Header list of 1x02.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 11-MAR-05 1X02
TITLE SOLUTION STRUCTURE OF STEREO ARRAY ISOTOPE LABELED (SAIL) CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SAIL, STEREO ARRAY ISOTOPE LABELING, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.KAINOSHO,T.TORIZAWA,T.TERAUCHI,A.M.ONO,P.GUNTERT
REVDAT 3 02-MAR-22 1X02 1 REMARK LINK
REVDAT 2 24-FEB-09 1X02 1 VERSN
REVDAT 1 07-MAR-06 1X02 0
JRNL AUTH M.KAINOSHO,T.TORIZAWA,Y.IWASHITA,T.TERAUCHI,A.MEI ONO,
JRNL AUTH 2 P.GUNTERT
JRNL TITL OPTIMAL ISOTOPE LABELLING FOR NMR PROTEIN STRUCTURE
JRNL TITL 2 DETERMINATIONS.
JRNL REF NATURE V. 440 52 2006
JRNL REFN ISSN 0028-0836
JRNL PMID 16511487
JRNL DOI 10.1038/NATURE04525
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : P.GUNTERT ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X02 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000024209.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7MM SAIL CALMODULIN, 5MM MES
REMARK 210 -D13, 10MM BIS-TRIS-D19, 5MM
REMARK 210 CACL2, 0.1MM NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.0.17, SPARKY 3.110
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: A
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 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 GLN A 3 32.77 -89.63
REMARK 500 1 GLU A 6 -36.45 -32.80
REMARK 500 1 ASP A 20 89.23 -69.03
REMARK 500 1 MET A 72 -23.66 -39.22
REMARK 500 1 SER A 81 -29.96 -38.17
REMARK 500 1 GLU A 84 -27.97 -39.35
REMARK 500 1 ASP A 93 97.19 -67.67
REMARK 500 1 ASP A 129 109.10 -55.85
REMARK 500 2 GLU A 6 -32.56 -33.37
REMARK 500 2 GLN A 41 -63.19 -100.82
REMARK 500 2 ASP A 56 109.57 -39.40
REMARK 500 2 LYS A 94 -64.09 -92.98
REMARK 500 2 ASP A 118 -36.21 -39.63
REMARK 500 2 ASP A 129 106.70 -56.99
REMARK 500 2 THR A 146 41.36 -107.53
REMARK 500 3 ASP A 2 -28.32 -39.37
REMARK 500 3 GLN A 3 37.67 -84.42
REMARK 500 3 GLU A 6 -36.16 -31.67
REMARK 500 3 ASP A 20 93.82 -67.36
REMARK 500 3 GLU A 31 -61.92 -91.85
REMARK 500 3 GLN A 41 -64.20 -105.37
REMARK 500 3 ASP A 56 107.76 -36.70
REMARK 500 3 ALA A 57 -64.18 -93.36
REMARK 500 3 ASN A 60 -44.54 -131.16
REMARK 500 3 GLU A 84 -29.94 -36.89
REMARK 500 3 ASP A 118 -34.18 -37.34
REMARK 500 4 GLN A 3 41.42 -96.64
REMARK 500 4 GLU A 6 -30.91 -32.95
REMARK 500 4 GLN A 41 -69.79 -104.94
REMARK 500 4 ASP A 56 116.70 -35.49
REMARK 500 4 ALA A 57 -63.94 -99.91
REMARK 500 4 ASP A 78 -38.86 -39.77
REMARK 500 4 GLU A 84 -30.14 -35.93
REMARK 500 4 ASP A 93 83.73 -68.36
REMARK 500 4 ASP A 129 104.07 -59.62
REMARK 500 4 THR A 146 49.71 -92.57
REMARK 500 5 THR A 5 -72.24 -135.02
REMARK 500 5 ASN A 42 60.37 -110.89
REMARK 500 5 SER A 81 -30.02 -39.70
REMARK 500 5 ASP A 93 83.83 -69.81
REMARK 500 5 LEU A 112 -38.97 -34.27
REMARK 500 5 ASP A 118 -36.74 -36.57
REMARK 500 5 ASP A 129 99.70 -59.38
REMARK 500 5 ASN A 137 -179.89 -66.56
REMARK 500 6 GLN A 3 30.97 -88.46
REMARK 500 6 GLU A 6 -28.90 -34.48
REMARK 500 6 GLN A 41 -62.46 -100.63
REMARK 500 6 ASP A 56 104.00 -43.32
REMARK 500 6 ALA A 57 -71.04 -85.94
REMARK 500 6 SER A 81 -35.04 -34.54
REMARK 500
REMARK 500 THIS ENTRY HAS 175 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 CA A 200 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD2
REMARK 620 2 ASP A 20 OD1 8.5
REMARK 620 3 ASP A 22 OD1 101.3 93.8
REMARK 620 4 ASP A 22 OD2 117.6 111.5 23.0
REMARK 620 5 ASP A 24 OD2 82.0 88.2 109.4 94.6
REMARK 620 6 ASP A 24 OD1 56.0 59.8 92.6 89.1 33.4
REMARK 620 7 THR A 26 O 76.1 80.7 151.1 162.2 98.8 108.5
REMARK 620 8 THR A 26 OG1 105.8 114.1 132.8 110.3 40.2 72.6 74.0
REMARK 620 9 GLU A 31 OE1 139.8 133.7 72.0 71.0 138.1 158.8 91.3 107.0
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 250 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD2
REMARK 620 2 ASP A 56 OD1 23.7
REMARK 620 3 ASP A 58 OD2 80.0 96.8
REMARK 620 4 ASP A 58 OD1 55.4 77.8 33.4
REMARK 620 5 ASN A 60 OD1 61.1 65.9 40.9 53.4
