Header list of 1g7d.pdb file
Complete list - b 23 2 Bytes
HEADER CHAPERONE 10-NOV-00 1G7D
TITLE NMR STRUCTURE OF ERP29 C-DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOPLASMIC RETICULUM PROTEIN ERP29;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PQE30
KEYWDS ALPHA HELICAL PROTEIN, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.LIEPINSH,S.MKRTCHIAN,M.BARISHEV,A.SHARIPO,M.INGELMAN-SUNDBERG,
AUTHOR 2 G.OTTING
REVDAT 5 23-FEB-22 1G7D 1 REMARK
REVDAT 4 24-FEB-09 1G7D 1 VERSN
REVDAT 3 01-APR-03 1G7D 1 JRNL
REVDAT 2 04-JUL-01 1G7D 1 JRNL HEADER
REVDAT 1 29-NOV-00 1G7D 0
JRNL AUTH E.LIEPINSH,M.BARYSHEV,A.SHARIPO,M.INGELMAN-SUNDBERG,
JRNL AUTH 2 G.OTTING,S.MKRTCHIAN
JRNL TITL THIOREDOXIN FOLD AS HOMODIMERIZATION MODULE IN THE PUTATIVE
JRNL TITL 2 CHAPERONE ERP29: NMR STRUCTURES OF THE DOMAINS AND
JRNL TITL 3 EXPERIMENTAL MODEL OF THE 51 KDA DIMER.
JRNL REF STRUCTURE V. 9 457 2001
JRNL REFN ISSN 0969-2126
JRNL PMID 11435111
JRNL DOI 10.1016/S0969-2126(01)00607-4
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.5, OPAL 2.6
REMARK 3 AUTHORS : BRUKER (XWINNMR), LUGINBUL (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE INPUT FOR THE FINAL STRUCTURE
REMARK 3 CALCULATION OF C-DOMAIN PROTEIN CONSISTED OF 1492 UPPER LIMIT
REMARK 3 DISTANCE RESTRAINTS AND 340 MEASURED HN-HA, HA-HB, 15N-HB
REMARK 3 COUPLING CONSTANTS RESULTING IN 328 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1G7D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012325.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308; 308
REMARK 210 PH : 4.7; 4.7
REMARK 210 IONIC STRENGTH : .1; .1
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM C-DOMAIN ERP29 U-15N,13C;
REMARK 210 2MM C-DOMAIN ERP29
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA, HNCO, HN(CO)CA; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 2D NOESY, 2D
REMARK 210 TOCSY, DQF COSY; 3D HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PROSA 3.6, XEASY 970326, DYANA
REMARK 210 1.5, MOLMOL 2.6.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY,TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE SIGNAL ASSIGNMENT WAS DETERMINED USING TRIPLE
REMARK 210 -RESONANCE NMR SPECTROSCOPY. THE STRUCTURE WAS DETERMINED USING
REMARK 210 STANDARD 2D 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: 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 HG SER A 225 OE2 GLU A 229 1.58
REMARK 500 OD1 ASP A 215 HG SER A 219 1.60
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 2 PHE A 168 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 TYR A 202 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 6 TRP A 198 CB - CG - CD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 6 LYS A 252 CB - CA - C ANGL. DEV. = 12.6 DEGREES
