Header list of 1cb3.pdb file
Complete list - 3 20 Bytes
HEADER MOLTEN GLOBULE STATE 26-FEB-99 1CB3 TITLE LOCAL INTERACTIONS DRIVE THE FORMATION OF NON-NATIVE STRUCTURE IN THE TITLE 2 DENATURED STATE OF HUMAN ALPHA-LACTALBUMIN: A HIGH RESOLUTION TITLE 3 STRUCTURAL CHARACTERIZATION OF A PEPTIDE MODEL IN AQUEOUS SOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: LCA; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 OTHER_DETAILS: ACETYLATED N-TERMINUS AMIDATED C-TERMINUS SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 4 ORGANISM_COMMON: HUMAN; SOURCE 5 ORGANISM_TAXID: 9606; SOURCE 6 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. KEYWDS MOLTEN GLOBULE STATE, PROTEIN FOLDING, NON-NATIVE INTERACTIONS, KEYWDS 2 ALPHA- LACTALBUMIN EXPDTA SOLUTION NMR NUMMDL 40 AUTHOR S.J.DEMAREST,Y.HUA,D.P.RALEIGH REVDAT 5 03-NOV-21 1CB3 1 COMPND SOURCE REMARK LINK REVDAT 4 24-FEB-09 1CB3 1 VERSN REVDAT 3 01-APR-03 1CB3 1 JRNL REVDAT 2 06-OCT-99 1CB3 1 REMARK REVDAT 1 08-JUN-99 1CB3 0 JRNL AUTH S.J.DEMAREST,Y.HUA,D.P.RALEIGH JRNL TITL LOCAL INTERACTIONS DRIVE THE FORMATION OF NONNATIVE JRNL TITL 2 STRUCTURE IN THE DENATURED STATE OF HUMAN ALPHA-LACTALBUMIN: JRNL TITL 3 A HIGH RESOLUTION STRUCTURAL CHARACTERIZATION OF A PEPTIDE JRNL TITL 4 MODEL IN AQUEOUS SOLUTION. JRNL REF BIOCHEMISTRY V. 38 7380 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10353850 JRNL DOI 10.1021/BI990320Z REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: BOND LENGTHS (A) : 0.0035; REMARK 3 BOND ANGLES (DEGREES) : 0.59; REMARK 3 IMPROPER ANGLES (DEGREES) : 0.35; REMARK 3 PARAMETER FILE 1 : PARALLHDG.PRO; REMARK 3 TOPOLOGY FILE 1 : TOPALLHDG.PRO REMARK 4 REMARK 4 1CB3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-99. REMARK 100 THE DEPOSITION ID IS D_1000000548. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 283 REMARK 210 PH : 2.8 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : ROESY; TOCSY; DQF-COSY; E.COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.851 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40 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: REMARK 210 THE STRUCTURE WAS DETERMINED USING 1H NMR SPECTROSCOPY ON A REMARK 210 CHEMICALLY REMARK 210 SYNTHESIZED PEPTIDE CORRESPONDING TO RESIDUES 120-130 OF HUMAN REMARK 210 ALPHA- REMARK 210 LACTALBUMIN 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: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O TRP A 4 H HIS A 7 1.55 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 1 ASP A 2 -70.10 61.05 REMARK 500 1 TRP A 4 -54.61 -16.87 REMARK 500 1 HIS A 7 -64.47 -122.91 REMARK 500 1 LYS A 8 148.41 58.98 REMARK 500 1 LEU A 10 -156.04 34.48 REMARK 500 2 ASP A 2 -69.12 62.20 REMARK 500 2 TRP A 4 -55.11 -16.69 REMARK 500 2 LYS A 8 -148.07 -111.57 REMARK 500 3 ASP A 2 -68.46 59.72 REMARK 500 3 TRP A 4 -50.38 -22.29 REMARK 500 3 LYS A 8 -141.89 43.03 REMARK 500 3 LEU A 10 112.09 56.25 REMARK 500 4 ASP A 2 -69.52 62.32 REMARK 500 4 TRP A 4 -56.52 -14.34 REMARK 500 4 HIS A 7 -137.94 -129.04 REMARK 500 4 LYS A 8 -143.64 67.37 REMARK 500 4 ALA A 9 -164.04 -55.33 REMARK 500 4 LEU A 10 102.76 54.95 REMARK 500 5 ASP A 2 -69.57 61.91 REMARK 500 5 TRP A 4 -55.35 -15.41 REMARK 500 5 HIS A 7 -68.84 -133.39 REMARK 500 5 LYS A 8 175.71 50.85 REMARK 500 6 ASP A 2 -68.85 62.07 REMARK 500 6 TRP A 4 -55.67 -16.49 REMARK 500 6 LYS A 8 -155.19 -104.45 REMARK 500 6 ALA A 9 94.17 -48.51 REMARK 500 6 LEU A 10 108.70 -167.79 REMARK 500 7 ASP A 2 -70.38 64.01 REMARK 500 7 TRP A 4 -54.46 -15.15 REMARK 500 7 HIS A 7 -137.87 -128.56 REMARK 500 7 LYS A 8 173.36 64.77 REMARK 500 8 ASP A 2 -70.36 61.42 REMARK 500 8 TRP A 4 -54.64 -15.65 REMARK 500 9 ASP A 2 -69.66 60.99 REMARK 500 9 TRP A 4 -57.86 -16.69 REMARK 500 9 HIS A 7 -70.67 -119.24 REMARK 500 9 LYS A 8 -142.71 43.59 REMARK 500 10 ASP A 2 -69.96 61.86 REMARK 500 10 TRP A 4 -55.55 -15.18 REMARK 500 10 HIS A 7 -142.79 -130.47 REMARK 500 10 LYS A 8 172.72 62.59 REMARK 500 10 LEU A 10 115.30 -177.63 REMARK 500 11 ASP A 2 -69.23 62.07 REMARK 500 11 TRP A 4 -55.22 -17.38 REMARK 500 11 LYS A 8 -163.89 -63.90 REMARK 500 12 ASP A 2 -67.25 62.30 REMARK 500 12 TRP A 4 -53.89 -19.48 REMARK 500 12 HIS A 7 -72.72 -117.94 REMARK 500 12 LYS A 8 -158.73 41.56 REMARK 500 12 LEU A 10 -88.43 55.75 REMARK 500 REMARK 500 THIS ENTRY HAS 168 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 12 DBREF 1CB3 A 1 11 UNP P00709 LALBA_HUMAN 120 130 SEQADV 1CB3 ALA A 11 UNP P00709 CYS 130 SEE REMARK 999 SEQRES 1 A 13 ACE ILE ASP TYR TRP LEU ALA HIS LYS ALA LEU ALA NH2 HET ACE A 0 6 HET NH2 A 12 3 HETNAM ACE ACETYL GROUP HETNAM NH2 AMINO GROUP FORMUL 1 ACE C2 H4 O FORMUL 1 NH2 H2 N HELIX 1 1 TRP A 4 HIS A 7 1 4 LINK C ACE A 0 N ILE A 1 1555 1555 1.31 LINK C ALA A 11 N NH2 A 12 1555 1555 1.31 SITE 1 AC2 2 LEU A 10 ALA A 11 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 - 3 20 Bytes