Header list of 1jbi.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 05-JUN-01 1JBI
TITLE NMR STRUCTURE OF THE LCCL DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COCHLIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LCCL MODULE;
COMPND 5 SYNONYM: COCH-5B2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: M13MP18;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM 109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMED23
KEYWDS ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.LIEPINSH,M.TREXLER,A.KAIKKONEN,J.WEIGELT,L.BANYAI,L.PATTHY,G.OTTING
REVDAT 3 23-FEB-22 1JBI 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1JBI 1 VERSN
REVDAT 1 17-OCT-01 1JBI 0
JRNL AUTH E.LIEPINSH,M.TREXLER,A.KAIKKONEN,J.WEIGELT,L.BANYAI,
JRNL AUTH 2 L.PATTHY,G.OTTING
JRNL TITL NMR STRUCTURE OF THE LCCL DOMAIN AND IMPLICATIONS FOR DFNA9
JRNL TITL 2 DEAFNESS DISORDER.
JRNL REF EMBO J. V. 20 5347 2001
JRNL REFN ISSN 0261-4189
JRNL PMID 11574466
JRNL DOI 10.1093/EMBOJ/20.19.5347
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, OPAL 2.2
REMARK 3 AUTHORS : BRUKER (XWINNMR), LUGINBUHL (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2532 RESTRAINTS, 1193 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 270 DIHEDRAL ANGLE RESTRAINTS AND 69
REMARK 3 RESIDUAL DIPOLAR COUPLING RESTRAINTS
REMARK 4
REMARK 4 1JBI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013587.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301; 301
REMARK 210 PH : 4.9; 4.9
REMARK 210 IONIC STRENGTH : 0.1; 0.1
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM LCCL; 90% H2O, 10% D2O;
REMARK 210 3MG/ML LCCL U-15N; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY,2D ROESY, 2D DQF
REMARK 210 -COSY,2D TOCSY; 3D-15N-SEPARATED-NOESY,3D-15N-SEPARATED-TOCSY,
REMARK 210 1H-15N-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PROSA 3.4, XEASY 2.6, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY,TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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 1 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 5 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 8 ARG A 54 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 9 ARG A 72 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 14 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 19 TYR A 67 CB - CG - CD1 ANGL. DEV. = -4.0 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 CYS A 8 13.37 54.33
REMARK 500 1 CYS A 28 75.51 41.15
REMARK 500 1 LEU A 30 63.95 -69.52
REMARK 500 1 ILE A 39 -67.02 63.36
REMARK 500 1 SER A 60 -13.00 -145.86
REMARK 500 1 ARG A 90 62.08 61.28
REMARK 500 1 SER A 92 35.50 -78.82
REMARK 500 2 CYS A 8 13.70 51.24
REMARK 500 2 CYS A 28 70.33 41.05
REMARK 500 2 ILE A 39 -64.12 62.03
REMARK 500 2 SER A 60 -14.32 -146.84
REMARK 500 2 ARG A 90 62.28 65.07
REMARK 500 2 SER A 92 33.96 -78.78
REMARK 500 2 ALA A 93 115.35 -165.91
REMARK 500 3 ALA A 2 98.89 -179.99
REMARK 500 3 THR A 7 46.27 -102.21
REMARK 500 3 CYS A 8 13.00 51.21
REMARK 500 3 CYS A 28 70.49 32.35
REMARK 500 3 ILE A 39 -60.84 63.64
REMARK 500 3 SER A 60 -13.46 -147.09
REMARK 500 3 ARG A 90 61.86 60.09
REMARK 500 3 SER A 92 33.79 -78.91
REMARK 500 3 ALA A 93 112.50 -161.92
REMARK 500 4 CYS A 8 13.45 56.51
REMARK 500 4 ALA A 20 147.39 -175.86
REMARK 500 4 CYS A 28 70.76 28.19
REMARK 500 4 ILE A 39 -65.59 61.39
REMARK 500 4 SER A 60 -66.07 -146.86
REMARK 500 4 PRO A 70 -179.35 -68.18