REMARK 500 7 PHE A 168 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 8 ARG A 251 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 9 TYR A 202 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 11 GLU A 220 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 12 TRP A 198 CB - CG - CD2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 12 GLU A 220 CB - CA - C ANGL. DEV. = 13.8 DEGREES
REMARK 500 12 ALA A 255 C - N - CA ANGL. DEV. = 19.7 DEGREES
REMARK 500 12 ALA A 255 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 14 PHE A 168 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 14 LYS A 252 CB - CA - C ANGL. DEV. = 14.3 DEGREES
REMARK 500 15 ARG A 242 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 16 TYR A 161 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 20 ARG A 251 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 20 ARG A 251 NE - CZ - NH2 ANGL. DEV. = -3.0 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 194 -31.92 85.54
REMARK 500 1 GLN A 212 -82.26 -118.11
REMARK 500 1 GLU A 234 3.73 -69.23
REMARK 500 1 PHE A 250 69.56 -155.89
REMARK 500 1 LYS A 252 -71.72 -97.47
REMARK 500 1 ALA A 255 33.05 -66.85
REMARK 500 2 THR A 194 -39.61 75.34
REMARK 500 2 GLN A 212 -93.66 -118.95
REMARK 500 2 GLU A 234 3.51 -68.61
REMARK 500 2 PHE A 250 27.03 -153.19
REMARK 500 2 ARG A 251 92.01 -61.64
REMARK 500 2 ALA A 255 98.71 -33.60
REMARK 500 2 GLU A 256 -6.10 -58.89
REMARK 500 2 GLU A 258 49.11 -39.32
REMARK 500 3 THR A 194 -33.82 85.70
REMARK 500 3 GLN A 212 -82.42 -106.85
REMARK 500 3 GLU A 234 3.79 -68.61
REMARK 500 3 LYS A 236 -6.72 -146.48
REMARK 500 3 LYS A 252 -71.36 -97.58
REMARK 500 3 ALA A 255 33.51 -69.64
REMARK 500 3 LYS A 257 47.81 -78.11
REMARK 500 4 ALA A 171 68.21 -69.10
REMARK 500 4 THR A 194 -39.72 86.29
REMARK 500 4 GLN A 212 -80.93 -123.62
REMARK 500 4 GLU A 234 3.32 -67.90
REMARK 500 4 LYS A 236 -26.13 -150.44
REMARK 500 4 LYS A 252 -71.05 -97.37
REMARK 500 4 ALA A 255 33.43 -61.72
REMARK 500 4 LYS A 257 23.38 -69.97
REMARK 500 5 THR A 194 -32.33 77.54
REMARK 500 5 GLN A 212 -82.46 -121.47
REMARK 500 5 LYS A 231 152.12 -45.58
REMARK 500 5 GLU A 234 6.26 -62.01
REMARK 500 5 LYS A 236 13.71 -144.81
REMARK 500 5 ARG A 251 69.34 -67.83
REMARK 500 5 LYS A 252 -71.26 -96.80
REMARK 500 5 ALA A 255 32.82 -69.55
REMARK 500 5 LYS A 257 23.99 -58.98
REMARK 500 6 SER A 172 -76.12 -82.95
REMARK 500 6 THR A 194 -31.75 82.31
REMARK 500 6 GLN A 212 -81.01 -119.84
REMARK 500 6 GLU A 214 0.81 -68.20
REMARK 500 6 LYS A 231 151.04 -49.81
REMARK 500 6 GLU A 234 3.70 -67.68
REMARK 500 6 LYS A 252 -71.72 -97.32
REMARK 500 6 ALA A 255 33.72 -69.43
REMARK 500 6 LYS A 257 23.95 -68.65
REMARK 500 7 THR A 194 -42.01 85.69
