Header list of 1xmw.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 04-OCT-04 1XMW TITLE CD3 EPSILON AND DELTA ECTODOMAIN FRAGMENT COMPLEX IN SINGLE-CHAIN TITLE 2 CONSTRUCT COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHIMERIC CD3 MOUSE EPSILON AND SHEEP DELTA ECTODOMAIN COMPND 3 FRAGMENT COMPLEX; COMPND 4 CHAIN: A; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, OVIS ARIES; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE, SHEEP; SOURCE 4 ORGANISM_TAXID: 10090,9940; SOURCE 5 STRAIN: ,; SOURCE 6 GENE: CD3E, CD3D; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: B834(DE3); SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-11A KEYWDS BETA-SHEET, C1-SET IMMUNOGLOBULIN SUPERFAMILY, H-BONDED G STRAND KEYWDS 2 PAIR, SINGLE-CHAIN, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR Z.-Y.J.SUN,S.T.KIM,I.C.KIM,A.FAHMY,E.L.REINHERZ,G.WAGNER REVDAT 3 02-MAR-22 1XMW 1 REMARK REVDAT 2 24-FEB-09 1XMW 1 VERSN REVDAT 1 30-NOV-04 1XMW 0 JRNL AUTH Z.Y.SUN,S.T.KIM,I.C.KIM,A.FAHMY,E.L.REINHERZ,G.WAGNER JRNL TITL SOLUTION STRUCTURE OF THE CD3EPSILONDELTA ECTODOMAIN AND JRNL TITL 2 COMPARISON WITH CD3EPSILONGAMMA AS A BASIS FOR MODELING T JRNL TITL 3 CELL RECEPTOR TOPOLOGY AND SIGNALING. JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 16867 2004 JRNL REFN ISSN 0027-8424 JRNL PMID 15557001 JRNL DOI 10.1073/PNAS.0407576101 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROSA 3.7, CYANA 1.0.4, X-PLOR 3.851 REMARK 3 AUTHORS : GUNTERT (PROSA), GUNTERT (CYANA), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XMW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-04. REMARK 100 THE DEPOSITION ID IS D_1000030530. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 17MM NAPO4, 50MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5MM, U-15N,13C,2D; 0.5MM REMARK 210 UNLABELED; 0.5MM, U-15N,13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HN(CO)CA; HN(CA)CB; REMARK 210 HN(COCA)CB; HNCO; HN(CA)CO; 15N- REMARK 210 NOESY; TOCSY; 13C-NOESY; 2D REMARK 210 NOESY; CCONH; HCCONH REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.13 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 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 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 TYR A 72 H GLN A 173 1.60 REMARK 500 H THR A 132 O GLN A 162 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 GLU A 4 92.56 52.57 REMARK 500 1 PRO A 22 35.05 -67.39 REMARK 500 1 LEU A 29 109.13 -59.95 REMARK 500 1 GLN A 40 -62.55 -131.76 REMARK 500 1 HIS A 42 44.52 -91.07 REMARK 500 1 ASN A 70 97.56 -64.84 REMARK 500 1 ASP A 83 -166.79 52.39 REMARK 500 1 ALA A 85 -66.50 -156.46 REMARK 500 1 LYS A 86 -158.84 -69.88 REMARK 500 1 LYS A 91 70.56 -113.58 REMARK 500 1 LYS A 92 -65.46 -92.87 REMARK 500 1 ASP A 93 74.12 52.01 REMARK 500 1 LYS A 102 43.81 -156.74 REMARK 500 1 SER A 105 -159.84 52.39 REMARK 500 1 LYS A 109 -75.29 -142.95 REMARK 500 1 LYS A 111 32.20 -165.09 REMARK 500 1 ARG A 112 -162.89 -78.70 REMARK 500 1 ALA A 113 -81.44 -52.75 REMARK 500 1 SER A 129 -148.94 -173.24 REMARK 500 1 GLN A 135 -174.89 -175.02 REMARK 500 1 THR A 137 95.32 -54.52 REMARK 500 1 ALA A 138 65.25 -101.83 REMARK 500 1 ASP A 144 95.11 -177.75 REMARK 500 1 LYS A 146 -43.43 -160.19 REMARK 500 1 ASN A 166 -74.34 -171.43 REMARK 500 1 LYS A 168 117.71 -174.83 REMARK 500 1 ARG A 177 85.19 49.65 REMARK 500 2 ASN A 5 19.38 -154.99 REMARK 500 2 LEU A 23 33.81 -155.62 REMARK 500 2 ASP A 24 179.63 52.83 REMARK 500 2 LYS A 41 77.25 52.07 REMARK 500 2 HIS A 42 40.56 -95.17 REMARK 500 2 ASN A 68 175.45 -50.36 REMARK 500 2 SER A 81 -66.16 -167.42 REMARK 500 2 ALA A 82 -47.57 -143.07 REMARK 500 2 ASP A 83 46.68 -140.00 REMARK 500 2 LYS A 92 88.30 52.68 REMARK 500 2 ASP A 94 80.51 -165.68 REMARK 500 2 ASP A 98 -158.67 -160.98 REMARK 500 2 LYS A 102 32.37 -98.41 REMARK 500 2 LYS A 111 -159.08 -155.47 REMARK 500 2 SER A 129 -160.67 179.53 REMARK 500 2 GLN A 135 -167.06 -176.72 REMARK 500 2 THR A 137 95.53 -54.67 REMARK 500 2 ALA A 138 64.08 -102.73 REMARK 500 2 ASP A 144 111.53 72.77 REMARK 500 2 LYS A 146 -55.92 -159.27 REMARK 500 2 LYS A 168 117.24 -173.99 REMARK 500 3 ALA A 3 -49.61 -139.18 REMARK 500 3 PRO A 22 38.63 -67.73 REMARK 500 REMARK 500 THIS ENTRY HAS 386 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 78 0.24 SIDE CHAIN REMARK 500 1 ARG A 112 0.22 SIDE CHAIN REMARK 500 1 ARG A 153 0.28 SIDE CHAIN REMARK 500 1 ARG A 158 0.22 SIDE CHAIN REMARK 500 1 ARG A 177 0.30 SIDE CHAIN REMARK 500 2 ARG A 78 0.25 SIDE CHAIN REMARK 500 2 ARG A 112 0.21 SIDE CHAIN REMARK 500 2 ARG A 153 0.30 SIDE CHAIN REMARK 500 2 ARG A 158 0.21 SIDE CHAIN REMARK 500 2 ARG A 177 0.24 SIDE CHAIN REMARK 500 3 ARG A 78 0.28 SIDE CHAIN REMARK 500 3 ARG A 112 0.28 SIDE CHAIN REMARK 500 3 ARG A 153 0.24 SIDE CHAIN REMARK 500 3 ARG A 158 0.29 SIDE CHAIN REMARK 500 3 ARG A 177 0.30 SIDE CHAIN REMARK 500 4 ARG A 78 0.25 SIDE CHAIN REMARK 500 4 ARG A 112 0.32 SIDE CHAIN REMARK 500 4 ARG A 153 0.23 SIDE CHAIN REMARK 500 4 ARG A 158 0.32 SIDE CHAIN REMARK 500 4 ARG A 177 0.27 SIDE CHAIN REMARK 500 5 ARG A 78 0.24 SIDE CHAIN REMARK 500 5 ARG A 112 0.23 SIDE CHAIN REMARK 500 5 ARG A 153 0.23 SIDE CHAIN REMARK 500 5 ARG A 158 0.26 SIDE CHAIN REMARK 500 5 ARG A 177 0.24 SIDE CHAIN REMARK 500 6 ARG A 78 0.24 SIDE CHAIN REMARK 500 6 ARG A 112 0.31 SIDE CHAIN REMARK 500 6 ARG A 153 0.32 SIDE CHAIN REMARK 500 6 ARG A 158 0.30 SIDE CHAIN REMARK 500 6 ARG A 177 0.23 SIDE CHAIN REMARK 500 7 ARG A 78 0.32 SIDE CHAIN REMARK 500 7 ARG A 