Header list of 1b0q.pdb file
Complete list - 16 202 Bytes
HEADER HORMONE/GROWTH FACTOR 12-NOV-98 1B0Q
TITLE DITHIOL ALPHA MELANOTROPIN PEPTIDE CYCLIZED VIA RHENIUM METAL
TITLE 2 COORDINATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (CYCLIC ALPHA MELANOCYTE STIMULATING HORMONE);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MSH;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: COMPOUND CYCLIZED THROUGH RHENIUM METAL COODINATION
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES
KEYWDS ALPHA MELANOCYTE STIMULATING HORMONE, RHENIUM TECHNETIUM, HORMONE-
KEYWDS 2 GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
AUTHOR M.F.GIBLIN,N.WANG,T.J.HOFFMAN,S.S.JURISSON,T.P.QUINN
REVDAT 5 16-FEB-22 1B0Q 1 REMARK LINK
REVDAT 4 24-FEB-09 1B0Q 1 VERSN
REVDAT 3 26-SEP-01 1B0Q 3 ATOM
REVDAT 2 29-DEC-99 1B0Q 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 18-NOV-98 1B0Q 0
JRNL AUTH M.F.GIBLIN,N.WANG,T.J.HOFFMAN,S.S.JURISSON,T.P.QUINN
JRNL TITL DESIGN AND CHARACTERIZATION OF ALPHA-MELANOTROPIN PEPTIDE
JRNL TITL 2 ANALOGS CYCLIZED THROUGH RHENIUM AND TECHNETIUM METAL
JRNL TITL 3 COORDINATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 95 12814 1998
JRNL REFN ISSN 0027-8424
JRNL PMID 9788997
JRNL DOI 10.1073/PNAS.95.22.12814
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SYBYL
REMARK 3 AUTHORS : TRIPOS, INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MODELING DETAILS CAN BE FOUND IN THE
REMARK 3 JNRL CITATION ABOVE
REMARK 4
REMARK 4 1B0Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008004.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BRUKER UXNMR UXNMR, SYBYL
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: MINIMIZED AVERAGE STRUCTURE
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 GLU A 2 90.75 -172.60
REMARK 500 ARG A 5 142.82 170.94
REMARK 500 TRP A 6 -34.02 -140.43
REMARK 500 LYS A 8 139.06 -170.41
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 RE A 182 RE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP A 6 N
REMARK 620 2 CYS A 7 N 87.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RE A 182
DBREF 1B0Q A 1A 11 PDB 1B0Q 1B0Q 1 11
SEQRES 1 A 12 ACE CYS GLU HIS DPN ARG TRP CYS LYS PRO VAL NH2
HET ACE A 1A 6
HET DPN A 4 20
HET NH2 A 11 3
HET RE A 182 1
HETNAM ACE ACETYL GROUP
HETNAM DPN D-PHENYLALANINE
HETNAM NH2 AMINO GROUP
HETNAM RE RHENIUM
FORMUL 1 ACE C2 H4 O
FORMUL 1 DPN C9 H11 N O2
FORMUL 1 NH2 H2 N
FORMUL 2 RE RE
LINK C ACE A 1A N CYS A 1 1555 1555 1.34
LINK C HIS A 3 N DPN A 4 1555 1555 1.34
LINK C DPN A 4 N ARG A 5 1555 1555 1.34
LINK C VAL A 10 N NH2 A 11 1555 1555 1.34
LINK N TRP A 6 RE RE A 182 1555 1555 2.05
LINK N CYS A 7 RE RE A 182 1555 1555 1.99
SITE 1 AC1 4 CYS A 1 ARG A 5 TRP A 6 CYS A 7
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