Header list of 1ccm.pdb file
Complete list - 29 20 Bytes
HEADER PLANT SEED PROTEIN 14-APR-93 1CCM
TITLE DIRECT NOE REFINEMENT OF CRAMBIN FROM 2D NMR DATA USING A SLOW-COOLING
TITLE 2 ANNEALING PROTOCOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CRAMBIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRAMBE HISPANICA SUBSP. ABYSSINICA;
SOURCE 3 ORGANISM_TAXID: 3721;
SOURCE 4 STRAIN: SUBSP. ABYSSINICA
KEYWDS PLANT SEED PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 8
AUTHOR A.M.J.J.BONVIN,J.A.C.RULLMANN,R.M.J.N.LAMERICHS,R.BOELENS,R.KAPTEIN
REVDAT 3 29-NOV-17 1CCM 1 REMARK HELIX
REVDAT 2 24-FEB-09 1CCM 1 VERSN
REVDAT 1 31-OCT-93 1CCM 0
JRNL AUTH A.M.BONVIN,J.A.RULLMANN,R.M.LAMERICHS,R.BOELENS,R.KAPTEIN
JRNL TITL "ENSEMBLE" ITERATIVE RELAXATION MATRIX APPROACH: A NEW NMR
JRNL TITL 2 REFINEMENT PROTOCOL APPLIED TO THE SOLUTION STRUCTURE OF
JRNL TITL 3 CRAMBIN.
JRNL REF PROTEINS V. 15 385 1993
JRNL REFN ISSN 0887-3585
JRNL PMID 8460109
JRNL DOI 10.1002/PROT.340150406
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.M.J.J.BONVIN,J.A.C.RULLMANN,R.M.J.N.LAMERICHS,R.BOELENS,
REMARK 1 AUTH 2 R.KAPTEIN
REMARK 1 TITL "ENSEMBLE" ITERATIVE RELAXATION MATRIX APPROACH: A NEW NMR
REMARK 1 TITL 2 REFINEMENT PROTOCOL APPLIED TO THE SOLUTION STRUCTURE OF
REMARK 1 TITL 3 CRAMBIN
REMARK 1 REF PROTEINS V. 15 385 1993
REMARK 1 REFN ISSN 0887-3585
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.A.C.RULLMANN,A.M.J.J.BONVIN,R.BOELENS,R.KAPTEIN
REMARK 1 TITL STRUCTURE DETERMINATION BY NMR-APPLICATION TO CRAMBIN
REMARK 1 EDIT D.M.SOUMPASIS, T.M.JOVIN
REMARK 1 REF COMPUTATION OF BIOMOLECULAR 1 1992
REMARK 1 REF 2 STRUCTURES; ACHIEVEMENTS
REMARK 1 REF 3 PROBLEMS, AND PERSPECTIVES
REMARK 1 PUBL SPRINGER-VERLAG, BERLIN
REMARK 1 REFN
REMARK 1 REFERENCE 3
REMARK 1 AUTH R.M.J.M.LAMERICHS
REMARK 1 TITL 2D NMR STUDIES OF BIOMOLECULES: PROTEIN STRUCTURE AND
REMARK 1 TITL 2 PROTEIN-DNA INTERACTIONS
REMARK 1 REF THESIS 1989
REMARK 1 REFN
REMARK 1 REFERENCE 4
REMARK 1 AUTH R.M.J.N.LAMERICHS,L.J.BERLINER,R.BOELENS,A.DEMARCO,M.LLINAS,
REMARK 1 AUTH 2 R.KAPTEIN
REMARK 1 TITL SECONDARY STRUCTURE AND HYDROGEN BONDING OF CRAMBIN IN
REMARK 1 TITL 2 SOLUTION
REMARK 1 REF EUR.J.BIOCHEM. V. 171 307 1988
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.A.W.H.VERMEULEN,R.M.J.M.LAMERICHS,L.J.BERLINER,A.DEMARCO,
REMARK 1 AUTH 2 M.LLINAS,R.BOELENS,J.ALLEMAN,R.KAPTEIN
REMARK 1 TITL 1H NMR CHARACTERIZATION OF TWO CRAMBIN SPECIES
REMARK 1 REF FEBS LETT. V. 219 426 1987
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GROMOS
REMARK 3 AUTHORS : VAN GUNSTEREN,BERENDSEN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CCM 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_1000172234.
