
REMARK 465 24 GLU X 93
REMARK 465 24 GLU X 94
REMARK 465 24 GLY X 95
REMARK 465 24 HIS X 96
REMARK 465 24 SER X 97
REMARK 465 24 HIS X 98
REMARK 465 24 SER X 99
REMARK 465 24 HIS X 100
REMARK 465 24 GLY X 101
REMARK 465 24 ALA X 102
REMARK 465 24 GLY X 103
REMARK 465 24 GLU X 104
REMARK 465 24 PHE X 105
REMARK 465 24 ASN X 106
REMARK 465 24 LEU X 107
REMARK 465 24 LYS X 108
REMARK 465 24 GLN X 109
REMARK 465 24 GLU X 110
REMARK 465 24 LEU X 111
REMARK 465 25 MET X 1
REMARK 465 25 THR X 2
REMARK 465 25 GLN X 3
REMARK 465 25 SER X 4
REMARK 465 25 SER X 5
REMARK 465 25 LYS X 77
REMARK 465 25 SER X 78
REMARK 465 25 SER X 79
REMARK 465 25 VAL X 80
REMARK 465 25 THR X 81
REMARK 465 25 LEU X 82
REMARK 465 25 ASN X 83
REMARK 465 25 GLY X 84
REMARK 465 25 HIS X 85
REMARK 465 25 LYS X 86
REMARK 465 25 HIS X 87
REMARK 465 25 PRO X 88
REMARK 465 25 HIS X 89
REMARK 465 25 SER X 90
REMARK 465 25 HIS X 91
REMARK 465 25 ARG X 92
REMARK 465 25 GLU X 93
REMARK 465 25 GLU X 94
REMARK 465 25 GLY X 95
REMARK 465 25 HIS X 96
REMARK 465 25 SER X 97
REMARK 465 25 HIS X 98
REMARK 465 25 SER X 99
REMARK 465 25 HIS X 100
REMARK 465 25 GLY X 101
REMARK 465 25 ALA X 102
REMARK 465 25 GLY X 103
REMARK 465 25 GLU X 104
REMARK 465 25 PHE X 105
REMARK 465 25 ASN X 106
REMARK 465 25 LEU X 107
REMARK 465 25 LYS X 108
REMARK 465 25 GLN X 109
REMARK 465 25 GLU X 110
REMARK 465 25 LEU X 111
REMARK 465 26 MET X 1
REMARK 465 26 THR X 2
REMARK 465 26 GLN X 3
REMARK 465 26 SER X 4
REMARK 465 26 SER X 5
REMARK 465 26 LYS X 77
REMARK 465 26 SER X 78
REMARK 465 26 SER X 79
REMARK 465 26 VAL X 80
REMARK 465 26 THR X 81
REMARK 465 26 LEU X 82
REMARK 465 26 ASN X 83
REMARK 465 26 GLY X 84
REMARK 465 26 HIS X 85
REMARK 465 26 LYS X 86
REMARK 465 26 HIS X 87
REMARK 465 26 PRO X 88
REMARK 465 26 HIS X 89
REMARK 465 26 SER X 90
REMARK 465 26 HIS X 91
REMARK 465 26 ARG X 92
REMARK 465 26 GLU X 93
REMARK 465 26 GLU X 94
REMARK 465 26 GLY X 95
REMARK 465 26 HIS X 96
REMARK 465 26 SER X 97
REMARK 465 26 HIS X 98
REMARK 465 26 SER X 99
REMARK 465 26 HIS X 100
REMARK 465 26 GLY X 101
REMARK 465 26 ALA X 102
REMARK 465 26 GLY X 103
REMARK 465 26 GLU X 104
REMARK 465 26 PHE X 105
REMARK 465 26 ASN X 106
REMARK 465 26 LEU X 107
REMARK 465 26 LYS X 108
REMARK 465 26 GLN X 109
REMARK 465 26 GLU X 110
REMARK 465 26 LEU X 111
REMARK 465 27 MET X 1
REMARK 465 27 THR X 2
REMARK 465 27 GLN X 3
REMARK 465 27 SER X 4
REMARK 465 27 SER X 5
REMARK 465 27 LYS X 77
REMARK 465 27 SER X 78
REMARK 465 27 SER X 79
REMARK 465 27 VAL X 80
REMARK 465 27 THR X 81
REMARK 465 27 LEU X 82
REMARK 465 27 ASN X 83
REMARK 465 27 GLY X 84
REMARK 465 27 HIS X 85
REMARK 465 27 LYS X 86
REMARK 465 27 HIS X 87
REMARK 465 27 PRO X 88
REMARK 465 27 HIS X 89
REMARK 465 27 SER X 90
REMARK 465 27 HIS X 91
REMARK 465 27 ARG X 92
REMARK 465 27 GLU X 93
REMARK 465 27 GLU X 94
REMARK 465 27 GLY X 95
REMARK 465 27 HIS X 96
REMARK 465 27 SER X 97
REMARK 465 27 HIS X 98
