Header list of 1m23.pdb file
Complete list - 23 20 Bytes
HEADER MEMBRANE PROTEIN 09-DEC-98 1M23
TITLE STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (P23);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CYTOPLASMIC DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED FROM THE GOLGI
SOURCE 4 STACK OF THE ER (ENDOPLASMIC RETICULUM) OF NEW ZEALAND WHITE RABBIT
SOURCE 5 (ORYCTOLAGUS CUNICULUS) LIVER CELLS.
KEYWDS TRANSPORT, PROTEIN TRANSPORT, TRANSMEMBRANE, GLYCOPROTEIN, VESICULAR
KEYWDS 2 TRANSPORT, COP, COATOMER, GOLGI STACK, SOLUTION STRUCTURE, P23
KEYWDS 3 FAMILY, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.WEIDLER,C.REINHARD,F.WIELAND,P.ROESCH
REVDAT 4 23-FEB-22 1M23 1 REMARK
REVDAT 3 24-FEB-09 1M23 1 VERSN
REVDAT 2 01-APR-03 1M23 1 JRNL
REVDAT 1 29-SEP-99 1M23 0
JRNL AUTH C.REINHARD,C.HARTER,M.BREMSER,B.BRUGGER,K.SOHN,J.B.HELMS,
JRNL AUTH 2 F.WIELAND
JRNL TITL RECEPTOR-INDUCED POLYMERIZATION OF COATOMER.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 96 1224 1999
JRNL REFN ISSN 0027-8424
JRNL PMID 9990005
JRNL DOI 10.1073/PNAS.96.4.1224
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.840
REMARK 3 AUTHORS : BRUNGER, NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRATEGY USED FOR NMR STRUCTURE
REMARK 3 CALCULATION: EXPERIMENTAL RESTRAINTS FOR THE STRUCTURE
REMARK 3 CALCULATIONS INITIALLY, FREQUENCY DEGENERATED NOESY CROSS-PEAKS
REMARK 3 WERE INCORPORATED INTO THE STRUCTURE CALCULATION AS 'AMBIGUOUS'.
REMARK 3 SUBSEQUENTLY, THE PROTON-PROTON DISTANCES IN THE CALCULATED
REMARK 3 STRUCTURES WERE DETERMINED USING THE PROGRAM 'BACKCALC_DB 2.0'
REMARK 3 (SOFTWARE SYMBIOSE, INC., BAYREUTH, GERMANY) AND COMPARED WITH
REMARK 3 THE COMBINATIONS OF DISTANCES POSSIBLE FOR EACH FREQUENCY
REMARK 3 DEGENERATED NOESY CROSS-PEAK. IF ONLY ONE OF THE POSSIBLE
REMARK 3 DISTANCE COMBINATIONS WAS FULFILLED IN MORE THAN 50% OF THE
REMARK 3 CALCULATED STRUCTURES, THE DISTANCE INFORMATION WAS USED IN
REMARK 3 FURTHER STRUCTURE CALCULATIONS. THIS PROCEDURE WAS REPEATED
REMARK 3 SEVERAL TIMES, LEADING TO A TOTAL OF 223 INTRARESIDUAL AND 249
REMARK 3 INTERRESIDUAL NOE CONNECTIVITIES. STRUCTURE CALCULATIONS
REMARK 3 STRUCTURES CALCULATIONS WERE PERFORMED USING A MODIFIED AB
REMARK 3 INITIO SIMULATED ANNEALING PROTOCOL (NILGES, UNPUBLISHED) WITH X-
REMARK 3 PLOR V3.840. THE CALCULATION STRATEGY INCLUDES FLOATING
REMARK 3 ASSIGNMENT OF PROCHIRAL GROUPS AND A REDUCED PRESENTATION FOR
REMARK 3 NON-BONDED INTERACTIONS FOR PART OF THE CALCULATION TO INCREASE
REMARK 3 EFFICIENCY. A MORE DETAILED DESCRIPTION OF THE PROTOCOL IS GIVEN
REMARK 3 IN KHARRAT ET AL. (EMBO J. 14 (1995) 3572-84). STRUCTURE
REMARK 3 PARAMETERS WERE EXTRACTED FROM THE STANDARD FILES PARALLHDG.PRO
REMARK 3 AND TOPALLHDG.PRO OF X-PLOR V3.840. IN EACH ROUND OF THE
REMARK 3 STRUCTURE CALCULATION 100 STRUCTURES WERE CALCULATED. OF THE 100
REMARK 3 STRUCTURES RESULTING FROM THE FINAL ROUND OF STRUCTURE
REMARK 3 CALCULATION, THOSE 30 STRUCTURES THAT SHOWED THE LOWEST TOTAL
REMARK 3 ENERGY VALUES WERE SELECTED FOR FURTHER CHARACTERIZATION.
