Header list of 1tm6.pdb file
Complete list - 2 20 Bytes
HEADER PROTEIN TRANSPORT 10-JUN-04 1TM6
TITLE NMR STRUCTURE OF THE FREE ZINC BINDING C-TERMINAL DOMAIN OF SECA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PREPROTEIN TRANSLOCASE SECA SUBUNIT;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS ZINC FINGER, BETA HAIRPIN, SECA, PROTEIN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.M.MATOUSEK,A.T.ALEXANDRESCU
REVDAT 4 02-MAR-22 1TM6 1 REMARK LINK
REVDAT 3 24-FEB-09 1TM6 1 VERSN
REVDAT 2 20-DEC-05 1TM6 1 JRNL
REVDAT 1 12-OCT-04 1TM6 0
JRNL AUTH W.M.MATOUSEK,A.T.ALEXANDRESCU
JRNL TITL NMR STRUCTURE OF THE C-TERMINAL DOMAIN OF SECA IN THE FREE
JRNL TITL 2 STATE
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1702 163 2004
JRNL REFN ISSN 0006-3002
JRNL PMID 15488768
JRNL DOI 10.1016/J.BBAPAP.2004.08.012
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2000, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TM6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022764.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298
REMARK 210 PH : 7.40; 6.03; 6.14; 6.43
REMARK 210 IONIC STRENGTH : 2.7MM ZNCL; 10MM PO4 BUFFER;
REMARK 210 2.7MM ZNCL; 10MM PO4 BUFFER;
REMARK 210 1.6MM ZNCL; 10MM PO4 BUFFER;
REMARK 210 2.7MM ZNCL; 10MM PO4 BUFFER
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 2.5MM PROTEIN, 2.7MM ZNCL, 10MM
REMARK 210 PO4 BUFFER; 1.4MM PROTEIN, 1.6MM
REMARK 210 ZNCL, 10MM PO4 BUFFER; 2.5MM
REMARK 210 PROTEIN, 2.7MM ZNCL, 10MM PO4
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; NATURAL
REMARK 210 ABUNDANCE N-HSQC; NATURAL
REMARK 210 ABUNDANCE C-HSQC; HYDROGEN
REMARK 210 EXCHANGE; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : STANDARD X-PLOR PROTOCOL; 1.
REMARK 210 DISTANCE GEOMETRY SUB-EMBED 2.
REMARK 210 DISTANCE GEOMETRY FULL EMBED 3.
REMARK 210 SIMULATED ANNEALING 4. SIMULATED
REMARK 210 ANNEALING REFINE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY,TARGET
REMARK 210 FUNCTION
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 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 GLY A 11 H LYS A 13 1.53
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 ASP A 4 68.74 -110.81
REMARK 500 1 PRO A 5 -107.02 -61.49
REMARK 500 1 CYS A 6 -149.10 33.53
REMARK 500 1 SER A 10 -126.61 -167.08
REMARK 500 1 LYS A 12 -58.37 65.17
REMARK 500 1 LYS A 13 -72.45 -31.94
REMARK 500 1 CYS A 17 -65.60 -95.89
REMARK 500 2 ASP A 4 58.95 -115.36
REMARK 500 2 PRO A 5 -109.38 -63.27
REMARK 500 2 CYS A 6 -144.25 30.78
REMARK 500 2 SER A 10 -135.40 -170.43
REMARK 500 2 LYS A 12 -64.09 67.48
REMARK 500 2 LYS A 13 -32.50 -33.66
REMARK 500 2 CYS A 17 -63.89 -98.36
REMARK 500 3 ARG A 2 -164.46 42.96
REMARK 500 3 ASP A 4 57.33 -113.67
REMARK 500 3 PRO A 5 -111.57 -63.58
REMARK 500 3 CYS A 6 -149.29 33.12
REMARK 500 3 SER A 10 -138.43 -172.73
REMARK 500 3 LYS A 12 -35.01 -157.85
REMARK 500 3 LYS A 13 -73.39 -39.99
REMARK 500 3 CYS A 17 -69.73 -95.83
REMARK 500 3 ARG A 20 -35.18 -148.10
REMARK 500 3 LEU A 21 84.64 57.56
REMARK 500 4 ARG A 2 25.26 174.89
REMARK 500 4 ASN A 3 37.10 -96.16
REMARK 500 4 ASP A 4 64.71 -108.58
REMARK 500 4 PRO A 5 -109.41 -60.72
