Header list of 1crr.pdb file
Complete list - b 16 2 Bytes
HEADER ONCOGENE PROTEIN 24-NOV-93 1CRR
TITLE THE SOLUTION STRUCTURE AND DYNAMICS OF RAS P21. GDP DETERMINED BY
TITLE 2 HETERONUCLEAR THREE AND FOUR DIMENSIONAL NMR SPECTROSCOPY
SPLIT 1CRP 1CRR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-H-RAS P21 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS ONCOGENE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.J.KRAULIS,P.J.DOMAILLE,S.L.CAMPBELL-BURK,T.VAN AKEN,E.D.LAUE
REVDAT 3 16-FEB-22 1CRR 1 REMARK LINK
REVDAT 2 24-FEB-09 1CRR 1 VERSN
REVDAT 1 31-JUL-94 1CRR 0
JRNL AUTH P.J.KRAULIS,P.J.DOMAILLE,S.L.CAMPBELL-BURK,T.VAN AKEN,
JRNL AUTH 2 E.D.LAUE
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF RAS P21.GDP DETERMINED BY
JRNL TITL 2 HETERONUCLEAR THREE- AND FOUR-DIMENSIONAL NMR SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 33 3515 1994
JRNL REFN ISSN 0006-2960
JRNL PMID 8142349
JRNL DOI 10.1021/BI00178A008
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.L.CAMPBELL-BURK,P.J.DOMAILLE,M.A.STAROVASNIK,W.BOUCHER,
REMARK 1 AUTH 2 E.D.LAUE
REMARK 1 TITL SEQUENTIAL ASSIGNMENT OF THE BACKBONE NUCLEI (1H, 15N, AND
REMARK 1 TITL 2 13C) OF C-H-RAS P21 (1-166).GDP USING A NOVEL 4D NMR
REMARK 1 TITL 3 STRATEGY
REMARK 1 REF J.BIOMOL.NMR V. 2 639 1992
REMARK 1 REFN ISSN 0925-2738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CRR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172489.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
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 : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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 21 THR A 2 158.45 62.18
REMARK 500 21 VAL A 7 93.64 -62.18
REMARK 500 21 ALA A 11 175.19 54.00
REMARK 500 21 ILE A 24 -84.60 -92.82
REMARK 500 21 ASN A 26 85.88 69.97
REMARK 500 21 HIS A 27 116.65 -179.26
REMARK 500 21 PHE A 28 103.72 -56.56
REMARK 500 21 GLU A 31 83.58 179.80
REMARK 500 21 ASP A 33 63.29 179.02
REMARK 500 21 THR A 35 23.95 -149.59
REMARK 500 21 ILE A 46 59.84 -90.29
REMARK 500 21 GLU A 49 50.21 -142.31
REMARK 500 21 ALA A 59 -73.26 -135.86
REMARK 500 21 GLU A 62 -171.58 60.14
REMARK 500 21 GLU A 63 54.24 -169.03
REMARK 500 21 SER A 65 142.08 64.31
REMARK 500 21 ALA A 66 -66.75 -179.34
REMARK 500 21 THR A 74 -65.77 -91.98
REMARK 500 21 GLU A 76 -37.43 -141.34
REMARK 500 21 PHE A 82 110.08 -165.92
REMARK 500 21 ILE A 84 38.47 -93.15
REMARK 500 21 THR A 87 -31.55 83.24
REMARK 500 21 ASP A 107 74.05 -112.56
REMARK 500 21 ASP A 108 59.68 -169.54
REMARK 500 21 LYS A 117 30.69 74.17
REMARK 500 21 LEU A 120 -176.48 179.54
REMARK 500 21 ALA A 121 95.71 57.04
REMARK 500 21 ALA A 122 131.92 -20.26
REMARK 500 21 ARG A 123 92.45 -53.82
REMARK 500 21 SER A 145 97.55 -166.32
REMARK 500 21 THR A 148 13.85 -144.14
REMARK 500 22 VAL A 7 99.56 -60.99
REMARK 500 22 ILE A 24 -83.60 -97.71
REMARK 500 22 ASN A 26 55.41 70.07
REMARK 500 22 GLU A 31 81.45 172.59
REMARK 500 22 TYR A 32 43.55 -95.28
REMARK 500 22 ASP A 33 85.57 62.78
REMARK 500 22 PRO A 34 82.98 -68.03
REMARK 500 22 THR A 35 36.42 -174.05
REMARK 500 22 CYS A 51 115.47 -162.10
REMARK 500 22 ASP A 54 79.72 -100.75
