Header list of 1nhm.pdb file
Complete list - 23 20 Bytes
HEADER DNA-BINDING 17-NOV-94 1NHM
TITLE THE STRUCTURE OF THE HMG BOX AND ITS INTERACTION WITH DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIGH MOBILITY GROUP PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;
SOURCE 3 ORGANISM_COMMON: CHINESE HAMSTER;
SOURCE 4 ORGANISM_TAXID: 10029;
SOURCE 5 GENE: INSERT DERIVED BY PCR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5 ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX-2T;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T GENE: INSERT DERIVED BY PCR
KEYWDS DNA-BINDING
EXPDTA SOLUTION NMR
AUTHOR C.M.READ,P.D.CARY,C.CRANE-ROBINSON,P.C.DRISCOLL,M.O.M.CARILLO,
AUTHOR 2 D.G.NORMAN
REVDAT 3 23-FEB-22 1NHM 1 REMARK
REVDAT 2 24-FEB-09 1NHM 1 VERSN
REVDAT 1 07-FEB-95 1NHM 0
JRNL AUTH C.M.READ,P.D.CARY,C.CRANE-ROBINSON,P.C.DRISCOLL,
JRNL AUTH 2 M.O.M.CARILLO,D.G.NORMAN
JRNL TITL THE STRUCTURE OF THE HMG BOX AND ITS INTERACTION WITH DNA
JRNL REF NUCLEIC ACIDS MOL.BIOL. V. 9 222 1995
JRNL REFN ISSN 0933-1891
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.M.READ,P.D.CARY,C.CRANE-ROBINSON,P.C.DRISCOLL,D.G.NORMAN
REMARK 1 TITL SOLUTION STRUCTURE OF A DNA-BINDING DOMAIN FROM HMG1
REMARK 1 REF NUCLEIC ACIDS RES. V. 21 3427 1993
REMARK 1 REFN ISSN 0305-1048
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.0
REMARK 3 AUTHORS : NILGES ET AL. (SIMULATED ANNEALING, YASAP),
REMARK 3 BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NHM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175289.
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 : 1
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
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 TRP A 43 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 TRP A 43 CD1 - NE1 - CE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 TRP A 43 NE1 - CE2 - CZ2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 TRP A 43 NE1 - CE2 - CD2 ANGL. DEV. = -6.2 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 ALA A 4 77.35 3.31
REMARK 500 PRO A 5 159.31 -32.31
REMARK 500 ARG A 7 83.91 2.65
REMARK 500 PRO A 8 176.63 -53.11
REMARK 500 PRO A 9 150.42 -36.02
REMARK 500 ALA A 11 -68.11 106.94
REMARK 500 HIS A 27 62.59 -113.86
REMARK 500 PRO A 28 36.48 -79.33
REMARK 500 GLU A 41 -60.64 -90.02
REMARK 500 THR A 46 -150.07 -97.66
REMARK 500 ALA A 48 25.25 32.18
REMARK 500 GLN A 52 -56.59 -27.31
REMARK 500 GLU A 66 -27.44 -39.43
REMARK 500 ALA A 74 37.94 -98.85
REMARK 500 ASP A 79 61.55 85.44
REMARK 500 ALA A 80 58.65 152.27
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 ARG A 7 0.31 SIDE CHAIN
REMARK 500 ARG A 20 0.32 SIDE CHAIN
REMARK 500 ARG A 73 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NHN RELATED DB: PDB
DBREF 1NHM A 3 81 UNP P07156 HMG1_CRIGR 58 136
SEQRES 1 A 81 GLY SER ASN ALA PRO LYS ARG PRO PRO SER ALA PHE PHE
SEQRES 2 A 81 LEU PHE CYS SER GLU TYR ARG PRO LYS ILE LYS GLY GLU
SEQRES 3 A 81 HIS PRO GLY LEU SER ILE GLY ASP VAL ALA LYS LYS LEU
SEQRES 4 A 81 GLY GLU MET TRP ASN ASN THR ALA ALA ASP ASP LYS GLN
SEQRES 5 A 81 PRO TYR GLU LYS LYS ALA ALA LYS LEU LYS GLU LYS TYR
SEQRES 6 A 81 GLU LYS ASP ILE ALA ALA TYR ARG ALA LYS GLY LYS PRO
SEQRES 7 A 81 ASP ALA ALA
HELIX 1 H1 PHE A 12 GLU A 18 1 7
HELIX 2 H1' PRO A 21 GLU A 26 1H1 AND H1' BEND AROUND H2 6
HELIX 3 H2 GLY A 33 ASN A 44 1 12
HELIX 4 H3 PRO A 53 ARG A 73 1 21
CISPEP 1 ASP A 79 ALA A 80 0 0.14
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
Complete list - 23 20 Bytes