REMARK 500 4 CYS A 6 -151.39 35.19
REMARK 500 4 SER A 10 -134.24 -164.93
REMARK 500 4 CYS A 17 -68.79 -104.67
REMARK 500 4 ARG A 20 -94.82 -51.80
REMARK 500 4 LEU A 21 97.73 -47.97
REMARK 500 5 ASP A 4 70.32 -116.18
REMARK 500 5 PRO A 5 -109.28 -60.75
REMARK 500 5 CYS A 6 -150.89 34.48
REMARK 500 5 SER A 10 -124.69 -176.20
REMARK 500 5 LYS A 12 -70.70 78.38
REMARK 500 5 LYS A 13 -60.30 -18.29
REMARK 500 5 CYS A 17 -67.14 -97.16
REMARK 500 5 ARG A 20 -94.22 -64.83
REMARK 500 5 LEU A 21 52.63 -158.30
REMARK 500 6 ARG A 2 -102.13 -88.31
REMARK 500 6 ASP A 4 68.05 -109.39
REMARK 500 6 PRO A 5 -111.18 -60.76
REMARK 500 6 CYS A 6 -149.46 34.46
REMARK 500 6 SER A 10 -127.05 -174.98
REMARK 500 6 LYS A 12 -59.41 64.89
REMARK 500 6 LYS A 13 -67.54 -28.20
REMARK 500 6 CYS A 17 -63.97 -104.35
REMARK 500
REMARK 500 THIS ENTRY HAS 172 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 1 ARG A 2 0.28 SIDE CHAIN
REMARK 500 2 ARG A 2 0.25 SIDE CHAIN
REMARK 500 2 ARG A 20 0.28 SIDE CHAIN
REMARK 500 3 ARG A 2 0.20 SIDE CHAIN
REMARK 500 3 ARG A 20 0.21 SIDE CHAIN
REMARK 500 4 ARG A 2 0.27 SIDE CHAIN
REMARK 500 4 ARG A 20 0.24 SIDE CHAIN
REMARK 500 5 ARG A 2 0.30 SIDE CHAIN
REMARK 500 5 ARG A 20 0.22 SIDE CHAIN
REMARK 500 6 ARG A 20 0.32 SIDE CHAIN
REMARK 500 7 ARG A 2 0.22 SIDE CHAIN
REMARK 500 7 ARG A 20 0.31 SIDE CHAIN
REMARK 500 8 ARG A 2 0.27 SIDE CHAIN
REMARK 500 8 ARG A 20 0.20 SIDE CHAIN
REMARK 500 9 ARG A 2 0.18 SIDE CHAIN
REMARK 500 9 ARG A 20 0.30 SIDE CHAIN
REMARK 500 10 ARG A 2 0.29 SIDE CHAIN
REMARK 500 10 ARG A 20 0.32 SIDE CHAIN
REMARK 500 11 ARG A 2 0.31 SIDE CHAIN
REMARK 500 11 ARG A 20 0.32 SIDE CHAIN
REMARK 500 12 ARG A 2 0.20 SIDE CHAIN
REMARK 500 12 ARG A 20 0.28 SIDE CHAIN
REMARK 500 13 ARG A 2 0.29 SIDE CHAIN
REMARK 500 13 ARG A 20 0.26 SIDE CHAIN
REMARK 500 14 ARG A 2 0.24 SIDE CHAIN
REMARK 500 14 ARG A 20 0.20 SIDE CHAIN
REMARK 500 15 ARG A 2 0.24 SIDE CHAIN
REMARK 500 15 ARG A 20 0.27 SIDE CHAIN
REMARK 500 16 ARG A 2 0.26 SIDE CHAIN
REMARK 500 16 ARG A 20 0.16 SIDE CHAIN
REMARK 500 17 ARG A 2 0.30 SIDE CHAIN
REMARK 500 17 ARG A 20 0.31 SIDE CHAIN
REMARK 500 18 ARG A 2 0.21 SIDE CHAIN
REMARK 500 18 ARG A 20 0.19 SIDE CHAIN
REMARK 500 19 ARG A 20 0.31 SIDE CHAIN
REMARK 500 20 ARG A 2 0.25 SIDE CHAIN
REMARK 500 20 ARG A 20 0.31 SIDE CHAIN
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 ZN A 23B ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 6 SG
REMARK 620 2 CYS A 8 SG 85.1
REMARK 620 3 CYS A 17 SG 161.1 106.1
REMARK 620 4 HIS A 18 ND1 89.5 174.5 79.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 23B
DBREF 1TM6 A 1 22 UNP P10408 SECA_ECOLI 880 901
SEQRES 1 A 22 GLY ARG ASN ASP PRO CYS PRO CYS GLY SER GLY LYS LYS
SEQRES 2 A 22 TYR LYS GLN CYS HIS GLY ARG LEU GLN
HET ZN A 23B 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 LYS A 12 HIS A 18 1 7
LINK SG CYS A 6 ZN ZN A 23B 1555 1555 2.35
LINK SG CYS A 8 ZN ZN A 23B 1555 1555 2.30
LINK SG CYS A 17 ZN ZN A 23B 1555 1555 2.39
LINK ND1 HIS A 18 ZN ZN A 23B 1555 1555 2.42
SITE 1 AC1 5 CYS A 6 PRO A 7 CYS A 8 CYS A 17
SITE 2 AC1 5 HIS A 18
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 - 2 20 Bytes