Header list of 1qlk.pdb file
Complete list - r 2 2 Bytes
HEADER CALCIUM-BINDING 26-SEP-97 1QLK
TITLE SOLUTION STRUCTURE OF CA(2+)-LOADED RAT S100B (BETABETA) NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-100 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SUBUNITS A AND B;
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 GENE: S100BETA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HMS174 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11B
KEYWDS S100BETA, S100B, EF-HAND, S100 PROTEIN, CALCIUM-BINDING PROTEIN,
KEYWDS 2 FOUR-HELIX BUNDLE, CALCIUM-BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.C.DROHAT,D.M.BALDISSERI,R.R.RUSTANDI,D.J.WEBER
REVDAT 3 02-MAR-22 1QLK 1 REMARK LINK
REVDAT 2 24-FEB-09 1QLK 1 VERSN
REVDAT 1 11-NOV-98 1QLK 0
JRNL AUTH A.C.DROHAT,D.M.BALDISSERI,R.R.RUSTANDI,D.J.WEBER
JRNL TITL SOLUTION STRUCTURE OF CALCIUM-BOUND RAT S100B(BETABETA) AS
JRNL TITL 2 DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY,.
JRNL REF BIOCHEMISTRY V. 37 2729 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9485423
JRNL DOI 10.1021/BI972635P
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.C.DROHAT,J.C.AMBURGEY,F.ABILDGAARD,M.R.STARICH,
REMARK 1 AUTH 2 D.BALDISSERI,D.J.WEBER
REMARK 1 TITL SOLUTION STRUCTURE OF RAT APO-S100B(BETA BETA) AS DETERMINED
REMARK 1 TITL 2 BY NMR SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 35 11577 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.C.AMBURGEY,F.ABILDGAARD,M.R.STARICH,S.SHAH,D.C.HILT,
REMARK 1 AUTH 2 D.J.WEBER
REMARK 1 TITL 1H, 13C AND 15N NMR ASSIGNMENTS AND SOLUTION SECONDARY
REMARK 1 TITL 2 STRUCTURE OF RAT APO-S100 BETA
REMARK 1 REF J.BIOMOL.NMR V. 6 171 1995
REMARK 1 REFN ISSN 0925-2738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QLK 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_1000175919.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 22MM
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE MAIN REFERENCE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600.13 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR V3.851(ONLINE)
REMARK 210 V3.851(ONLINE)
REMARK 210 METHOD USED : SEE MAIN REFERENCE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : SEE MAIN REFERENCE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: PLEASE SEE MAIN REFERENCE FOR DETAILS
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
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 ASN A 38 -75.76 -48.93
REMARK 500 1 GLU A 39 19.70 -163.04
REMARK 500 1 LYS A 48 -61.07 -159.00
REMARK 500 1 PHE A 87 17.44 -67.47
REMARK 500 1 GLU A 89 -99.15 -48.73
REMARK 500 1 ASN B 38 -75.60 -49.07
REMARK 500 1 GLU B 39 19.95 -163.38
REMARK 500 1 LYS B 48 -60.66 -159.01
REMARK 500 1 PHE B 87 16.94 -67.19
REMARK 500 1 GLU B 89 -100.17 -49.05
REMARK 500 2 ASN A 37 -72.30 -58.16
REMARK 500 2 GLU A 39 -77.36 -89.91
REMARK 500 2 SER A 41 18.02 -145.24
REMARK 500 2 LEU A 44 -75.34 -89.99
REMARK 500 2 ASN B 37 -72.05 -58.62
REMARK 500 2 GLU B 39 -77.39 -89.69
REMARK 500 2 SER B 41 17.82 -145.78
REMARK 500 2 LEU B 44 -74.61 -90.31
REMARK 500 3 LYS A 24 -37.94 -153.47
REMARK 500 3 HIS A 25 75.40 -159.80
REMARK 500 3 GLU A 39 -79.69 -91.91
REMARK 500 3 SER A 41 -54.16 -148.20
REMARK 500 3 GLU A 46 142.70 -179.31
REMARK 500 3 LYS A 48 -23.22 -161.53
REMARK 500 3 PHE A 88 -89.93 -109.97
REMARK 500 3 LYS B 24 -38.82 -154.24
REMARK 500 3 HIS B 25 75.65 -159.41
REMARK 500 3 GLU B 39 -79.75 -91.79
REMARK 500 3 SER B 41 -53.63 -147.99
REMARK 500 3 GLU B 46 142.77 -179.09
REMARK 500 3 LYS B 48 -23.45 -161.22
REMARK 500 3 PHE B 88 -90.02 -110.09
REMARK 500 4 LYS A 24 -125.49 -160.11
REMARK 500 4 GLU A 39 -14.85 -154.58
REMARK 500 4 GLU A 45 10.55 -150.91
REMARK 500 4 LYS A 48 -53.49 -136.35
REMARK 500 4 PHE A 88 -80.05 -90.03
REMARK 500 4 GLU A 89 -73.37 -114.65
REMARK 500 4 LYS B 24 -125.19 -160.18
REMARK 500 4 GLU B 39 -14.97 -154.71
REMARK 500 4 GLU B 45 10.78 -150.95
REMARK 500 4 LYS B 48 -53.70 -135.89
REMARK 500 4 PHE B 88 -80.02 -89.95
