Header list of 1qgp.pdb file
Complete list - v 3 2 Bytes
HEADER HYDROLASE 03-MAY-99 1QGP
TITLE NMR STRUCTURE OF THE Z-ALPHA DOMAIN OF ADAR1, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (DOUBLE STRANDED RNA ADENOSINE DEAMINASE);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: Z-ALPHA DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET28A;
SOURCE 8 OTHER_DETAILS: HHHHHH HISTIDINE TAG WAS ADDED AT THE N- TERMINUS FOR
SOURCE 9 EASE OF PURIFICATION
KEYWDS Z-ALPHA-Z-DNA BINDING DOMAIN, RNA-EDITING, Z-DNA RECOGNITION, ADAR1,
KEYWDS 2 HELIX- TURN-HELIX, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR M.SCHADE,C.J.TURNER,R.KUEHNE,P.SCHMIEDER,K.LOWENHAUPT,A.HERBERT,
AUTHOR 2 A.RICH,H.OSCHKINAT
REVDAT 4 03-NOV-21 1QGP 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1QGP 1 VERSN
REVDAT 2 01-APR-03 1QGP 1 JRNL
REVDAT 1 19-OCT-99 1QGP 0
JRNL AUTH M.SCHADE,C.J.TURNER,R.KUHNE,P.SCHMIEDER,K.LOWENHAUPT,
JRNL AUTH 2 A.HERBERT,A.RICH,H.OSCHKINAT
JRNL TITL THE SOLUTION STRUCTURE OF THE ZALPHA DOMAIN OF THE HUMAN RNA
JRNL TITL 2 EDITING ENZYME ADAR1 REVEALS A PREPOSITIONED BINDING SURFACE
JRNL TITL 3 FOR Z-DNA.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 96 12465 1999
JRNL REFN ISSN 0027-8424
JRNL PMID 10535945
JRNL DOI 10.1073/PNAS.96.22.12465
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QGP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000000988.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 0.137 M NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NA-PHOSPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY (1H; 13C; 15N); 15N TOCSY
REMARK 210 -HSQC; 2D TOCSY; HCCHTOCSY; HNCA;
REMARK 210 HN(CO)CA; HNCACB; HN(CO)CACB;
REMARK 210 HNCO; HN(CA)CO
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX750; DRX600; SELF-BUIL
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 SER A 125
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 O ILE A 172 H LEU A 176 1.56
REMARK 500 O GLU A 140 H LEU A 144 1.57
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 GLU A 132 -135.20 -64.27
REMARK 500 1 LEU A 133 -87.44 59.18
REMARK 500 1 GLU A 152 101.73 -58.04
REMARK 500 1 VAL A 199 91.72 -64.11
REMARK 500 2 GLU A 132 -133.94 -64.34
REMARK 500 2 LEU A 133 -88.87 59.81
REMARK 500 2 LYS A 154 96.21 -52.54
REMARK 500 3 GLN A 131 32.10 -91.93
REMARK 500 3 LEU A 133 -80.25 -112.70
REMARK 500 3 LEU A 150 -84.12 -54.34
REMARK 500 3 LYS A 154 89.87 -57.18
REMARK 500 4 GLN A 131 53.36 -96.51
REMARK 500 4 GLU A 132 42.38 -90.69
REMARK 500 4 SER A 134 -53.01 72.85
REMARK 500 4 LEU A 150 -81.66 -54.16
REMARK 500 4 LYS A 154 94.02 -53.48
REMARK 500 5 GLU A 132 81.86 -61.92
