Header list of 1far.pdb file
Complete list - 23 202 Bytes
HEADER SERINE/THREONINE PROTEIN KINASE 05-SEP-96 1FAR
TITLE RAF-1 CYSTEINE RICH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAF-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CYSTEINE-RICH DOMAIN;
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, PROTO-ONCOGENE, ZINC,
KEYWDS 2 ATP-BINDING, PHORBOL-ESTER BINDING, SERINE-THREONINE PROTEIN KINASE
KEYWDS 3 COMPLEX
EXPDTA SOLUTION NMR
AUTHOR H.R.MOTT,S.L.CAMPBELL
REVDAT 3 23-FEB-22 1FAR 1 REMARK LINK
REVDAT 2 24-FEB-09 1FAR 1 VERSN
REVDAT 1 27-JAN-97 1FAR 0
JRNL AUTH H.R.MOTT,J.W.CARPENTER,S.ZHONG,S.GHOSH,R.M.BELL,S.L.CAMPBELL
JRNL TITL THE SOLUTION STRUCTURE OF THE RAF-1 CYSTEINE-RICH DOMAIN: A
JRNL TITL 2 NOVEL RAS AND PHOSPHOLIPID BINDING SITE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 93 8312 1996
JRNL REFN ISSN 0027-8424
JRNL PMID 8710867
JRNL DOI 10.1073/PNAS.93.16.8312
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 1FAR 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_1000173210.
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 : 1
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: 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 TYR A 170 CB - CG - CD2 ANGL. DEV. = 16.2 DEGREES
REMARK 500 TYR A 170 CD1 - CG - CD2 ANGL. DEV. = -65.6 DEGREES
REMARK 500 TYR A 170 CB - CG - CD1 ANGL. DEV. = -10.1 DEGREES
REMARK 500 TYR A 170 CG - CD1 - CE1 ANGL. DEV. = -48.1 DEGREES
REMARK 500 TYR A 170 CG - CD2 - CE2 ANGL. DEV. = -46.2 DEGREES
REMARK 500 TYR A 170 CD1 - CE1 - CZ ANGL. DEV. = -44.5 DEGREES
REMARK 500 TYR A 170 CE1 - CZ - OH ANGL. DEV. = 16.9 DEGREES
REMARK 500 TYR A 170 CE1 - CZ - CE2 ANGL. DEV. = -68.5 DEGREES
REMARK 500 TYR A 170 CZ - CE2 - CD2 ANGL. DEV. = -46.9 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 THR A 138 -161.83 -70.05
REMARK 500 ARG A 143 109.76 -56.39
REMARK 500 LYS A 148 -81.62 -117.25
REMARK 500 CYS A 155 -84.51 -88.61
REMARK 500 GLN A 156 -17.27 166.01
REMARK 500 PHE A 158 172.21 -42.68
REMARK 500 LEU A 160 -169.33 -118.92
REMARK 500 ASN A 161 99.25 -54.88
REMARK 500 HIS A 173 -158.20 -94.18
REMARK 500 PRO A 181 -87.65 -74.76
REMARK 500 MET A 183 175.50 -58.83
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 ARG A 143 0.23 SIDE CHAIN
REMARK 500 ARG A 164 0.31 SIDE CHAIN
REMARK 500 TYR A 170 0.45 SIDE CHAIN
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 ZN A 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 152 SG
REMARK 620 2 CYS A 155 SG 102.4
REMARK 620 3 HIS A 173 ND1 93.9 83.5
REMARK 620 4 CYS A 176 SG 97.5 122.3 148.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 139 ND1
REMARK 620 2 CYS A 165 SG 99.9
REMARK 620 3 CYS A 168 SG 170.4 87.5
REMARK 620 4 CYS A 184 SG 88.3 156.8 87.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZINC-COORDINATION RESIDUES.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZINC-COORDINATION RESIDUES.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FAQ RELATED DB: PDB
DBREF 1FAR A 136 187 UNP P04049 RAF1_HUMAN 136 187
SEQRES 1 A 52 LEU THR THR HIS ASN PHE ALA ARG LYS THR PHE LEU LYS
SEQRES 2 A 52 LEU ALA PHE CYS ASP ILE CYS GLN LYS PHE LEU LEU ASN
SEQRES 3 A 52 GLY PHE ARG CYS GLN THR CYS GLY TYR LYS PHE HIS GLU
SEQRES 4 A 52 HIS CYS SER THR LYS VAL PRO THR MET CYS VAL ASP TRP
HET ZN A 1 1
HET ZN A 2 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLU A 174 CYS A 176 5 3
SHEET 1 A 3 ALA A 142 LYS A 144 0
SHEET 2 A 3 GLY A 162 CYS A 165 -1 N ARG A 164 O ALA A 142
SHEET 3 A 3 TYR A 170 PHE A 172 -1 N PHE A 172 O PHE A 163
LINK ZN ZN A 1 SG CYS A 152 1555 1555 2.36
LINK ZN ZN A 1 SG CYS A 155 1555 1555 2.39
LINK ZN ZN A 1 ND1 HIS A 173 1555 1555 2.14
LINK ZN ZN A 1 SG CYS A 176 1555 1555 2.48
LINK ZN ZN A 2 ND1 HIS A 139 1555 1555 2.17
LINK ZN ZN A 2 SG CYS A 165 1555 1555 2.38
LINK ZN ZN A 2 SG CYS A 168 1555 1555 2.46
LINK ZN ZN A 2 SG CYS A 184 1555 1555 2.36
SITE 1 ZN1 4 CYS A 152 CYS A 155 HIS A 173 CYS A 176
SITE 1 ZN2 4 HIS A 139 CYS A 165 CYS A 168 CYS A 184
SITE 1 AC1 4 CYS A 152 CYS A 155 HIS A 173 CYS A 176
SITE 1 AC2 5 HIS A 139 CYS A 165 CYS A 168 TYR A 170
SITE 2 AC2 5 CYS A 184
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
Complete list - 23 202 Bytes