REMARK 500 4 GLU B 89 -72.24 -114.90
REMARK 500 5 GLU A 21 114.40 -164.97
REMARK 500 5 GLU A 39 22.57 -149.54
REMARK 500 5 LEU A 44 -71.85 -93.86
REMARK 500 5 LYS A 48 -39.57 -153.56
REMARK 500 5 PHE A 87 104.73 45.26
REMARK 500 5 GLU B 21 114.44 -164.58
REMARK 500
REMARK 500 THIS ENTRY HAS 247 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 92 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 18 O
REMARK 620 2 ASP A 23 O 57.3
REMARK 620 3 LYS A 26 O 133.4 83.8
REMARK 620 4 GLU A 31 OE1 115.0 161.0 109.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 93 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 63 OD1
REMARK 620 2 ASP A 65 OD1 81.4
REMARK 620 3 GLU A 67 O 120.3 53.3
REMARK 620 4 GLU A 72 OE2 68.1 98.5 81.3
REMARK 620 5 GLU A 72 OE1 118.9 126.5 75.3 56.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 92 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 18 O
REMARK 620 2 ASP B 23 O 60.2
REMARK 620 3 LYS B 26 O 145.3 91.2
REMARK 620 4 GLU B 31 OE1 108.3 152.2 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 93 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 63 OD1
REMARK 620 2 ASP B 65 OD1 86.5
REMARK 620 3 GLU B 67 O 124.3 54.9
REMARK 620 4 GLU B 72 OE2 68.7 101.9 80.9
REMARK 620 5 GLU B 72 OE1 115.1 125.8 73.0 51.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 93
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 93
DBREF 1QLK A 1 91 UNP P04631 S100B_RAT 1 91
DBREF 1QLK B 1 91 UNP P04631 S100B_RAT 1 91
SEQRES 1 A 92 MET SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP
SEQRES 2 A 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS
SEQRES 3 A 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN
SEQRES 4 A 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU
SEQRES 5 A 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP GLU ASP GLY
SEQRES 6 A 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 A 92 SER MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS
SEQRES 8 A 92 GLU
SEQRES 1 B 92 MET SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP
SEQRES 2 B 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS
SEQRES 3 B 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN
SEQRES 4 B 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU
SEQRES 5 B 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP GLU ASP GLY
SEQRES 6 B 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 B 92 SER MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS
SEQRES 8 B 92 GLU
HET CA A 92 1
HET CA A 93 1
HET CA B 92 1
HET CA B 93 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
HELIX 1 1 GLU A 2 ARG A 20 1 19
HELIX 2 2 LYS A 29 HIS A 42 1 14
HELIX 3 3 GLN A 50 LEU A 60 1 11
HELIX 4 4 PHE A 70 ALA A 83 1 14
HELIX 5 5 GLU B 2 ARG B 20 1 19
HELIX 6 6 LYS B 29 HIS B 42 1 14
HELIX 7 7 GLN B 50 LEU B 60 1 11
HELIX 8 8 PHE B 70 ALA B 83 1 14
LINK O SER A 18 CA CA A 92 1555 1555 2.97
LINK O ASP A 23 CA CA A 92 1555 1555 2.73
LINK O LYS A 26 CA CA A 92 1555 1555 2.90
LINK OE1 GLU A 31 CA CA A 92 1555 1555 2.61
LINK OD1 ASP A 63 CA CA A 93 1555 1555 2.98
LINK OD1 ASP A 65 CA CA A 93 1555 1555 2.28
LINK O GLU A 67 CA CA A 93 1555 1555 2.92
LINK OE2 GLU A 72 CA CA A 93 1555 1555 2.07
LINK OE1 GLU A 72 CA CA A 93 1555 1555 2.46
LINK O SER B 18 CA CA B 92 1555 1555 2.90
LINK O ASP B 23 CA CA B 92 1555 1555 2.52
LINK O LYS B 26 CA CA B 92 1555 1555 2.75
LINK OE1 GLU B 31 CA CA B 92 1555 1555 2.91
LINK OD1 ASP B 63 CA CA B 93 1555 1555 2.90
LINK OD1 ASP B 65 CA CA B 93 1555 1555 2.08
LINK O GLU B 67 CA CA B 93 1555 1555 2.89
LINK OE2 GLU B 72 CA CA B 93 1555 1555 2.16
LINK OE1 GLU B 72 CA CA B 93 1555 1555 2.66
SITE 1 AC1 5 TYR A 17 SER A 18 GLU A 21 LYS A 24
SITE 2 AC1 5 HIS A 25
SITE 1 AC2 4 ASP A 61 GLU A 62 ASP A 63 ASP A 65
SITE 1 AC3 5 PHE B 14 SER B 18 ASP B 23 LYS B 26
SITE 2 AC3 5 LEU B 27
SITE 1 AC4 6 ASP B 61 GLU B 62 ASP B 63 ASP B 65
SITE 2 AC4 6 GLU B 67 CYS B 68
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 - r 2 2 Bytes