Header list of 1rjt.pdb file
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HEADER CYTOKINE 20-NOV-03 1RJT TITLE NMR STRUCTURE OF CXC CHEMOKINE CXCL11/ITAC COMPND MOL_ID: 1; COMPND 2 MOLECULE: SMALL INDUCIBLE CYTOKINE B11; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CXCL11, INTERFERON-INDUCIBLE T-CELL ALPHA CHEMOATTRACTANT, COMPND 5 I-TAC, INTERFERON-GAMMA-INDUCIBLE PROTEIN-9, IP-9, H174, BETA-R1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: SYNTHESIZED WITH N15 ISOTOPE LABELS ON ALL LEUCINE SOURCE 4 AND VALINE RESIDUES. SEQUENCE IS NATURALLY FOUND IN HOMO SAPIENS SOURCE 5 (HUMAN). KEYWDS CHEMOKINE, CYTOKINE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR V.BOOTH,I.CLARK-LEWIS,B.D.SYKES REVDAT 4 02-MAR-22 1RJT 1 REMARK REVDAT 3 24-FEB-09 1RJT 1 VERSN REVDAT 2 10-AUG-04 1RJT 1 JRNL REVDAT 1 13-APR-04 1RJT 0 JRNL AUTH V.BOOTH,I.CLARK-LEWIS,B.D.SYKES JRNL TITL NMR STRUCTURE OF CXCR3 BINDING CHEMOKINE CXCL11 (ITAC). JRNL REF PROTEIN SCI. V. 13 2022 2004 JRNL REFN ISSN 0961-8368 JRNL PMID 15273303 JRNL DOI 10.1110/PS.04791404 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.2, CNS 1.2, ARIA 1.2 REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (CNS), NILGES (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1RJT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-03. REMARK 100 THE DEPOSITION ID IS D_1000020815. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 318; 303; 313 REMARK 210 PH : 4.5; 5.0; 5.0 REMARK 210 IONIC STRENGTH : 0; 0; 0 REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 2 MM CXCL11, PARTIAL N15 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N REMARK 210 -SEPARATED_NOESY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2 REMARK 210 REMARK 210 REMARK: ASSIGNMENTS WERE MADE FOR ALL THREE SAMPLE CONDITIONS. REMARK 210 STRUCTURE WAS CALCULATED USING DATA FROM ALL THREE CONDITIONS. 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 HB ILE A 43 HB2 ARG A 52 1.29 REMARK 500 HA LYS A 26 HG23 VAL A 68 1.34 REMARK 500 HB3 ALA A 27 HG12 ILE A 43 1.34 REMARK 500 H GLU A 25 O THR A 44 1.57 REMARK 500 HZ2 LYS A 46 OE1 GLU A 47 1.60 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 PHE A 4 99.89 61.36 REMARK 500 1 CYS A 9 58.83 -109.71 REMARK 500 1 PRO A 14 35.39 -84.66 REMARK 500 1 VAL A 16 -124.65 -123.49 REMARK 500 1 LYS A 17 110.35 -176.72 REMARK 500 1 ALA A 18 96.74 69.19 REMARK 500 1 VAL A 19 -155.69 -130.94 REMARK 500 1 LYS A 20 92.78 -69.10 REMARK 500 1 ALA A 22 -26.12 -179.95 REMARK 500 1 GLU A 25 72.50 68.71 REMARK 500 1 PRO A 32 21.83 -56.80 REMARK 500 1 SER A 33 14.46 56.01 REMARK 500 1 ASN A 35 8.72 -165.14 REMARK 500 1 ASN A 48 -55.34 -134.23 REMARK 500 1 ARG A 52 82.91 -150.16 REMARK 500 1 ASN A 55 -50.41 -156.64 REMARK 500 1 LYS A 57 -72.28 73.83 REMARK 500 1 GLN A 60 -11.59 66.13 REMARK 500 1 LYS A 71 -176.47 64.30 REMARK 500 2 LYS A 5 -76.06 -144.35 REMARK 500 2 CYS A 11 -75.60 -107.58 REMARK 500 2 ILE A 12 117.13 69.87 REMARK 500 2 PRO A 14 38.48 -81.24 REMARK 500 2 VAL A 16 -157.53 -114.21 REMARK 500 2 LYS A 17 95.34 -176.38 REMARK 500 2 ALA A 18 -154.80 -161.76 REMARK 500 2 VAL A 19 -164.72 50.49 REMARK 500 2 VAL A 21 39.21 -74.09 REMARK 500 2 ALA A 22 -41.90 -151.32 REMARK 500 2 GLU A 25 74.65 69.34 REMARK 500 2 MET A 30 75.98 -150.35 REMARK 500 2 PRO A 32 17.85 -55.90 REMARK 500 2 ASN A 35 15.23 -150.53 REMARK 500 2 GLU A 47 -81.03 -97.50 REMARK 500 2 LYS A 49 -163.02 -114.07 REMARK 500 2 LEU A 54 -83.14 -116.97 REMARK 500 2 LYS A 57 -69.88 -149.50 REMARK 500 3 ARG A 8 -54.66 -154.26 REMARK 500 3 VAL A 16 -141.50 60.09 REMARK 500 3 LYS A 17 -45.48 71.13 REMARK 500 3 ALA A 18 132.56 74.56 REMARK 500 3 VAL A 19 -143.65 -112.23 REMARK 500 3 LYS A 20 97.41 -69.98 REMARK 500 3 VAL A 21 66.46 -68.75 REMARK 500 3 ALA A 22 -34.32 -178.12 REMARK 500 3 GLU A 25 72.49 58.53 REMARK 500 3 LYS A 26 89.60 -151.50 REMARK 500 3 MET A 30 77.16 -150.54 REMARK 500 3 PRO A 32 35.63 -75.07 REMARK 500 3 SER A 33 7.12 59.74 REMARK 500 REMARK 500 THIS ENTRY HAS 179 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ILE A 24 GLU A 25 8 -146.00 REMARK 500 REMARK 500 REMARK: NULL DBREF 1RJT A 1 73 UNP O14625 SCYBB_HUMAN 22 94 SEQRES 1 A 73 PHE PRO MET PHE LYS ARG GLY ARG CYS LEU CYS ILE GLY SEQRES 2 A 73 PRO GLY VAL LYS ALA VAL LYS VAL ALA ASP ILE GLU LYS SEQRES 3 A 73 ALA SER ILE MET TYR PRO SER ASN ASN CYS ASP LYS ILE SEQRES 4 A 73 GLU VAL ILE ILE THR LEU LYS GLU ASN LYS GLY GLN ARG SEQRES 5 A 73 CYS LEU ASN PRO LYS SER LYS GLN ALA ARG LEU ILE ILE SEQRES 6 A 73 LYS LYS VAL GLU ARG LYS ASN PHE HELIX 1 1 GLN A 60 GLU A 69 1 10 SSBOND 1 CYS A 9 CYS A 36 1555 1555 2.02 SSBOND 2 CYS A 11 CYS A 53 1555 1555 2.03 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