REMARK 465 27 SER X 99
REMARK 465 27 HIS X 100
REMARK 465 27 GLY X 101
REMARK 465 27 ALA X 102
REMARK 465 27 GLY X 103
REMARK 465 27 GLU X 104
REMARK 465 27 PHE X 105
REMARK 465 27 ASN X 106
REMARK 465 27 LEU X 107
REMARK 465 27 LYS X 108
REMARK 465 27 GLN X 109
REMARK 465 27 GLU X 110
REMARK 465 27 LEU X 111
REMARK 465 28 MET X 1
REMARK 465 28 THR X 2
REMARK 465 28 GLN X 3
REMARK 465 28 SER X 4
REMARK 465 28 SER X 5
REMARK 465 28 LYS X 77
REMARK 465 28 SER X 78
REMARK 465 28 SER X 79
REMARK 465 28 VAL X 80
REMARK 465 28 THR X 81
REMARK 465 28 LEU X 82
REMARK 465 28 ASN X 83
REMARK 465 28 GLY X 84
REMARK 465 28 HIS X 85
REMARK 465 28 LYS X 86
REMARK 465 28 HIS X 87
REMARK 465 28 PRO X 88
REMARK 465 28 HIS X 89
REMARK 465 28 SER X 90
REMARK 465 28 HIS X 91
REMARK 465 28 ARG X 92
REMARK 465 28 GLU X 93
REMARK 465 28 GLU X 94
REMARK 465 28 GLY X 95
REMARK 465 28 HIS X 96
REMARK 465 28 SER X 97
REMARK 465 28 HIS X 98
REMARK 465 28 SER X 99
REMARK 465 28 HIS X 100
REMARK 465 28 GLY X 101
REMARK 465 28 ALA X 102
REMARK 465 28 GLY X 103
REMARK 465 28 GLU X 104
REMARK 465 28 PHE X 105
REMARK 465 28 ASN X 106
REMARK 465 28 LEU X 107
REMARK 465 28 LYS X 108
REMARK 465 28 GLN X 109
REMARK 465 28 GLU X 110
REMARK 465 28 LEU X 111
REMARK 465 29 MET X 1
REMARK 465 29 THR X 2
REMARK 465 29 GLN X 3
REMARK 465 29 SER X 4
REMARK 465 29 SER X 5
REMARK 465 29 LYS X 77
REMARK 465 29 SER X 78
REMARK 465 29 SER X 79
REMARK 465 29 VAL X 80
REMARK 465 29 THR X 81
REMARK 465 29 LEU X 82
REMARK 465 29 ASN X 83
REMARK 465 29 GLY X 84
REMARK 465 29 HIS X 85
REMARK 465 29 LYS X 86
REMARK 465 29 HIS X 87
REMARK 465 29 PRO X 88
REMARK 465 29 HIS X 89
REMARK 465 29 SER X 90
REMARK 465 29 HIS X 91
REMARK 465 29 ARG X 92
REMARK 465 29 GLU X 93
REMARK 465 29 GLU X 94
REMARK 465 29 GLY X 95
REMARK 465 29 HIS X 96
REMARK 465 29 SER X 97
REMARK 465 29 HIS X 98
REMARK 465 29 SER X 99
REMARK 465 29 HIS X 100
REMARK 465 29 GLY X 101
REMARK 465 29 ALA X 102
REMARK 465 29 GLY X 103
REMARK 465 29 GLU X 104
REMARK 465 29 PHE X 105
REMARK 465 29 ASN X 106
REMARK 465 29 LEU X 107
REMARK 465 29 LYS X 108
REMARK 465 29 GLN X 109
REMARK 465 29 GLU X 110
REMARK 465 29 LEU X 111
REMARK 465 30 MET X 1
REMARK 465 30 THR X 2
REMARK 465 30 GLN X 3
REMARK 465 30 SER X 4
REMARK 465 30 SER X 5
REMARK 465 30 LYS X 77
REMARK 465 30 SER X 78
REMARK 465 30 SER X 79
REMARK 465 30 VAL X 80
REMARK 465 30 THR X 81
REMARK 465 30 LEU X 82
REMARK 465 30 ASN X 83
REMARK 465 30 GLY X 84
REMARK 465 30 HIS X 85
REMARK 465 30 LYS X 86
REMARK 465 30 HIS X 87
REMARK 465 30 PRO X 88
REMARK 465 30 HIS X 89
REMARK 465 30 SER X 90
REMARK 465 30 HIS X 91
REMARK 465 30 ARG X 92
REMARK 465 30 GLU X 93
REMARK 465 30 GLU X 94
REMARK 465 30 GLY X 95
REMARK 465 30 HIS X 96
REMARK 465 30 SER X 97
REMARK 465 30 HIS X 98
REMARK 465 30 SER X 99
REMARK 465 30 HIS X 100
REMARK 465 30 GLY X 101
REMARK 465 30 ALA X 102
REMARK 465 30 GLY X 103
REMARK 465 30 GLU X 104
REMARK 465 30 PHE X 105