REMARK 500 7 GLN A 212 -86.77 -119.99
REMARK 500 7 LYS A 231 150.71 -45.36
REMARK 500
REMARK 500 THIS ENTRY HAS 148 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 2 PHE A 168 0.10 SIDE CHAIN
REMARK 500 3 ARG A 242 0.08 SIDE CHAIN
REMARK 500 3 ARG A 251 0.21 SIDE CHAIN
REMARK 500 5 ARG A 223 0.12 SIDE CHAIN
REMARK 500 5 ARG A 242 0.10 SIDE CHAIN
REMARK 500 5 ARG A 251 0.08 SIDE CHAIN
REMARK 500 6 PHE A 168 0.09 SIDE CHAIN
REMARK 500 6 PHE A 216 0.12 SIDE CHAIN
REMARK 500 6 ARG A 242 0.10 SIDE CHAIN
REMARK 500 6 ARG A 251 0.23 SIDE CHAIN
REMARK 500 7 TYR A 161 0.07 SIDE CHAIN
REMARK 500 7 ARG A 251 0.19 SIDE CHAIN
REMARK 500 8 ASP A 162 0.09 SIDE CHAIN
REMARK 500 8 ARG A 223 0.18 SIDE CHAIN
REMARK 500 9 TYR A 161 0.08 SIDE CHAIN
REMARK 500 9 ARG A 177 0.12 SIDE CHAIN
REMARK 500 9 ARG A 251 0.20 SIDE CHAIN
REMARK 500 10 ARG A 177 0.10 SIDE CHAIN
REMARK 500 10 ARG A 223 0.08 SIDE CHAIN
REMARK 500 11 ARG A 177 0.09 SIDE CHAIN
REMARK 500 11 PHE A 216 0.14 SIDE CHAIN
REMARK 500 12 ARG A 177 0.08 SIDE CHAIN
REMARK 500 13 PHE A 168 0.10 SIDE CHAIN
REMARK 500 13 ARG A 177 0.09 SIDE CHAIN
REMARK 500 13 ASP A 211 0.07 SIDE CHAIN
REMARK 500 13 PHE A 216 0.12 SIDE CHAIN
REMARK 500 14 PHE A 216 0.10 SIDE CHAIN
REMARK 500 14 ARG A 251 0.12 SIDE CHAIN
REMARK 500 16 PHE A 216 0.09 SIDE CHAIN
REMARK 500 17 ARG A 174 0.10 SIDE CHAIN
REMARK 500 17 ARG A 223 0.09 SIDE CHAIN
REMARK 500 18 ARG A 177 0.08 SIDE CHAIN
REMARK 500 18 ASP A 211 0.07 SIDE CHAIN
REMARK 500 18 PHE A 216 0.10 SIDE CHAIN
REMARK 500 18 ARG A 223 0.07 SIDE CHAIN
REMARK 500 18 ARG A 242 0.08 SIDE CHAIN
REMARK 500 19 ASP A 211 0.07 SIDE CHAIN
REMARK 500 19 ARG A 242 0.08 SIDE CHAIN
REMARK 500 20 ARG A 174 0.11 SIDE CHAIN
REMARK 500 20 PHE A 216 0.08 SIDE CHAIN
REMARK 500 20 ARG A 251 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G7E RELATED DB: PDB
REMARK 900 N-DOMAIN OF ERP29 PROTEIN
DBREF 1G7D A 155 260 UNP P52555 ERP29_RAT 155 260
SEQRES 1 A 106 PRO GLY CYS LEU PRO ALA TYR ASP ALA LEU ALA GLY GLN
SEQRES 2 A 106 PHE ILE GLU ALA SER SER ARG GLU ALA ARG GLN ALA ILE
SEQRES 3 A 106 LEU LYS GLN GLY GLN ASP GLY LEU SER GLY VAL LYS GLU
SEQRES 4 A 106 THR ASP LYS LYS TRP ALA SER GLN TYR LEU LYS ILE MET
SEQRES 5 A 106 GLY LYS ILE LEU ASP GLN GLY GLU ASP PHE PRO ALA SER
SEQRES 6 A 106 GLU LEU ALA ARG ILE SER LYS LEU ILE GLU ASN LYS MET
SEQRES 7 A 106 SER GLU GLY LYS LYS GLU GLU LEU GLN ARG SER LEU ASN
SEQRES 8 A 106 ILE LEU THR ALA PHE ARG LYS LYS GLY ALA GLU LYS GLU
SEQRES 9 A 106 GLU LEU
HELIX 1 1 PRO A 159 ALA A 171 1 13
HELIX 2 2 SER A 173 LEU A 188 1 16
HELIX 3 3 ASP A 195 GLN A 212 1 18
HELIX 4 4 GLU A 214 ASN A 230 1 17
HELIX 5 5 LYS A 236 PHE A 250 1 15
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 - b 23 2 Bytes