Header list of 1bct.pdb file
Complete list - b 16 2 Bytes
HEADER PHOTORECEPTOR 07-JUL-93 1BCT
TITLE THREE-DIMENSIONAL STRUCTURE OF PROTEOLYTIC FRAGMENT 163-231 OF
TITLE 2 BACTERIOOPSIN DETERMINED FROM NUCLEAR MAGNETIC RESONANCE DATA IN
TITLE 3 SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACTERIORHODOPSIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOBACTERIUM SALINARUM;
SOURCE 3 ORGANISM_TAXID: 2242
KEYWDS PHOTORECEPTOR
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR D.E.NOLDE,I.L.BARSUKOV,A.L.LOMIZE,A.S.ARSENIEV
REVDAT 4 16-FEB-22 1BCT 1 REMARK
REVDAT 3 24-FEB-09 1BCT 1 VERSN
REVDAT 2 15-OCT-94 1BCT 1 SOURCE JRNL
REVDAT 1 30-APR-94 1BCT 0
JRNL AUTH I.L.BARSUKOV,D.E.NOLDE,A.L.LOMIZE,A.S.ARSENIEV
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF PROTEOLYTIC FRAGMENT 163-231
JRNL TITL 2 OF BACTERIOOPSIN DETERMINED FROM NUCLEAR MAGNETIC RESONANCE
JRNL TITL 3 DATA IN SOLUTION.
JRNL REF EUR.J.BIOCHEM. V. 206 665 1992
JRNL REFN ISSN 0014-2956
JRNL PMID 1606953
JRNL DOI 10.1111/J.1432-1033.1992.TB16972.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.L.BARSUKOV,G.V.ABDULAEVA,A.S.ARSENIEV,V.F.BYSTROV
REMARK 1 TITL SEQUENCE-SPECIFIC 1H (SLASH)NMR ASSIGNMENT AND CONFORMATION
REMARK 1 TITL 2 OF PROTEOLYTIC FRAGMENT 163-231 OF BACTERIOOPSIN
REMARK 1 REF EUR.J.BIOCHEM. V. 192 321 1990
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BCT 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_1000171600.
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 : 14
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 2 ARG A 164 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 2 ARG A 227 NE - CZ - NH2 ANGL. DEV. = -3.2 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 1 SER A 193 40.14 -163.09
REMARK 500 2 ARG A 164 86.32 -163.19
REMARK 500 2 SER A 193 69.72 -174.47
REMARK 500 3 GLU A 166 -174.66 -69.87
REMARK 500 3 SER A 193 76.72 -174.10
REMARK 500 3 GLU A 194 -71.04 -64.94
REMARK 500 3 ARG A 227 100.11 -55.22
REMARK 500 3 ILE A 229 -19.77 -145.98
REMARK 500 4 GLU A 166 -26.32 -144.92
REMARK 500 4 SER A 193 -57.48 -162.07
REMARK 500 4 GLU A 194 46.01 -150.43
REMARK 500 4 ARG A 225 -57.51 -158.60
REMARK 500 4 SER A 226 53.30 -157.83
REMARK 500 4 ARG A 227 -57.93 -154.40
REMARK 500 5 ARG A 164 -64.45 -163.20
REMARK 500 5 GLU A 166 -75.49 -81.45
REMARK 500 5 SER A 193 -49.64 -172.23
REMARK 500 5 GLU A 194 -45.48 -132.73
REMARK 500 5 ALA A 196 -7.29 -153.56
REMARK 500 5 ARG A 225 -66.66 -168.64
REMARK 500 5 ALA A 228 -64.36 -159.38
REMARK 500 6 ARG A 164 -58.54 -174.64
REMARK 500 6 PRO A 165 -81.52 -67.40
REMARK 500 6 GLU A 166 44.30 -78.27
REMARK 500 6 SER A 193 -55.49 -153.57
REMARK 500 6 GLU A 194 -66.98 -150.33
REMARK 500 6 ARG A 227 -57.80 -150.34
REMARK 500 7 GLU A 166 -166.39 62.83
REMARK 500 7 VAL A 167 -76.13 69.95
REMARK 500 7 SER A 193 -34.05 -155.74
REMARK 500 7 ARG A 225 -60.70 -161.14
REMARK 500 8 GLU A 166 -45.07 78.22
REMARK 500 8 VAL A 167 -172.40 55.65
REMARK 500 8 SER A 193 -40.81 -159.25
REMARK 500 8 GLU A 194 77.91 64.50
REMARK 500 8 ARG A 225 -56.53 -158.02
REMARK 500 8 SER A 226 43.80 -148.23
REMARK 500 8 ARG A 227 -47.22 -137.20
REMARK 500 8 ILE A 229 -78.63 -77.11
REMARK 500 9 ARG A 164 161.04 64.08
REMARK 500 9 PRO A 165 -164.02 -73.25
REMARK 500 9 SER A 193 24.97 -167.84
REMARK 500 9 GLU A 194 55.37 36.19
REMARK 500 9 ARG A 227 104.71 -58.04
REMARK 500 9 ILE A 229 -40.77 -140.61
REMARK 500 10 SER A 193 -42.34 -164.16
REMARK 500 11 ARG A 164 69.42 61.84
REMARK 500 11 VAL A 167 -170.74 52.16
REMARK 500 11 SER A 193 -10.68 -151.07
REMARK 500 11 GLU A 194 55.69 -158.48
REMARK 500
REMARK 500 THIS ENTRY HAS 81 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET A 163 ARG A 164 14 -149.59
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BCT A 163 231 UNP P02945 BACR_HALN1 176 244
SEQRES 1 A 69 MET ARG PRO GLU VAL ALA SER THR PHE LYS VAL LEU ARG
SEQRES 2 A 69 ASN VAL THR VAL VAL LEU TRP SER ALA TYR PRO VAL VAL
SEQRES 3 A 69 TRP LEU ILE GLY SER GLU GLY ALA GLY ILE VAL PRO LEU
SEQRES 4 A 69 ASN ILE GLU THR LEU LEU PHE MET VAL LEU ASP VAL SER
SEQRES 5 A 69 ALA LYS VAL GLY PHE GLY LEU ILE LEU LEU ARG SER ARG
SEQRES 6 A 69 ALA ILE PHE GLY
HELIX 1 H1 ALA A 168 ILE A 191 1KINK AT PRO 186 24
HELIX 2 H2 ILE A 198 ARG A 225 1UNSTABLE ON ILE 198 - PRO 200 28
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 - b 16 2 Bytes