REMARK 500 4 SER A 92 33.81 -80.50
REMARK 500 5 CYS A 8 13.23 51.82
REMARK 500 5 CYS A 28 71.89 40.79
REMARK 500 5 ILE A 39 -66.97 62.44
REMARK 500 5 ASN A 59 73.47 -65.90
REMARK 500 5 SER A 60 -13.80 -147.20
REMARK 500 5 PRO A 70 171.11 -59.70
REMARK 500 5 SER A 89 79.32 -100.47
REMARK 500 5 SER A 92 33.79 -78.91
REMARK 500 5 ALA A 93 108.68 -161.96
REMARK 500 6 CYS A 8 13.68 49.82
REMARK 500 6 ARG A 16 64.42 -119.89
REMARK 500 6 CYS A 28 76.63 42.08
REMARK 500 6 ILE A 39 -61.29 63.90
REMARK 500 6 ASN A 59 74.35 -64.03
REMARK 500 6 SER A 60 -21.27 -146.72
REMARK 500 6 SER A 92 33.39 -78.73
REMARK 500 6 ALA A 93 95.44 -160.27
REMARK 500 7 PRO A 3 -179.79 -64.99
REMARK 500 7 CYS A 8 13.32 57.85
REMARK 500 7 CYS A 28 76.09 40.87
REMARK 500
REMARK 500 THIS ENTRY HAS 158 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 THR A 1 ALA A 2 4 -65.98
REMARK 500 THR A 1 ALA A 2 19 -139.20
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 1 TYR A 41 0.07 SIDE CHAIN
REMARK 500 1 ARG A 65 0.13 SIDE CHAIN
REMARK 500 1 TYR A 67 0.08 SIDE CHAIN
REMARK 500 2 ARG A 72 0.10 SIDE CHAIN
REMARK 500 3 TYR A 36 0.08 SIDE CHAIN
REMARK 500 3 ARG A 72 0.12 SIDE CHAIN
REMARK 500 5 ARG A 72 0.09 SIDE CHAIN
REMARK 500 6 TYR A 41 0.08 SIDE CHAIN
REMARK 500 6 TYR A 67 0.07 SIDE CHAIN
REMARK 500 6 ARG A 90 0.09 SIDE CHAIN
REMARK 500 8 ARG A 54 0.09 SIDE CHAIN
REMARK 500 9 ARG A 16 0.09 SIDE CHAIN
REMARK 500 9 TYR A 41 0.07 SIDE CHAIN
REMARK 500 10 TYR A 41 0.08 SIDE CHAIN
REMARK 500 10 TYR A 67 0.07 SIDE CHAIN
REMARK 500 11 ARG A 16 0.10 SIDE CHAIN
REMARK 500 11 TYR A 41 0.07 SIDE CHAIN
REMARK 500 12 TYR A 75 0.08 SIDE CHAIN
REMARK 500 12 ARG A 90 0.08 SIDE CHAIN
REMARK 500 13 ARG A 90 0.15 SIDE CHAIN
REMARK 500 14 ARG A 54 0.15 SIDE CHAIN
REMARK 500 14 ARG A 72 0.08 SIDE CHAIN
REMARK 500 15 ARG A 16 0.12 SIDE CHAIN
REMARK 500 15 ARG A 72 0.11 SIDE CHAIN
REMARK 500 16 ARG A 16 0.08 SIDE CHAIN
REMARK 500 16 TYR A 41 0.10 SIDE CHAIN
REMARK 500 18 ARG A 72 0.10 SIDE CHAIN
REMARK 500 19 TYR A 36 0.07 SIDE CHAIN
REMARK 500 20 TYR A 41 0.11 SIDE CHAIN
REMARK 500 20 ARG A 90 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JBI A 1 100 UNP O43405 COCH_HUMAN 27 126
SEQADV 1JBI THR A 1 UNP O43405 ALA 27 CONFLICT
SEQADV 1JBI LEU A 99 UNP O43405 LYS 125 CONFLICT
SEQADV 1JBI GLU A 100 UNP O43405 GLY 126 CONFLICT
SEQRES 1 A 100 THR ALA PRO ILE ALA ILE THR CYS PHE THR ARG GLY LEU
SEQRES 2 A 100 ASP ILE ARG LYS GLU LYS ALA ASP VAL LEU CYS PRO GLY
SEQRES 3 A 100 GLY CYS PRO LEU GLU GLU PHE SER VAL TYR GLY ASN ILE
SEQRES 4 A 100 VAL TYR ALA SER VAL SER SER ILE CYS GLY ALA ALA VAL
SEQRES 5 A 100 HIS ARG GLY VAL ILE SER ASN SER GLY GLY PRO VAL ARG
SEQRES 6 A 100 VAL TYR SER LEU PRO GLY ARG GLU ASN TYR SER SER VAL
SEQRES 7 A 100 ASP ALA ASN GLY ILE GLN SER GLN MET LEU SER ARG TRP
SEQRES 8 A 100 SER ALA SER PHE THR VAL THR LEU GLU
HELIX 1 1 SER A 46 GLY A 55 1 10
SHEET 1 A 5 ILE A 4 ALA A 5 0
SHEET 2 A 5 LYS A 19 CYS A 24 1 O ASP A 21 N ILE A 4
SHEET 3 A 5 GLY A 62 LEU A 69 -1 N GLY A 62 O CYS A 24
SHEET 4 A 5 SER A 94 THR A 98 -1 O SER A 94 N LEU A 69
SHEET 5 A 5 TYR A 41 ALA A 42 -1 N TYR A 41 O PHE A 95
SHEET 1 B 3 VAL A 35 TYR A 36 0
SHEET 2 B 3 GLN A 84 GLN A 86 1 O GLN A 84 N VAL A 35
SHEET 3 B 3 VAL A 78 ASP A 79 -1 O VAL A 78 N SER A 85
SSBOND 1 CYS A 8 CYS A 24 1555 1555 2.04
SSBOND 2 CYS A 28 CYS A 48 1555 1555 2.03
CRYST1 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 23 2 Bytes