REMARK 4
REMARK 4 1M23 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007011.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 280
REMARK 210 PH : 3.6
REMARK 210 IONIC STRENGTH : 650 MM
REMARK 210 PRESSURE : 10E+5 PA ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; CLEAN-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX 600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE 2.0, X-PLOR 3.840
REMARK 210 METHOD USED : SIMULATED ANNEALING, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY, AGREEMENT WITH
REMARK 210 EXPERIMENTAL DATA
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 LEU A 2 -14.40 -44.91
REMARK 500 1 PHE A 6 -64.92 -93.42
REMARK 500 1 ALA A 8 -93.59 -62.37
REMARK 500 2 ALA A 8 -91.94 -80.45
REMARK 500 3 PHE A 6 -60.02 -91.84
REMARK 500 3 ALA A 8 -94.60 -80.04
REMARK 500 4 PHE A 6 -60.91 -91.21
REMARK 500 4 ALA A 8 -94.03 -68.64
REMARK 500 5 PHE A 6 -64.27 -91.85
REMARK 500 5 ALA A 8 -95.01 -80.83
REMARK 500 6 ALA A 8 -91.59 -71.20
REMARK 500 7 ALA A 8 -92.04 -74.04
REMARK 500 8 PHE A 6 -62.93 -93.50
REMARK 500 8 ALA A 8 -90.11 -79.81
REMARK 500 9 ALA A 8 -94.02 -69.84
REMARK 500 10 PHE A 6 -62.95 -93.26
REMARK 500 10 ALA A 8 -89.42 -77.24
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 1 ARG A 3 0.28 SIDE CHAIN
REMARK 500 1 ARG A 4 0.32 SIDE CHAIN
REMARK 500 2 ARG A 3 0.27 SIDE CHAIN
REMARK 500 2 ARG A 4 0.27 SIDE CHAIN
REMARK 500 3 ARG A 3 0.23 SIDE CHAIN
REMARK 500 3 ARG A 4 0.24 SIDE CHAIN
REMARK 500 4 ARG A 3 0.32 SIDE CHAIN
REMARK 500 4 ARG A 4 0.26 SIDE CHAIN
REMARK 500 5 ARG A 3 0.21 SIDE CHAIN
REMARK 500 5 ARG A 4 0.13 SIDE CHAIN
REMARK 500 6 ARG A 3 0.28 SIDE CHAIN
REMARK 500 6 ARG A 4 0.13 SIDE CHAIN
REMARK 500 7 ARG A 3 0.31 SIDE CHAIN
REMARK 500 7 ARG A 4 0.16 SIDE CHAIN
REMARK 500 8 ARG A 3 0.30 SIDE CHAIN
REMARK 500 9 ARG A 3 0.32 SIDE CHAIN
REMARK 500 9 ARG A 4 0.32 SIDE CHAIN
REMARK 500 10 ARG A 3 0.30 SIDE CHAIN
REMARK 500 10 ARG A 4 0.20 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1M23 A 2 13 UNP Q28735 TMP21_RABIT 207 218
SEQRES 1 A 13 TYR LEU ARG ARG PHE PHE LYS ALA LYS LYS LEU ILE GLU
HELIX 1 1 LEU A 2 LEU A 11 1 10
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