112 0.26 SIDE CHAIN REMARK 500 7 ARG A 153 0.29 SIDE CHAIN REMARK 500 7 ARG A 158 0.32 SIDE CHAIN REMARK 500 7 ARG A 177 0.22 SIDE CHAIN REMARK 500 8 ARG A 78 0.23 SIDE CHAIN REMARK 500 8 ARG A 112 0.25 SIDE CHAIN REMARK 500 8 ARG A 153 0.26 SIDE CHAIN REMARK 500 8 ARG A 158 0.26 SIDE CHAIN REMARK 500 8 ARG A 177 0.32 SIDE CHAIN REMARK 500 9 ARG A 78 0.31 SIDE CHAIN REMARK 500 9 ARG A 112 0.23 SIDE CHAIN REMARK 500 9 ARG A 153 0.31 SIDE CHAIN REMARK 500 9 ARG A 158 0.23 SIDE CHAIN REMARK 500 9 ARG A 177 0.27 SIDE CHAIN REMARK 500 10 ARG A 78 0.29 SIDE CHAIN REMARK 500 10 ARG A 112 0.30 SIDE CHAIN REMARK 500 10 ARG A 153 0.18 SIDE CHAIN REMARK 500 10 ARG A 158 0.21 SIDE CHAIN REMARK 500 10 ARG A 177 0.25 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 75 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 CD3 EPSILON AND DELTA ECTODOMAIN FRAGMENT COMPLEX IN REMARK 999 SINGLE-CHAIN CONSTRUCT WITH THE LINKER SEQUENCE REMARK 999 GSADDAKKDA AKKDDAKKDD AKKDGSQTNK AK (RESIDUE 80-112) DBREF 1XMW A 1 79 UNP P22646 CD3E_MOUSE 22 100 DBREF 1XMW A 113 178 UNP P18438 CD3D_SHEEP 23 88 SEQRES 1 A 178 ASP ASP ALA GLU ASN ILE GLU TYR LYS VAL SER ILE SER SEQRES 2 A 178 GLY THR SER VAL GLU LEU THR CYS PRO LEU ASP SER ASP SEQRES 3 A 178 GLU ASN LEU LYS TRP GLU LYS ASN GLY GLN GLU LEU PRO SEQRES 4 A 178 GLN LYS HIS ASP LYS HIS LEU VAL LEU GLN ASP PHE SER SEQRES 5 A 178 GLU VAL GLU ASP SER GLY TYR TYR VAL CYS TYR THR PRO SEQRES 6 A 178 ALA SER ASN LYS ASN THR TYR LEU TYR LEU LYS ALA ARG SEQRES 7 A 178 VAL GLY SER ALA ASP ASP ALA LYS LYS ASP ALA ALA LYS SEQRES 8 A 178 LYS ASP ASP ALA LYS LYS ASP ASP ALA LYS LYS ASP GLY SEQRES 9 A 178 SER GLN THR ASN LYS ALA LYS ARG ALA LEU GLU VAL LEU SEQRES 10 A 178 GLU ALA GLU ASP LYS VAL ILE LEU LYS CYS ASN SER SER SEQRES 11 A 178 ILE THR LEU LEU GLN GLY THR ALA GLY GLN GLU VAL SER SEQRES 12 A 178 ASP ASN LYS THR LEU ASN LEU GLY LYS ARG ILE GLU ASP SEQRES 13 A 178 PRO ARG GLY MET TYR GLN CYS GLY GLU ASN ALA LYS SER SEQRES 14 A 178 PHE THR LEU GLN VAL TYR TYR ARG MET HELIX 1 1 SER A 52 SER A 57 1 6 SHEET 1 A 3 LYS A 9 SER A 13 0 SHEET 2 A 3 SER A 16 THR A 20 -1 O THR A 20 N LYS A 9 SHEET 3 A 3 HIS A 45 LEU A 48 -1 O LEU A 46 N LEU A 19 SHEET 1 B 6 LYS A 30 LYS A 33 0 SHEET 2 B 6 GLY A 58 TYR A 63 -1 O TYR A 63 N LYS A 30 SHEET 3 B 6 THR A 71 LYS A 76 -1 O LEU A 75 N GLY A 58 SHEET 4 B 6 THR A 171 TYR A 176 1 O GLN A 173 N TYR A 72 SHEET 5 B 6 ARG A 158 GLN A 162 -1 N GLY A 159 O VAL A 174 SHEET 6 B 6 THR A 132 GLY A 136 -1 N THR A 132 O GLN A 162 SHEET 1 C 2 GLU A 115 ALA A 119 0 SHEET 2 C 2 LYS A 122 LYS A 126 -1 O LYS A 126 N GLU A 115 SSBOND 1 CYS A 21 CYS A 62 1555 1555 2.02 SSBOND 2 CYS A 127 CYS A 163 1555 1555 2.02 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