Header list of 1itm.pdb file
Complete list - 23 20 Bytes
HEADER CYTOKINE 28-FEB-94 1ITM TITLE ANALYSIS OF THE SOLUTION STRUCTURE OF HUMAN INTERLEUKIN 4 DETERMINED TITLE 2 BY HETERONUCLEAR THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE TITLE 3 TECHNIQUES COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERLEUKIN-4; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606 KEYWDS CYTOKINE EXPDTA SOLUTION NMR AUTHOR C.REDFIELD,L.J.SMITH,J.BOYD,G.M.P.LAWRENCE,R.G.EDWARDS,C.J.GERSHATER, AUTHOR 2 R.A.G.SMITH,C.M.DOBSON REVDAT 3 23-FEB-22 1ITM 1 REMARK REVDAT 2 24-FEB-09 1ITM 1 VERSN REVDAT 1 31-MAY-94 1ITM 0 JRNL AUTH C.REDFIELD,L.J.SMITH,J.BOYD,G.M.LAWRENCE,R.G.EDWARDS, JRNL AUTH 2 C.J.GERSHATER,R.A.SMITH,C.M.DOBSON JRNL TITL ANALYSIS OF THE SOLUTION STRUCTURE OF HUMAN INTERLEUKIN-4 JRNL TITL 2 DETERMINED BY HETERONUCLEAR THREE-DIMENSIONAL NUCLEAR JRNL TITL 3 MAGNETIC RESONANCE TECHNIQUES. JRNL REF J.MOL.BIOL. V. 238 23 1994 JRNL REFN ISSN 0022-2836 JRNL PMID 8145254 JRNL DOI 10.1006/JMBI.1994.1265 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.J.SMITH,C.REDFIELD,J.BOYD,G.M.P.LAWRENCE,R.G.EDWARDS, REMARK 1 AUTH 2 R.A.G.SMITH,C.M.DOBSON REMARK 1 TITL HUMAN INTERLEUKIN 4: THE SOLUTION STRUCTURE OF A REMARK 1 TITL 2 FOUR-HELIX-BUNDLE PROTEIN REMARK 1 REF J.MOL.BIOL. V. 224 899 1992 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.REDFIELD,L.J.SMITH,J.BOYD,G.M.P.LAWRENCE,R.G.EDWARDS, REMARK 1 AUTH 2 R.A.G.SMITH,C.M.DOBSON REMARK 1 TITL SECONDARY STRUCTURE AND TOPOLOGY OF HUMAN INTERLEUKIN 4 IN REMARK 1 TITL 2 SOLUTION REMARK 1 REF BIOCHEMISTRY V. 30 11029 1991 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1ITM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000174263. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 HG1 THR A 39 H THR A 40 1.31 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 CYS A 3 N - CA - C ANGL. DEV. = 21.6 DEGREES REMARK 500 TRP A 91 CG - CD1 - NE1 ANGL. DEV. = -7.4 DEGREES REMARK 500 TRP A 91 CD1 - NE1 - CE2 ANGL. DEV. = 8.2 DEGREES REMARK 500 TRP A 91 NE1 - CE2 - CZ2 ANGL. DEV. = 7.9 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 LEU A 7 -70.82 -49.37 REMARK 500 THR A 22 -152.22 -132.19 REMARK 500 THR A 28 114.71 -18.77 REMARK 500 ALA A 35 10.35 -149.03 REMARK 500 LYS A 37 -61.58 -16.90 REMARK 500 THR A 39 -166.38 -126.00 REMARK 500 GLU A 60 -47.96 -25.09 REMARK 500 THR A 63 52.52 24.87 REMARK 500 THR A 69 -90.30 -158.42 REMARK 500 ALA A 70 -51.25 -149.42 REMARK 500 LEU A 96 -127.34 -128.67 REMARK 500 ASN A 97 -59.51 -148.78 REMARK 500 PRO A 100 -179.82 -69.69 REMARK 500 LYS A 102 64.29 -111.37 REMARK 500 GLU A 103 144.94 -21.15 REMARK 500 ALA A 104 -77.87 -112.87 REMARK 500 LEU A 109 -61.15 3.49 REMARK 500 LYS A 123 2.19 -69.57 REMARK 500 LYS A 126 46.14 -95.72 REMARK 500 CYS A 127 -36.59 -136.13 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 ARG A 47 0.32 SIDE CHAIN REMARK 500 ARG A 53 0.24 SIDE CHAIN REMARK 500 ARG A 64 0.24 SIDE CHAIN REMARK 500 ARG A 75 0.29 SIDE CHAIN REMARK 500 ARG A 81 0.30 SIDE CHAIN REMARK 500 ARG A 85 0.19 SIDE CHAIN REMARK 500 ARG A 88 0.21 SIDE CHAIN REMARK 500 ARG A 115 0.29 SIDE CHAIN REMARK 500 ARG A 121 0.29 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1ITM A 1 129 UNP P05112 IL4_HUMAN 25 153 SEQRES 1 A 130 MET HIS LYS CYS ASP ILE THR LEU GLN GLU ILE ILE LYS SEQRES 2 A 130 THR LEU ASN SER LEU THR GLU GLN LYS THR LEU CYS THR SEQRES 3 A 130 GLU LEU THR VAL THR ASP ILE PHE ALA ALA SER LYS ASN SEQRES 4 A 130 THR THR GLU LYS GLU THR PHE CYS ARG ALA ALA THR VAL SEQRES 5 A 130 LEU ARG GLN PHE TYR SER HIS HIS GLU LYS ASP THR ARG SEQRES 6 A 130 CYS LEU GLY ALA THR ALA GLN GLN PHE HIS ARG HIS LYS SEQRES 7 A 130 GLN LEU ILE ARG PHE LEU LYS ARG LEU ASP ARG ASN LEU SEQRES 8 A 130 TRP GLY LEU ALA GLY LEU ASN SER CYS PRO VAL LYS GLU SEQRES 9 A 130 ALA ASN GLN SER THR LEU GLU ASN PHE LEU GLU ARG LEU SEQRES 10 A 130 LYS THR ILE MET ARG GLU LYS TYR SER LYS CYS SER SER HELIX 1 H1 ILE A 5 GLU A 19 1 15 HELIX 2 H2 GLU A 41 HIS A 59 1 19 HELIX 3 H3 GLN A 71 ALA A 94 1 24 HELIX 4 H4 GLU A 110 SER A 125 1 16 SHEET 1 S1 2 VAL A 29 ASP A 31 0 SHEET 2 S1 2 ASN A 105 THR A 108 -1 SSBOND 1 CYS A 3 CYS A 127 1555 1555 2.02 SSBOND 2 CYS A 24 CYS A 65 1555 1555 2.02 SSBOND 3 CYS A 46 CYS A 99 1555 1555 2.02 CISPEP 1 HIS A 1 LYS A 2 0 0.21 CISPEP 2 LYS A 2 CYS A 3 0 -0.09 CISPEP 3 CYS A 127 SER A 128 0 0.12 CISPEP 4 SER A 128 SER A 129 0 0.00 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
Complete list - 23 20 Bytes