Header list of 1cb1.pdb file
Complete list - b 16 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 13-DEC-91 1CB1
TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF CA2+-LOADED PORCINE CALBINDIN
TITLE 2 D9K DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALBINDIN D9K;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823
KEYWDS CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 13
AUTHOR M.AKKE,T.DRAKENBERG,W.J.CHAZIN
REVDAT 4 16-FEB-22 1CB1 1 REMARK
REVDAT 3 24-FEB-09 1CB1 1 VERSN
REVDAT 2 01-APR-03 1CB1 1 JRNL
REVDAT 1 31-OCT-93 1CB1 0
JRNL AUTH M.AKKE,T.DRAKENBERG,W.J.CHAZIN
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF CA(2+)-LOADED
JRNL TITL 2 PORCINE CALBINDIN D9K DETERMINED BY NUCLEAR MAGNETIC
JRNL TITL 3 RESONANCE SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 31 1011 1992
JRNL REFN ISSN 0006-2960
JRNL PMID 1734952
JRNL DOI 10.1021/BI00119A009
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.DRAKENBERG,T.HOFMANN,W.J.CHAZIN
REMARK 1 TITL 1H NMR STUDIES OF PORCINE CALBINDIN D9K IN SOLUTION:
REMARK 1 TITL 2 SEQUENTIAL RESONANCE ASSIGNMENT, SECONDARY STRUCTURE, AND
REMARK 1 TITL 3 GLOBAL FOLD
REMARK 1 REF BIOCHEMISTRY V. 28 5946 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISGEO, AMBER RESTRAINED MOLECULAR DYNAMICS
REMARK 3 ANNEALING
REMARK 3 AUTHORS : HAVEL,WUTHRICH (DISGEO), GIPPERT,YIP,WRIGHT,CASE
REMARK 3 (AMBER RESTRAINED MOLECULAR DYNAMICS ANNEALING)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CB1 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_1000172203.
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 : 13
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 3 PRO A 37 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 10 PHE A 50 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 12 PHE A 50 CB - CG - CD2 ANGL. DEV. = -4.3 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 ASN A 21 -16.70 -143.07
REMARK 500 1 PHE A 36 95.81 -165.27
REMARK 500 1 PRO A 37 72.08 -67.81
REMARK 500 1 LEU A 39 35.34 -80.40
REMARK 500 1 THR A 45 107.75 -50.67
REMARK 500 1 ASN A 56 80.09 -159.33
REMARK 500 1 ASP A 58 -52.73 -120.59
REMARK 500 1 GLU A 60 -94.00 -132.07
REMARK 500 2 LYS A 1 124.80 60.69
REMARK 500 2 PHE A 36 63.90 -152.05
REMARK 500 2 PRO A 37 109.12 -53.26
REMARK 500 2 SER A 38 16.72 59.85
REMARK 500 2 LEU A 39 48.49 -84.39
REMARK 500 2 ARG A 44 -94.34 -128.07
REMARK 500 2 ASP A 47 100.06 -163.41
REMARK 500 2 ASP A 48 -57.83 -160.55
REMARK 500 2 ASP A 54 70.43 -69.34
REMARK 500 2 ASP A 58 -73.09 -157.15
REMARK 500 2 ILE A 73 99.58 -51.38
REMARK 500 3 ALA A -1 -135.72 -91.50
REMARK 500 3 ASN A 21 0.49 -151.57
REMARK 500 3 GLU A 35 -147.95 -83.19
REMARK 500 3 PRO A 37 -4.16 -48.81
REMARK 500 3 LEU A 40 -50.02 66.16
REMARK 500 3 LYS A 71 91.20 -63.23
REMARK 500 4 ASP A 19 150.77 109.93
REMARK 500 4 PHE A 36 72.41 -162.12
REMARK 500 4 PRO A 43 107.88 -55.82
REMARK 500 4 ASP A 47 -14.31 -143.64
REMARK 500 4 ASN A 56 -47.89 -165.06
REMARK 500 4 ASP A 58 -54.01 -165.30
REMARK 500 5 ASP A 19 106.65 178.23
REMARK 500 5 PRO A 20 48.62 -75.40
REMARK 500 5 PHE A 36 87.36 -164.91
REMARK 500 5 SER A 38 -14.37 -44.67
REMARK 500 5 LEU A 39 49.43 -80.03
REMARK 500 5 ARG A 44 -61.49 -156.82
REMARK 500 5 THR A 45 -84.26 58.14
REMARK 500 5 LEU A 46 -59.76 50.40
REMARK 500 5 ASP A 48 -62.94 -140.86
REMARK 500 5 ASP A 54 66.94 -65.78
REMARK 500 5 GLU A 60 -130.75 -142.34
REMARK 500 5 SER A 74 64.85 -69.98
REMARK 500 6 LYS A 16 -71.87 -79.30
REMARK 500 6 ASP A 19 148.93 166.80
REMARK 500 6 PHE A 36 68.16 -160.16
REMARK 500 6 SER A 38 38.90 33.60
REMARK 500 6 LEU A 40 70.74 -69.00
REMARK 500 6 ARG A 44 67.48 -59.71
REMARK 500 6 ASP A 47 -24.41 -163.85
REMARK 500
REMARK 500 THIS ENTRY HAS 118 RAMACHANDRAN OUTLIERS.
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 2 TYR A 13 0.09 SIDE CHAIN
REMARK 500 2 PHE A 63 0.08 SIDE CHAIN
REMARK 500 3 PHE A 36 0.10 SIDE CHAIN
REMARK 500 5 PHE A 63 0.08 SIDE CHAIN
REMARK 500 6 PHE A 63 0.09 SIDE CHAIN
REMARK 500 7 TYR A 13 0.08 SIDE CHAIN
REMARK 500 7 PHE A 50 0.19 SIDE CHAIN
REMARK 500 8 PHE A 50 0.19 SIDE CHAIN
REMARK 500 10 TYR A 13 0.11 SIDE CHAIN
REMARK 500 10 PHE A 50 0.19 SIDE CHAIN
REMARK 500 12 TYR A 13 0.08 SIDE CHAIN
REMARK 500 12 PHE A 50 0.14 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CB1 A -2 75 UNP P02632 S100G_PIG 1 78
SEQRES 1 A 78 SER ALA GLN LYS SER PRO ALA GLU LEU LYS SER ILE PHE
SEQRES 2 A 78 GLU LYS TYR ALA ALA LYS GLU GLY ASP PRO ASN GLN LEU
SEQRES 3 A 78 SER LYS GLU GLU LEU LYS GLN LEU ILE GLN ALA GLU PHE
SEQRES 4 A 78 PRO SER LEU LEU LYS GLY PRO ARG THR LEU ASP ASP LEU
SEQRES 5 A 78 PHE GLN GLU LEU ASP LYS ASN GLY ASP GLY GLU VAL SER
SEQRES 6 A 78 PHE GLU GLU PHE GLN VAL LEU VAL LYS LYS ILE SER GLN
HELIX 1 1 SER A 2 ALA A 15 1 14
HELIX 2 2 SER A 24 PHE A 36 1 13
HELIX 3 3 ASP A 47 LEU A 53 1 7
HELIX 4 4 PHE A 63 SER A 74 1 12
SHEET 1 A 2 GLN A 22 LEU A 23 0
SHEET 2 A 2 VAL A 61 SER A 62 -1 O VAL A 61 N LEU A 23
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