Header list of 1k76.pdb file
Complete list - 27 202 Bytes
HEADER SIGNALING PROTEIN 18-OCT-01 1K76
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL SEM-5 SH3 DOMAIN (MINIMIZED
TITLE 2 AVERAGE STRUCTURE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEX MUSCLE ABNORMAL PROTEIN 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN (RESIDUES 155-214);
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 3 ORGANISM_TAXID: 6239;
SOURCE 4 GENE: SEM-5;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET19B
KEYWDS ALL BETA PROTEIN, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR J.FERREON,D.VOLK,B.LUXON,D.GORENSTEIN,V.HILSER
REVDAT 3 27-OCT-21 1K76 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1K76 1 VERSN
REVDAT 1 20-MAY-03 1K76 0
JRNL AUTH J.FERREON,D.VOLK,B.LUXON,D.GORENSTEIN,V.HILSER
JRNL TITL SOLUTION STRUCTURE, DYNAMICS AND THERMODYNAMICS OF THE
JRNL TITL 2 NATIVE STATE ENSEMBLE OF SEM-5 C-TERMINAL SH3 DOMAIN
JRNL REF BIOCHEMISTRY V. 42 5582 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12741814
JRNL DOI 10.1021/BI030005J
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER, ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K76 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014645.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.8
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 13C,15N 1MM SEM-5 SH3 DOMAIN 50
REMARK 210 MM SODIUM ACETATE BUFFER, 10 MM
REMARK 210 CACL2, 100 MM NACL,PH 4.8, 90%
REMARK 210 H20, 10%D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-NOESY-HSQC; 3D 13C-NOESY
REMARK 210 -HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX, VNMR
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
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 : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED
REMARK 210 USING TRIPLE-RESONANCE NMR SPECTROSCOPY
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 HIS A 1
REMARK 465 MET A 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HE2 PHE A 51 HG13 VAL A 56 1.10
REMARK 500 OD2 ASP A 27 HD12 LEU A 44 1.42
REMARK 500 O SER A 61 HA ASN A 62 1.45
REMARK 500 OD1 ASP A 27 HD23 LEU A 44 1.52
REMARK 500 O ASN A 60 N ASN A 62 1.63
REMARK 500 C SER A 61 CA ASN A 62 1.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 3 N GLU A 3 CA -0.282
REMARK 500 GLU A 3 CA GLU A 3 CB -0.138
REMARK 500 GLU A 3 CA GLU A 3 C -0.273
REMARK 500 GLU A 3 C THR A 4 N -0.184
REMARK 500 THR A 4 N THR A 4 CA -0.218
REMARK 500 LYS A 5 CB LYS A 5 CG -0.192
REMARK 500 LYS A 24 CA LYS A 24 CB -0.141
REMARK 500 ARG A 25 CD ARG A 25 NE -0.136
REMARK 500 ARG A 25 NE ARG A 25 CZ -0.105
REMARK 500 ARG A 47 CZ ARG A 47 NH1 0.115
REMARK 500 ARG A 48 CD ARG A 48 NE -0.115
REMARK 500 ASN A 60 CA ASN A 60 C -0.226
REMARK 500 ASN A 60 C SER A 61 N -0.166
REMARK 500 SER A 61 N SER A 61 CA -0.254
REMARK 500 SER A 61 CA SER A 61 CB -0.100
REMARK 500 SER A 61 C ASN A 62 N -0.186
REMARK 500 ASN A 62 N ASN A 62 CA -0.290
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 3 CA - C - N ANGL. DEV. = -13.6 DEGREES
REMARK 500 LYS A 5 CG - CD - CE ANGL. DEV. = -18.0 DEGREES
REMARK 500 PHE A 11 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 LYS A 24 CB - CG - CD ANGL. DEV. = -30.0 DEGREES
REMARK 500 ARG A 25 NE - CZ - NH1 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ARG A 25 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG A 48 NE - CZ - NH1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASN A 60 CB - CA - C ANGL. DEV. = -12.6 DEGREES
REMARK 500 ASN A 60 N - CA - CB ANGL. DEV. = 15.6 DEGREES
REMARK 500 ASN A 60 CA - C - N ANGL. DEV. = -15.4 DEGREES
REMARK 500 ASN A 62 C - N - CA ANGL. DEV. = -23.5 DEGREES
REMARK 500 ASN A 62 CA - CB - CG ANGL. DEV. = -23.9 DEGREES
REMARK 500 ASN A 62 N - CA - C ANGL. DEV. = -22.9 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 LYS A 24 -166.19 -123.28
REMARK 500 ASN A 45 -37.75 79.65
REMARK 500 ASN A 46 -23.05 -171.78
REMARK 500 ALA A 57 114.65 -161.34
REMARK 500 ASN A 60 62.24 38.54
REMARK 500 SER A 61 94.93 -25.22
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 47 0.16 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K76 A 3 62 UNP P29355 SEM5_CAEEL 155 214
SEQADV 1K76 ALA A 57 UNP P29355 CYS 209 ENGINEERED MUTATION
SEQRES 1 A 62 HIS MET GLU THR LYS PHE VAL GLN ALA LEU PHE ASP PHE
SEQRES 2 A 62 ASN PRO GLN GLU SER GLY GLU LEU ALA PHE LYS ARG GLY
SEQRES 3 A 62 ASP VAL ILE THR LEU ILE ASN LYS ASP ASP PRO ASN TRP
SEQRES 4 A 62 TRP GLU GLY GLN LEU ASN ASN ARG ARG GLY ILE PHE PRO
SEQRES 5 A 62 SER ASN TYR VAL ALA PRO TYR ASN SER ASN
SHEET 1 A 5 ARG A 47 PRO A 52 0
SHEET 2 A 5 TRP A 39 LEU A 44 -1 N GLY A 42 O GLY A 49
SHEET 3 A 5 VAL A 28 ASN A 33 -1 N THR A 30 O GLN A 43
SHEET 4 A 5 PHE A 6 ALA A 9 -1 N VAL A 7 O ILE A 29
SHEET 5 A 5 VAL A 56 PRO A 58 -1 O ALA A 57 N GLN A 8
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 - 27 202 Bytes