REMARK 465 30 ASN X 106
REMARK 465 30 LEU X 107
REMARK 465 30 LYS X 108
REMARK 465 30 GLN X 109
REMARK 465 30 GLU X 110
REMARK 465 30 LEU X 111
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 2 ARG X 47 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ARG X 47 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 4 ARG X 32 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 5 ARG X 32 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 6 ARG X 32 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 7 ARG X 47 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 8 TYR X 71 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 9 ARG X 47 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 9 ARG X 65 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 10 ARG X 65 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 12 ARG X 65 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 12 TYR X 71 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 21 ARG X 32 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 22 TYR X 71 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 23 ARG X 32 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 23 ARG X 47 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 24 ARG X 65 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 27 ARG X 32 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 28 ARG X 65 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 30 ARG X 32 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 MET X 17 99.95 60.36
REMARK 500 1 ASP X 18 52.73 -64.33
REMARK 500 1 CYS X 19 -126.91 55.30
REMARK 500 1 CYS X 22 -39.51 -165.52
REMARK 500 1 ILE X 26 -73.56 -72.40
REMARK 500 1 LEU X 33 -159.67 -89.01
REMARK 500 1 THR X 45 10.06 -149.63
REMARK 500 1 GLN X 56 -52.10 -150.23
REMARK 500 1 VAL X 57 136.37 -171.32
REMARK 500 1 SER X 58 -72.40 -145.29
REMARK 500 1 ALA X 68 29.76 -72.98
REMARK 500 1 SER X 78 18.63 52.25
REMARK 500 1 SER X 79 42.06 -79.40
REMARK 500 1 LEU X 82 -88.36 -155.20
REMARK 500 1 ASN X 83 11.17 58.50
REMARK 500 1 HIS X 87 143.27 79.26
REMARK 500 1 SER X 90 -176.28 146.76
REMARK 500 1 ARG X 92 -160.40 -175.07
REMARK 500 1 GLU X 93 134.61 148.07
REMARK 500 1 GLU X 94 6.75 -167.25
REMARK 500 1 HIS X 98 -175.39 170.30
REMARK 500 1 GLU X 104 56.34 -152.41
REMARK 500 1 GLN X 109 -48.43 -166.01
REMARK 500 1 GLU X 110 -39.52 74.36
REMARK 500 2 SER X 4 85.73 -168.01
REMARK 500 2 ASP X 18 -127.73 -65.77
REMARK 500 2 CYS X 19 -73.61 -121.73
REMARK 500 2 CYS X 22 -71.28 -148.66
REMARK 500 2 ILE X 26 -73.70 -73.06
REMARK 500 2 ALA X 44 0.66 -63.13
REMARK 500 2 GLN X 56 -33.90 -166.53
REMARK 500 2 SER X 58 -101.59 -167.42
REMARK 500 2 ALA X 68 22.43 -70.34
REMARK 500 3 CYS X 22 -68.19 -159.62
REMARK 500 3 ILE X 26 -71.48 -62.96
REMARK 500 3 ALA X 44 11.83 -69.70
REMARK 500 3 THR X 45 -4.65 -143.03
REMARK 500 3 GLN X 56 -32.73 -154.01
REMARK 500 3 SER X 58 -113.67 -132.17
