Header list of 1cxr.pdb file
Complete list - 14 20 Bytes
HEADER PLANT PROTEIN 30-AUG-99 1CXR
TITLE AUTOMATED 2D NOESY ASSIGNMENT AND STRUCTURE CALCULATION OF
TITLE 2 CRAMBIN(S22/I25) WITH SELF-CORRECTING DISTANCE GEOMETRY BASED
TITLE 3 NOAH/DIAMOD PROGRAMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CRAMBIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ISOFORM OF CRAMBIN (46 RESIDUES);
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRAMBE HISPANICA SUBSP. ABYSSINICA;
SOURCE 3 ORGANISM_TAXID: 3721;
SOURCE 4 STRAIN: SUBSP. ABYSSINICA;
SOURCE 5 ORGAN: SEED
KEYWDS CRAMBIN, CRAMBE ABYSSINICA, PLANT SEED PROTEIN FEB. 20, 1997, PLANT
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR Y.XU,J.WU,D.GORENSTEIN,W.BRAUN
REVDAT 6 14-MAR-18 1CXR 1 SEQADV
REVDAT 5 24-JAN-18 1CXR 1 JRNL REMARK
REVDAT 4 24-FEB-09 1CXR 1 VERSN
REVDAT 3 01-APR-03 1CXR 1 JRNL
REVDAT 2 01-NOV-99 1CXR 1 COMPND
REVDAT 1 07-SEP-99 1CXR 0
JRNL AUTH Y.XU,J.WU,D.GORENSTEIN,W.BRAUN
JRNL TITL AUTOMATED 2D NOESY ASSIGNMENT AND STRUCTURE CALCULATION OF
JRNL TITL 2 CRAMBIN(S22/I25) WITH THE SELF-CORRECTING DISTANCE GEOMETRY
JRNL TITL 3 BASED NOAH/DIAMOD PROGRAMS.
JRNL REF J.MAGN.RESON. V. 136 76 1999
JRNL REFN ISSN 0022-2364
JRNL PMID 9887292
JRNL DOI 10.1006/JMRE.1998.1616
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.MUMENTHALER,W.BRAUN
REMARK 1 TITL AUTOMATED ASSIGNMENT OF SIMULATED, EXPERIMENTAL NOESY
REMARK 1 TITL 2 SPECTRA OF PROTEINS BY FEEDBACK FILTERING AND
REMARK 1 TITL 3 SELF-CORRECTING DISTANCE GEOMETRY
REMARK 1 REF J.MOL.BIOL. V. 254 465 1995
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1995.0631
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.MUMENTHALER,P.GUNTERT,W.BRAUN,K.WUTHRICH
REMARK 1 TITL AUTOMATED COMBINED ASSIGNMENT OF NOESY SPECTRA AND
REMARK 1 TITL 2 THREE-DIMENSIONAL PROTEIN STRUCTURE DETERMINATION
REMARK 1 REF J.BIOMOL.NMR V. 10 351 1997
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1018383106236
REMARK 1 REFERENCE 3
REMARK 1 AUTH Y.XU,C.H.SCHEIN,W.BRAUN
REMARK 1 TITL COMBINED AUTOMATED ASSIGNMENT OF NMR SPECTRA AND CALCULATION
REMARK 1 TITL 2 OF THREE- DIMENSIONAL PROTEIN STRUCTURES
REMARK 1 REF BIOLOGICAL MAGNETIC V. 17 37 1999
REMARK 1 REF 2 RESONANCE
REMARK 1 PUBL KLUWER/ACADEMIC/PLENUM PUBLISHERS
REMARK 1 REFERENCE 4
REMARK 1 AUTH T.H.SCHAUMANN,W.BRAUN,K.WUTHRICH
REMARK 1 TITL A PROGRAM, FANTOM, FOR ENERGY REFINEMENT OF POLYPEPTIDES AND
REMARK 1 TITL 2 PROTEINS USING A NEWTON-RAPHSON MINIMIZER IN THE TORSION
REMARK 1 TITL 3 ANGLE SPACE
REMARK 1 REF BIOPOLYMERS V. 29 679 1990
REMARK 1 REFN ISSN 0006-3525
REMARK 1 REFERENCE 5
REMARK 1 AUTH R.FRACZKIEWICZ,W.BRAUN
REMARK 1 TITL EXACT AND EFFICIENT ANALYTICAL CALCULATION OF THE ACCESSIBLE
REMARK 1 TITL 2 SURFACE AREAS AND THEIR GRADIENTS MACROMOLECULES
REMARK 1 REF J.COMPUT.CHEM. V. 19 319 1998
REMARK 1 REFN ISSN 0192-8651
REMARK 1 DOI 10.1002/(SICI)1096-987X(199802)19:3<319::AID-JCC6>3.3.CO;2-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NOAH 1.0, FANTOM 4.0
REMARK 3 AUTHORS : C.MUMENTHALER, Y.XU, W.BRAUN (NOAH), TH.SCHAUMANN,
REMARK 3 W.BRAUN, K.WUTHRICH, R.FRACZKIEWICZ (FANTOM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE REFERENCE: J. MAGN. RESON. 136, P76
REMARK 3 -85(1999)
REMARK 4