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 : 8
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 1 THR A 1 CA - CB - CG2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 1 ILE A 7 CA - CB - CG1 ANGL. DEV. = 18.1 DEGREES
REMARK 500 1 PHE A 13 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 ARG A 17 CB - CA - C ANGL. DEV. = 20.3 DEGREES
REMARK 500 1 TYR A 29 CB - CG - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 TYR A 44 CB - CG - CD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 2 THR A 1 CA - CB - CG2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 2 PHE A 13 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ARG A 17 CB - CA - C ANGL. DEV. = 17.5 DEGREES
REMARK 500 2 ARG A 17 N - CA - CB ANGL. DEV. = -11.0 DEGREES
REMARK 500 2 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 2 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 2 TYR A 29 CB - CG - CD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ILE A 33 CG1 - CB - CG2 ANGL. DEV. = -13.8 DEGREES
REMARK 500 2 TYR A 44 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 PHE A 13 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 3 TYR A 29 CB - CG - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 3 TYR A 44 CB - CG - CD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 4 PHE A 13 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 4 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 TYR A 29 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 4 TYR A 44 CB - CG - CD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 5 PHE A 13 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 5 TYR A 29 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 5 TYR A 44 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 6 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 TYR A 29 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 7 PHE A 13 CB - CG - CD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 7 TYR A 29 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 7 TYR A 44 CB - CG - CD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 8 PHE A 13 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 8 TYR A 29 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 8 TYR A 44 CB - CG - CD1 ANGL. DEV. = -5.3 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 THR A 21 -71.71 -8.51
REMARK 500 1 PRO A 36 -38.51 -38.71
REMARK 500 2 SER A 6 41.34 -108.67
REMARK 500 2 ILE A 7 -41.24 47.84
REMARK 500 2 THR A 21 -68.39 -148.78
REMARK 500 2 ALA A 38 -0.64 73.50
REMARK 500 3 THR A 30 50.10 -143.50
REMARK 500 3 ALA A 38 -16.49 111.41
REMARK 500 3 ALA A 45 43.70 -103.75
REMARK 500 4 THR A 2 60.09 -101.55
REMARK 500 4 THR A 21 -71.30 -147.14
REMARK 500 4 ALA A 45 78.43 -108.56
REMARK 500 5 THR A 2 73.66 -110.85
REMARK 500 5 THR A 21 -70.39 -61.14
REMARK 500 5 ALA A 45 50.40 -95.21
REMARK 500 6 THR A 2 60.19 -101.87
REMARK 500 6 THR A 21 -67.52 -149.47
REMARK 500 7 ARG A 17 40.71 -97.07
REMARK 500 7 PRO A 19 -65.88 0.24
REMARK 500 8 THR A 2 68.66 -102.51
REMARK 500 8 THR A 21 -69.28 -154.55
REMARK 500 8 THR A 30 49.12 -145.19
REMARK 500 8 ALA A 38 -29.13 48.21
REMARK 500 8 ALA A 45 35.75 -91.07
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 ARG A 17 LEU A 18 7 147.58
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 10 0.15 SIDE CHAIN
REMARK 500 1 TYR A 29 0.07 SIDE CHAIN
REMARK 500 2 ARG A 17 0.11 SIDE CHAIN
REMARK 500 3 TYR A 29 0.08 SIDE CHAIN
REMARK 500 4 TYR A 29 0.10 SIDE CHAIN
REMARK 500 6 TYR A 44 0.07 SIDE CHAIN
REMARK 500 7 TYR A 29 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 2 ARG A 17 -12.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CCN RELATED DB: PDB
DBREF 1CCM A 1 46 UNP P01542 CRAM_CRAAB 1 46
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 PRO GLU ALA LEU 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 H1 ILE A 7 LEU A 18 13/10 CONFORMATION RES 17,18 12
HELIX 2 H2 GLU A 23 THR A 30 1 8
SHEET 1 S1 2 THR A 1 CYS A 4 0
SHEET 2 S1 2 CYS A 32 ILE A 35 -1
SSBOND 1 CYS A 3 CYS A 40 1555 1555 2.03
SSBOND 2 CYS A 4 CYS A 32 1555 1555 2.04
SSBOND 3 CYS A 16 CYS A 26 1555 1555 2.05
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 - 29 20 Bytes