Header list of 1bj8.pdb file
Complete list - 16 202 Bytes
HEADER RECEPTOR 02-JUL-98 1BJ8
TITLE THIRD N-TERMINAL DOMAIN OF GP130, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GP130;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIRD N-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS RECEPTOR, SIGNAL TRANSDUCER OF IL-6 TYPE CYTOKINES, THIRD N-TERMINAL
KEYWDS 2 DOMAIN, TRANSMEMBRANE, GLYCOPROTEIN
EXPDTA SOLUTION NMR
AUTHOR T.KERNEBECK,S.PFLANZ,G.MULLER-NEWEN,G.KURAPKAT,R.M.SCHEEK,K.DIJKSTRA,
AUTHOR 2 P.C.HEINRICH,A.WOLLMER,S.GRZESIEK,J.GROTZINGER
REVDAT 3 16-FEB-22 1BJ8 1 REMARK
REVDAT 2 24-FEB-09 1BJ8 1 VERSN
REVDAT 1 13-JAN-99 1BJ8 0
JRNL AUTH T.KERNEBECK,S.PFLANZ,G.MULLER-NEWEN,G.KURAPKAT,R.M.SCHEEK,
JRNL AUTH 2 K.DIJKSTRA,P.C.HEINRICH,A.WOLLMER,S.GRZESIEK,J.GROTZINGER
JRNL TITL THE SIGNAL TRANSDUCER GP130: SOLUTION STRUCTURE OF THE
JRNL TITL 2 CARBOXY-TERMINAL DOMAIN OF THE CYTOKINE RECEPTOR HOMOLOGY
JRNL TITL 3 REGION.
JRNL REF PROTEIN SCI. V. 8 5 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10210178
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.MULLER-NEWEN,S.PFLANZ,U.HASSIEPEN,J.STAHL,A.WOLLMER,
REMARK 1 AUTH 2 P.C.HEINRICH,J.GROTZINGER
REMARK 1 TITL THE SIGNAL TRANSDUCER GP130--BACTERIAL EXPRESSION, REFOLDING
REMARK 1 TITL 2 AND PROPERTIES OF THE CARBOXY-TERMINAL DOMAIN OF THE
REMARK 1 TITL 3 CYTOKINE-BINDING MODULE
REMARK 1 REF EUR.J.BIOCHEM. V. 247 425 1997
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DDD
REMARK 3 AUTHORS : SCHEEK
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FINAL 22 STRUCTURES WERE CALCULATED
REMARK 3 USING A TOTAL OF 1575 RESTRAINTS. DISTANCE BOUND DRIVEN DYNAMICS
REMARK 3 WAS DONE FOR 1000 STEPS AT 1000 KELVIN, FOLLOWED BY 1000 STEPS
REMARK 3 OF SIMULATED ANNEALING TO 10 KELVIN. THE MEAN STRUCTURE WAS
REMARK 3 ENERGY MINIMIZED USING THE GROMOS PROGRAMM PACKAGE.
REMARK 4
REMARK 4 1BJ8 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_1000171820.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 200 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CBCA(CO)NH; CBCANH; C(CO)NH;
REMARK 210 HNCA; HBHA(CO)NH; 15N-EDITED
REMARK 210 HOHAHA; 13C-EDITED TOCSY; 15N-
REMARK 210 EDITED NOESY; 13C-EDITED NOESY;
REMARK 210 HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY500; INOVA600; DMX600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DDD
REMARK 210 METHOD USED : DISTANCE GEOMETRY, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 22
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN
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 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.9 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 ASP A 2 -103.41 -125.41
REMARK 500 LYS A 3 -169.79 -129.49
REMARK 500 ASN A 7 138.21 3.95
REMARK 500 HIS A 10 -174.33 -68.42
REMARK 500 GLU A 18 -79.17 31.31
REMARK 500 ASN A 30 150.66 -49.08
REMARK 500 SER A 32 -35.57 175.81
REMARK 500 ILE A 33 137.23 -37.20
REMARK 500 LYS A 34 -144.26 -98.31
REMARK 500 SER A 35 38.97 -75.50
REMARK 500 ILE A 37 103.69 49.06
REMARK 500 SER A 54 -152.51 -96.90
REMARK 500 PRO A 58 77.21 -67.81
REMARK 500 GLU A 59 -63.51 -120.28
REMARK 500 THR A 61 43.13 -88.18
REMARK 500 SER A 63 81.72 -164.61
REMARK 500 THR A 64 97.88 36.63
REMARK 500 SER A 66 -14.21 61.12
REMARK 500 ASP A 72 50.03 71.85
REMARK 500 PHE A 76 -11.00 62.31
REMARK 500 GLU A 88 129.67 -28.24
REMARK 500 ASP A 89 -157.07 119.76
REMARK 500 TRP A 94 135.44 -39.78
REMARK 500 TRP A 97 128.23 -5.39
REMARK 500 GLU A 99 177.44 170.19
REMARK 500 TYR A 106 -124.53 33.49
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 TYR A 41 0.11 SIDE CHAIN
REMARK 500 TYR A 79 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BJ8 A 3 109 UNP P40189 IL6RB_HUMAN 219 325
SEQRES 1 A 109 MET ASP LYS VAL LYS PRO ASN PRO PRO HIS ASN LEU SER
SEQRES 2 A 109 VAL ILE ASN SER GLU GLU LEU SER SER ILE LEU LYS LEU
SEQRES 3 A 109 THR TRP THR ASN PRO SER ILE LYS SER VAL ILE ILE LEU
SEQRES 4 A 109 LYS TYR ASN ILE GLN TYR ARG THR LYS ASP ALA SER THR
SEQRES 5 A 109 TRP SER GLN ILE PRO PRO GLU ASP THR ALA SER THR ARG
SEQRES 6 A 109 SER SER PHE THR VAL GLN ASP LEU LYS PRO PHE THR GLU
SEQRES 7 A 109 TYR VAL PHE ARG ILE ARG CYS MET LYS GLU ASP GLY LYS
SEQRES 8 A 109 GLY TYR TRP SER ASP TRP SER GLU GLU ALA SER GLY ILE
SEQRES 9 A 109 THR TYR GLU ASP ARG
HELIX 1 1 ASP A 60 ALA A 62 5 3
SHEET 1 A 2 LEU A 24 THR A 27 0
SHEET 2 A 2 SER A 67 VAL A 70 -1 N VAL A 70 O LEU A 24
SHEET 1 B 3 LEU A 39 THR A 47 0
SHEET 2 B 3 GLU A 78 LYS A 87 -1 N MET A 86 O LYS A 40
SHEET 3 B 3 GLU A 99 ILE A 104 -1 N GLY A 103 O TYR A 79
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 - 16 202 Bytes