REMARK 4 1CXR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000009611.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 2.5 MM CRAMBIN(SER/ILE) 0.7 ML
REMARK 210 OF 75% D6-ACETONE, 20%H2O,5%D2O
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : VXRS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIAMOD 1.0
REMARK 210 METHOD USED : SELF-CORRECTING DISTANCE
REMARK 210 GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY,TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
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: 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 ALA A 24 -66.68 74.41
REMARK 500 1 TYR A 29 32.16 -89.98
REMARK 500 1 THR A 30 17.13 -140.00
REMARK 500 1 CYS A 32 -179.14 -64.87
REMARK 500 2 THR A 21 -85.70 -102.35
REMARK 500 2 SER A 22 -56.75 76.33
REMARK 500 2 THR A 28 -125.28 -90.09
REMARK 500 2 TYR A 29 40.15 -89.96
REMARK 500 2 ALA A 38 -94.32 -157.11
REMARK 500 3 THR A 21 34.07 -159.94
REMARK 500 3 SER A 22 -131.23 38.36
REMARK 500 3 GLU A 23 54.53 -90.05
REMARK 500 3 ALA A 24 -69.94 73.37
REMARK 500 3 PRO A 36 -80.23 -75.00
REMARK 500 3 ALA A 45 -65.82 75.59
REMARK 500 4 THR A 21 -76.60 -135.08
REMARK 500 4 SER A 22 60.37 35.77
REMARK 500 4 ALA A 38 -93.58 -156.93
REMARK 500 4 ASP A 43 -60.24 -110.00
REMARK 500 5 THR A 21 136.73 64.70
REMARK 500 5 SER A 22 -82.36 -63.96
REMARK 500 5 GLU A 23 -75.90 -90.00
REMARK 500 5 ALA A 24 -70.45 -171.21
REMARK 500 5 TYR A 29 32.70 -90.04
REMARK 500 5 THR A 30 18.07 -140.01
REMARK 500 5 ALA A 38 60.98 34.66
REMARK 500 5 ALA A 45 -63.86 75.89
REMARK 500 6 ILE A 7 -14.56 83.49
REMARK 500 6 THR A 21 -77.99 -131.41
REMARK 500 6 TYR A 44 -51.46 -138.83
REMARK 500 6 ALA A 45 -64.99 75.42
REMARK 500 7 PHE A 13 40.21 -90.00
REMARK 500 7 THR A 21 99.58 61.19
REMARK 500 7 GLU A 23 -89.17 -90.03
REMARK 500 7 ALA A 24 -94.59 -173.94
REMARK 500 7 PRO A 36 -168.30 -75.00
REMARK 500 7 ALA A 38 71.39 30.66
REMARK 500 8 THR A 21 -78.09 -134.64
REMARK 500 8 ALA A 24 -157.56 -149.70
REMARK 500 9 SER A 22 -143.07 46.09
REMARK 500 9 GLU A 23 45.62 -89.94
REMARK 500 9 ALA A 24 -66.79 75.54
REMARK 500 9 TYR A 29 46.19 -90.01
REMARK 500 9 THR A 30 12.20 -140.01
REMARK 500 9 TYR A 44 -51.88 -125.12
REMARK 500 9 ALA A 45 84.36 54.42
REMARK 500 10 THR A 21 74.07 58.47
REMARK 500 10 SER A 22 -78.04 -72.18
REMARK 500 10 ALA A 24 -66.73 74.37
REMARK 500 10 ALA A 27 -79.40 -90.01
REMARK 500
REMARK 500 THIS ENTRY HAS 52 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 3 ARG A 17 0.13 SIDE CHAIN
REMARK 500 6 ARG A 10 0.15 SIDE CHAIN
REMARK 500 8 ARG A 17 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CCM RELATED DB: PDB
REMARK 900 1CCM CONTAINS TWO ISOFORMS: SER22/ILE25 AND PRO22/LEU
DBREF 1CXR A 1 46 UNP P01542 CRAM_CRAAB 1 46
SEQADV 1CXR SER A 22 UNP P01542 PRO 22 ENGINEERED MUTATION
SEQRES 1 A 46 THR THR CYS CYS PRO SER ILE VAL ALA ARG SER ASN PHE
SEQRES 2 A 46 ASN VAL CYS ARG LEU PRO GLY THR SER GLU ALA ILE CYS
SEQRES 3 A 46 ALA THR TYR THR GLY CYS ILE ILE ILE PRO GLY ALA THR
SEQRES 4 A 46 CYS PRO GLY ASP TYR ALA ASN
HELIX 1 1 ILE A 7 CYS A 16 5 10
SSBOND 1 CYS A 3 CYS A 40 1555 1555 1.99
SSBOND 2 CYS A 4 CYS A 32 1555 1555 1.94
SSBOND 3 CYS A 16 CYS A 26 1555 1555 2.04
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 - 14 20 Bytes