REMARK 500 5 LEU A 133 -84.05 -122.35
REMARK 500 5 LYS A 154 93.50 -53.84
REMARK 500 6 GLN A 131 40.84 -96.22
REMARK 500 6 GLU A 132 -144.53 -87.58
REMARK 500 6 LEU A 133 136.88 62.88
REMARK 500 6 SER A 134 -57.22 71.99
REMARK 500 6 LYS A 154 96.41 -52.43
REMARK 500 6 ALA A 155 171.68 -52.57
REMARK 500 7 GLU A 132 45.53 -108.19
REMARK 500 7 LEU A 133 -82.22 -108.72
REMARK 500 7 LYS A 154 93.91 -53.15
REMARK 500 7 ALA A 198 47.14 -88.09
REMARK 500 8 GLU A 132 -146.76 -108.32
REMARK 500 8 LEU A 133 135.05 60.53
REMARK 500 8 SER A 134 -56.23 71.53
REMARK 500 8 GLU A 152 91.34 -55.77
REMARK 500 8 VAL A 199 57.94 -90.14
REMARK 500 9 GLU A 132 66.99 -107.98
REMARK 500 9 LEU A 133 -82.49 -119.15
REMARK 500 9 GLU A 152 108.36 -52.11
REMARK 500 9 SER A 200 74.85 -119.04
REMARK 500 10 GLU A 132 49.82 -84.27
REMARK 500 10 LEU A 133 -79.16 -107.04
REMARK 500 10 LYS A 154 97.35 -49.57
REMARK 500 11 GLU A 132 -149.22 -108.04
REMARK 500 11 LEU A 133 -83.87 57.07
REMARK 500 11 LEU A 150 54.88 -94.11
REMARK 500 11 ALA A 155 -177.90 -53.38
REMARK 500 12 GLN A 131 49.33 -86.00
REMARK 500 12 LEU A 133 -83.15 -111.61
REMARK 500 12 LEU A 150 80.10 -64.25
REMARK 500 13 GLU A 132 -160.25 -108.08
REMARK 500 13 LEU A 133 133.49 63.30
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QGP A 125 201 UNP P55265 DSRAD_HUMAN 125 201
SEQADV 1QGP SER A 125 UNP P55265 CYS 125 ENGINEERED MUTATION
SEQADV 1QGP ASP A 201 UNP P55265 THR 201 CONFLICT
SEQRES 1 A 77 SER LEU SER SER HIS PHE GLN GLU LEU SER ILE TYR GLN
SEQRES 2 A 77 ASP GLN GLU GLN ARG ILE LEU LYS PHE LEU GLU GLU LEU
SEQRES 3 A 77 GLY GLU GLY LYS ALA THR THR ALA HIS ASP LEU SER GLY
SEQRES 4 A 77 LYS LEU GLY THR PRO LYS LYS GLU ILE ASN ARG VAL LEU
SEQRES 5 A 77 TYR SER LEU ALA LYS LYS GLY LYS LEU GLN LYS GLU ALA
SEQRES 6 A 77 GLY THR PRO PRO LEU TRP LYS ILE ALA VAL SER ASP
HELIX 1 1 TYR A 136 LEU A 150 1SEE REMARK 650 15
HELIX 2 2 ALA A 158 LEU A 165 1 8
HELIX 3 3 LYS A 169 LYS A 182 1 14
SHEET 1 S1 1 LYS A 154 THR A 157 0
SHEET 1 S2 1 LEU A 185 GLU A 188 0
SHEET 1 S3 1 LEU A 194 ILE A 197 0
CISPEP 1 THR A 191 PRO A 192 1 0.21
CISPEP 2 THR A 191 PRO A 192 2 0.24
CISPEP 3 THR A 191 PRO A 192 3 0.11
CISPEP 4 THR A 191 PRO A 192 4 0.06
CISPEP 5 THR A 191 PRO A 192 5 0.25
CISPEP 6 THR A 191 PRO A 192 6 0.13
CISPEP 7 THR A 191 PRO A 192 7 0.30
CISPEP 8 THR A 191 PRO A 192 8 0.16
CISPEP 9 THR A 191 PRO A 192 9 0.16
CISPEP 10 THR A 191 PRO A 192 10 0.17
CISPEP 11 THR A 191 PRO A 192 11 0.24
CISPEP 12 THR A 191 PRO A 192 12 0.14
CISPEP 13 THR A 191 PRO A 192 13 0.20
CISPEP 14 THR A 191 PRO A 192 14 0.09
CISPEP 15 THR A 191 PRO A 192 15 0.24
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 - v 3 2 Bytes