REMARK 500 22 THR A 58 -175.20 51.93
REMARK 500 22 GLU A 63 49.04 174.93
REMARK 500 22 TYR A 64 166.75 61.52
REMARK 500 22 SER A 65 48.78 -149.76
REMARK 500 22 THR A 74 -61.35 -90.41
REMARK 500 22 GLU A 76 -37.19 -144.52
REMARK 500 22 THR A 87 -44.94 84.33
REMARK 500 22 ASP A 107 74.65 -106.36
REMARK 500 22 ASP A 108 54.53 -168.40
REMARK 500
REMARK 500 THIS ENTRY HAS 509 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 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 GDP A 200 O2B 92.6
REMARK 620 3 GDP A 200 O1B 108.3 54.2
REMARK 620 4 HOH A 202 O 87.3 156.3 103.4
REMARK 620 5 HOH A 203 O 55.6 52.0 54.3 110.6
REMARK 620 6 HOH A 204 O 61.6 103.1 67.5 56.3 54.5
REMARK 620 7 HOH A 205 O 147.0 60.6 73.1 125.2 109.9 138.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CRP RELATED DB: PDB
REMARK 900 RELATED ID: 1CRQ RELATED DB: PDB
DBREF 1CRR A 1 166 UNP P01112 RASH_HUMAN 1 166
SEQRES 1 A 166 MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY GLY
SEQRES 2 A 166 VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN ASN
SEQRES 3 A 166 HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP SER
SEQRES 4 A 166 TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS LEU
SEQRES 5 A 166 LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR SER
SEQRES 6 A 166 ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY PHE
SEQRES 7 A 166 LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE GLU
SEQRES 8 A 166 ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL LYS
SEQRES 9 A 166 ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN LYS
SEQRES 10 A 166 CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN ALA
SEQRES 11 A 166 GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE GLU
SEQRES 12 A 166 THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA PHE
SEQRES 13 A 166 TYR THR LEU VAL ARG GLU ILE ARG GLN HIS
HET MG A 201 1
HET GDP A 200 40
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 GDP C10 H15 N5 O11 P2
FORMUL 4 HOH *4(H2 O)
HELIX 1 A1 GLY A 15 GLN A 25 1 11
HELIX 2 A2 ALA A 66 GLY A 75 1 10
HELIX 3 A3 THR A 87 LYS A 104 1 18
HELIX 4 A4 SER A 127 GLY A 138 1 12
HELIX 5 A5 VAL A 152 HIS A 166 1 15
SHEET 1 S1 5 ASP A 38 ILE A 46 0
SHEET 2 S1 5 GLU A 49 ASP A 57 -1 O LEU A 53 N LYS A 42
SHEET 3 S1 5 THR A 2 VAL A 9 1 O LEU A 6 N LEU A 56
SHEET 4 S1 5 GLY A 77 ILE A 84 1 O LEU A 79 N VAL A 9
SHEET 5 S1 5 PRO A 110 LYS A 117 1 O VAL A 112 N CYS A 80
LINK OG SER A 17 MG MG A 201 1555 1555 2.47
LINK O2B GDP A 200 MG MG A 201 1555 1555 2.93
LINK O1B GDP A 200 MG MG A 201 1555 1555 2.46
LINK MG MG A 201 O HOH A 202 1555 1555 2.60
LINK MG MG A 201 O HOH A 203 1555 1555 2.74
LINK MG MG A 201 O HOH A 204 1555 1555 2.68
LINK MG MG A 201 O HOH A 205 1555 1555 2.72
SITE 1 AC1 7 LYS A 16 SER A 17 GDP A 200 HOH A 202
SITE 2 AC1 7 HOH A 203 HOH A 204 HOH A 205
SITE 1 AC2 18 GLY A 13 VAL A 14 GLY A 15 LYS A 16
SITE 2 AC2 18 SER A 17 ALA A 18 PHE A 28 ASP A 30
SITE 3 AC2 18 LYS A 117 ASP A 119 LEU A 120 SER A 145
SITE 4 AC2 18 ALA A 146 LYS A 147 MG A 201 HOH A 203
SITE 5 AC2 18 HOH A 204 HOH A 205
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 21
Complete list - b 16 2 Bytes