Header list of 1lbj.pdb file
Complete list - 23 20 Bytes
HEADER HORMONE/GROWTH FACTOR 03-APR-02 1LBJ
TITLE NMR SOLUTION STRUCTURE OF MOTILIN IN PHOSPHOLIPID BICELLAR SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MOTILIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE MOTILIN PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN)
KEYWDS A-HELIX, B-TURN OF TYPE I, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR A.ANDERSSON,L.MALER
REVDAT 4 23-FEB-22 1LBJ 1 REMARK
REVDAT 3 24-FEB-09 1LBJ 1 VERSN
REVDAT 2 13-JAN-04 1LBJ 1 JRNL
REVDAT 1 20-NOV-02 1LBJ 0
JRNL AUTH A.ANDERSSON,L.MALER
JRNL TITL NMR SOLUTION STRUCTURE AND DYNAMICS OF MOTILIN IN ISOTROPIC
JRNL TITL 2 PHOSPHOLIPID BICELLAR SOLUTION
JRNL REF J.BIOMOL.NMR V. 24 103 2002
JRNL REFN ISSN 0925-2738
JRNL PMID 12495026
JRNL DOI 10.1023/A:1020902915969
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.JARVET,J.ZDUNEK,P.DAMBERG,A.GRASLUND
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE AND POSITION OF PORCINE MOTILIN
REMARK 1 TITL 2 IN SODIUM DODECYL SULFATE MICELLES DETERMINED BY 1H NMR
REMARK 1 REF BIOCHEMISTRY V. 36 8153 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI970193B
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97.0, AMBER 5.0
REMARK 3 AUTHORS : MSI INC. (FELIX), PERALMANN, CASE, CALDWELL, ROSS,
REMARK 3 CHEATHAM, FERGUSON, SEIBEL, SINGH, WEINER &
REMARK 3 KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE BASED ON TOTAL OF 200
REMARK 3 DISTANCE AND 8 TORSION ANGLE CONSTRAINTS
REMARK 4
REMARK 4 1LBJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015813.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 50 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3 MM MOTILIN, 50MM KCL, 15%
REMARK 210 Q=0.5 DMPC,DMPG/DHPC
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA 2.8
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 21 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -3.7 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 THR A 6 107.26 77.95
REMARK 500 2 THR A 6 106.91 75.08
REMARK 500 3 VAL A 2 119.62 -167.00
REMARK 500 3 THR A 6 108.87 68.24
REMARK 500 4 VAL A 2 74.16 55.84
REMARK 500 4 THR A 6 108.47 80.24
REMARK 500 5 TYR A 7 -60.85 64.35
REMARK 500 6 PRO A 3 48.78 -80.50
REMARK 500 6 THR A 6 19.55 57.64
REMARK 500 6 TYR A 7 -59.40 62.95
REMARK 500 7 THR A 6 100.03 86.54
REMARK 500 8 ILE A 4 -77.33 -75.01
REMARK 500 8 THR A 6 89.30 67.36
REMARK 500 9 THR A 6 112.62 82.32
REMARK 500 10 THR A 6 99.46 65.14
REMARK 500 11 THR A 6 114.31 86.08
REMARK 500 12 THR A 6 92.41 62.28
REMARK 500 12 TYR A 7 -55.59 -22.85
REMARK 500 13 ILE A 4 -72.25 -129.23
REMARK 500 13 THR A 6 112.67 83.89
REMARK 500 14 THR A 6 99.14 62.13
REMARK 500 15 PRO A 3 49.18 -80.10
REMARK 500 15 TYR A 7 -57.02 65.30
REMARK 500 16 THR A 6 110.64 83.41
REMARK 500 17 VAL A 2 107.71 -38.50
REMARK 500 17 THR A 6 107.33 75.99
REMARK 500 18 VAL A 2 84.80 -1.31
REMARK 500 18 PRO A 3 72.71 -69.36
REMARK 500 18 THR A 6 108.67 81.35
REMARK 500 19 VAL A 2 76.67 38.11
REMARK 500 19 THR A 6 111.07 78.93
REMARK 500 20 THR A 6 26.70 45.80
REMARK 500 20 TYR A 7 -59.58 62.99
REMARK 500 21 TYR A 7 -60.15 -2.96
REMARK 500 22 ILE A 4 -77.30 -74.95
REMARK 500 22 THR A 6 100.55 70.49
REMARK 500 23 THR A 6 -17.72 93.18
REMARK 500 23 TYR A 7 -49.91 73.74
REMARK 500 24 THR A 6 70.88 59.74
REMARK 500 24 TYR A 7 -62.09 -12.24
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 7 0.08 SIDE CHAIN
REMARK 500 4 TYR A 7 0.10 SIDE CHAIN
REMARK 500 5 TYR A 7 0.07 SIDE CHAIN
REMARK 500 7 TYR A 7 0.07 SIDE CHAIN
REMARK 500 7 ARG A 18 0.07 SIDE CHAIN
REMARK 500 9 TYR A 7 0.07 SIDE CHAIN
REMARK 500 10 TYR A 7 0.08 SIDE CHAIN
REMARK 500 11 TYR A 7 0.08 SIDE CHAIN
REMARK 500 14 ARG A 18 0.08 SIDE CHAIN
REMARK 500 15 TYR A 7 0.09 SIDE CHAIN
REMARK 500 18 TYR A 7 0.12 SIDE CHAIN
REMARK 500 18 ARG A 18 0.11 SIDE CHAIN
REMARK 500 19 TYR A 7 0.11 SIDE CHAIN
REMARK 500 21 ARG A 18 0.10 SIDE CHAIN
REMARK 500 22 TYR A 7 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1LBJ A 1 22 UNP P12872 MOTI_HUMAN 26 47
SEQRES 1 A 22 PHE VAL PRO ILE PHE THR TYR GLY GLU LEU GLN ARG MET
SEQRES 2 A 22 GLN GLU LYS GLU ARG ASN LYS GLY GLN
HELIX 1 1 THR A 6 GLN A 22 1 17
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 - 23 20 Bytes