REMARK 620 6 THR A 62 O 101.5 82.9 97.4 121.4 68.1
REMARK 620 7 ASP A 64 OD1 145.1 137.1 76.9 109.6 84.5 56.7
REMARK 620 8 ASP A 64 OD2 133.0 150.9 54.4 78.3 86.5 95.7 41.3
REMARK 620 9 GLU A 67 OE1 99.9 102.8 126.9 104.8 156.2 133.4 114.9 99.1
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 300 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD2
REMARK 620 2 ASP A 93 OD1 21.1
REMARK 620 3 ASP A 95 OD2 80.4 96.5
REMARK 620 4 ASP A 95 OD1 57.5 62.9 43.7
REMARK 620 5 ASN A 97 OD1 63.7 84.6 48.8 75.3
REMARK 620 6 TYR A 99 O 89.5 90.7 126.7 145.0 79.8
REMARK 620 7 GLU A 104 OE1 84.8 68.5 99.7 62.4 136.6 131.5
REMARK 620 8 GLU A 104 OE2 128.5 119.6 78.4 75.1 125.2 139.9 53.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 350 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD2
REMARK 620 2 ASP A 129 OD1 32.8
REMARK 620 3 ASP A 131 OD2 83.2 71.5
REMARK 620 4 ASP A 131 OD1 80.1 55.2 28.8
REMARK 620 5 ASP A 133 OD2 93.2 100.0 38.8 67.6
REMARK 620 6 ASP A 133 OD1 56.0 73.6 52.4 74.3 38.6
REMARK 620 7 GLN A 135 O 52.0 74.5 133.9 129.5 123.0 88.7
REMARK 620 8 ASN A 137 OD1 163.4 143.7 111.8 109.6 102.9 138.6 114.0
REMARK 620 9 GLU A 140 OE1 116.5 112.4 150.4 128.2 147.2 156.8 72.4 46.9
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 350
DBREF 1X02 A 1 148 UNP P62155 CALM_XENLA 1 148
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MET MET THR ALA LYS
HET CA A 200 1
HET CA A 250 1
HET CA A 300 1
HET CA A 350 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 4(CA 2+)
HELIX 1 1 THR A 5 LEU A 18 1 14
HELIX 2 2 THR A 28 GLY A 40 1 13
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 ASP A 64 THR A 79 1 16
HELIX 5 5 SER A 81 ASP A 93 1 13
HELIX 6 6 SER A 101 GLU A 114 1 14
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 ASN A 137 THR A 146 1 10
LINK OD2 ASP A 20 CA CA A 200 1555 1555 4.86
LINK OD1 ASP A 20 CA CA A 200 1555 1555 2.73
LINK OD1 ASP A 22 CA CA A 200 1555 1555 4.47
LINK OD2 ASP A 22 CA CA A 200 1555 1555 2.78
LINK OD2 ASP A 24 CA CA A 200 1555 1555 3.90
LINK OD1 ASP A 24 CA CA A 200 1555 1555 2.79
LINK O THR A 26 CA CA A 200 1555 1555 2.31
LINK OG1 THR A 26 CA CA A 200 1555 1555 3.20
LINK OE1 GLU A 31 CA CA A 200 1555 1555 2.70
LINK OE2 GLU A 31 CA CA A 200 1555 1555 1.98
LINK OD2 ASP A 56 CA CA A 250 1555 1555 4.21
LINK OD1 ASP A 56 CA CA A 250 1555 1555 2.46
LINK OD2 ASP A 58 CA CA A 250 1555 1555 3.87
LINK OD1 ASP A 58 CA CA A 250 1555 1555 2.70
LINK OD1 ASN A 60 CA CA A 250 1555 1555 2.80
LINK O THR A 62 CA CA A 250 1555 1555 2.59
LINK OD1 ASP A 64 CA CA A 250 1555 1555 2.81
LINK OD2 ASP A 64 CA CA A 250 1555 1555 3.29
LINK OE1 GLU A 67 CA CA A 250 1555 1555 1.71
LINK OE2 GLU A 67 CA CA A 250 1555 1555 2.48
LINK OD2 ASP A 93 CA CA A 300 1555 1555 4.30
LINK OD1 ASP A 93 CA CA A 300 1555 1555 2.45
LINK OD2 ASP A 95 CA CA A 300 1555 1555 3.16
LINK OD1 ASP A 95 CA CA A 300 1555 1555 2.54
LINK OD1 ASN A 97 CA CA A 300 1555 1555 2.73
LINK O TYR A 99 CA CA A 300 1555 1555 1.89
LINK OE1 GLU A 104 CA CA A 300 1555 1555 2.58
LINK OE2 GLU A 104 CA CA A 300 1555 1555 2.22
LINK OD2 ASP A 129 CA CA A 350 1555 1555 3.92
LINK OD1 ASP A 129 CA CA A 350 1555 1555 2.74
LINK OD2 ASP A 131 CA CA A 350 1555 1555 4.18
LINK OD1 ASP A 131 CA CA A 350 1555 1555 2.79
LINK OD2 ASP A 133 CA CA A 350 1555 1555 3.52
LINK OD1 ASP A 133 CA CA A 350 1555 1555 2.70
LINK O GLN A 135 CA CA A 350 1555 1555 2.57
LINK OD1 ASN A 137 CA CA A 350 1555 1555 3.26
LINK OE1 GLU A 140 CA CA A 350 1555 1555 1.94
LINK OE2 GLU A 140 CA CA A 350 1555 1555 2.04
SITE 1 AC1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 5 GLU A 31
SITE 1 AC2 7 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 7 ILE A 63 ASP A 64 GLU A 67
SITE 1 AC3 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 5 GLU A 104
SITE 1 AC4 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 6 ASN A 137 GLU A 140
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
Complete list - r 2 2 Bytes