REMARK 500 4 MET X 17 15.78 86.95
REMARK 500 4 ASP X 18 -128.66 67.09
REMARK 500 4 CYS X 19 -37.35 -157.64
REMARK 500 4 THR X 20 -61.04 -125.32
REMARK 500 4 SER X 21 4.21 -61.47
REMARK 500 4 CYS X 22 -46.62 -155.90
REMARK 500 4 ALA X 44 -13.66 69.72
REMARK 500 4 GLN X 56 -62.85 -164.27
REMARK 500 4 SER X 58 -99.85 -147.92
REMARK 500 5 MET X 17 -176.44 58.62
REMARK 500 5 ASP X 18 -128.16 176.91
REMARK 500
REMARK 500 THIS ENTRY HAS 298 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER X 21 CYS X 22 3 -135.54
REMARK 500 LEU X 33 LYS X 34 5 -140.99
REMARK 500 GLN X 56 VAL X 57 7 138.13
REMARK 500 GLY X 28 SER X 29 11 149.18
REMARK 500 ASP X 18 CYS X 19 17 -147.41
REMARK 500 GLY X 28 SER X 29 17 146.58
REMARK 500 GLY X 35 VAL X 36 19 138.43
REMARK 500 MET X 17 ASP X 18 21 148.19
REMARK 500 GLY X 28 SER X 29 22 146.82
REMARK 500 MET X 17 ASP X 18 25 131.11
REMARK 500 SER X 21 CYS X 22 25 -145.49
REMARK 500 ASP X 18 CYS X 19 26 146.33
REMARK 500 MET X 17 ASP X 18 28 145.63
REMARK 500 GLY X 28 SER X 29 28 149.14
REMARK 500 GLY X 28 SER X 29 29 149.44
REMARK 500 MET X 17 ASP X 18 30 129.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG X 32 0.08 SIDE CHAIN
REMARK 500 1 TYR X 71 0.07 SIDE CHAIN
REMARK 500 3 TYR X 52 0.08 SIDE CHAIN
REMARK 500 4 ARG X 65 0.09 SIDE CHAIN
REMARK 500 5 TYR X 52 0.10 SIDE CHAIN
REMARK 500 7 ARG X 32 0.08 SIDE CHAIN
REMARK 500 8 ARG X 47 0.09 SIDE CHAIN
REMARK 500 15 ARG X 65 0.07 SIDE CHAIN
REMARK 500 15 TYR X 71 0.10 SIDE CHAIN
REMARK 500 17 ARG X 47 0.08 SIDE CHAIN
REMARK 500 18 ARG X 65 0.08 SIDE CHAIN
REMARK 500 19 ARG X 32 0.10 SIDE CHAIN
REMARK 500 19 ARG X 65 0.10 SIDE CHAIN
REMARK 500 20 ARG X 65 0.10 SIDE CHAIN
REMARK 500 24 ARG X 65 0.14 SIDE CHAIN
REMARK 500 25 ARG X 65 0.08 SIDE CHAIN
REMARK 500 29 TYR X 52 0.09 SIDE CHAIN
REMARK 500 29 ARG X 65 0.10 SIDE CHAIN
REMARK 500 30 ARG X 47 0.09 SIDE CHAIN
REMARK 500 30 ARG X 65 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OFH RELATED DB: PDB
DBREF 2OFG X 1 111 UNP Q59998 ATZN_SYNY3 1 111
SEQRES 1 X 111 MET THR GLN SER SER PRO LEU LYS THR GLN GLN MET GLN
SEQRES 2 X 111 VAL GLY GLY MET ASP CYS THR SER CYS LYS LEU LYS ILE
SEQRES 3 X 111 GLU GLY SER LEU GLU ARG LEU LYS GLY VAL ALA GLU ALA
SEQRES 4 X 111 SER VAL THR VAL ALA THR GLY ARG LEU THR VAL THR TYR
SEQRES 5 X 111 ASP PRO LYS GLN VAL SER GLU ILE THR ILE GLN GLU ARG
SEQRES 6 X 111 ILE ALA ALA LEU GLY TYR THR LEU ALA GLU PRO LYS SER
SEQRES 7 X 111 SER VAL THR LEU ASN GLY HIS LYS HIS PRO HIS SER HIS
SEQRES 8 X 111 ARG GLU GLU GLY HIS SER HIS SER HIS GLY ALA GLY GLU
SEQRES 9 X 111 PHE ASN LEU LYS GLN GLU LEU
HELIX 1 1 ASP X 18 SER X 21 5 4
HELIX 2 2 CYS X 22 GLU X 31 1 10
HELIX 3 3 SER X 58 ALA X 68 1 11
SHEET 1 A 4 VAL X 36 THR X 42 0
SHEET 2 A 4 ARG X 47 TYR X 52 -1 O ARG X 47 N THR X 42
SHEET 3 A 4 LYS X 8 VAL X 14 -1 N GLN X 10 O VAL X 50
SHEET 4 A 4 LEU X 73 ALA X 74 -1 O ALA X 74 N GLN X 13
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
