Header list of 1xwe.pdb file
Complete list - v 10 2 Bytes
HEADER SIGNALING PROTEIN 30-OCT-04 1XWE
TITLE NMR STRUCTURE OF C345C (NTR) DOMAIN OF C5 OF COMPLEMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COMPLEMENT C5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C345C DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: C5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS OB FIOLD, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR J.BRAMHAM,C.-T.THAI,D.C.SOARES,D.UHRIN,R.T.OGATA,P.N.BARLOW
REVDAT 4 10-NOV-21 1XWE 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1XWE 1 VERSN
REVDAT 2 22-MAR-05 1XWE 1 JRNL
REVDAT 1 21-DEC-04 1XWE 0
JRNL AUTH J.BRAMHAM,C.-T.THAI,D.C.SOARES,D.UHRIN,R.T.OGATA,P.N.BARLOW
JRNL TITL FUNCTIONAL INSIGHTS FROM THE STRUCTURE OF THE
JRNL TITL 2 MULTIFUNCTIONAL C345C DOMAIN OF C5 OF COMPLEMENT
JRNL REF J.BIOL.CHEM. V. 280 10636 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15598652
JRNL DOI 10.1074/JBC.M413126200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XWE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030843.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 20MM NA PHOSPAHTE; 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5-1.0MM C5-C345C; U-15N,13C;
REMARK 210 20MM NA PHOSPHATE BUFFER; 100MM
REMARK 210 NACL; 5UM EDTA; PH 6
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA 2.6, ANSIG 3.3, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEAILING, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LOWEST NOE
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 13
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
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 CYS A1514 -145.33 39.88
REMARK 500 1 THR A1524 -28.57 -175.39
REMARK 500 1 GLU A1553 -161.74 -116.24
REMARK 500 1 VAL A1555 -51.62 -132.67
REMARK 500 1 VAL A1573 80.64 38.19
REMARK 500 1 ASP A1577 80.98 61.08
REMARK 500 1 SER A1578 -166.68 -114.84
REMARK 500 1 ASN A1590 -11.02 -145.11
REMARK 500 1 ILE A1609 -14.11 -141.88
REMARK 500 1 LYS A1610 124.67 -38.67
REMARK 500 1 TYR A1611 -34.76 -133.60
REMARK 500 1 ASN A1612 -53.01 -151.81
REMARK 500 1 ALA A1613 -37.05 -170.52
REMARK 500 1 ARG A1616 -108.18 -175.65
REMARK 500 1 TYR A1617 -52.22 -134.71
REMARK 500 1 ILE A1618 94.43 32.74
REMARK 500 1 LEU A1621 92.70 54.96
REMARK 500 1 THR A1625 93.78 -59.35
REMARK 500 1 TRP A1626 103.85 -59.18
REMARK 500 1 PRO A1631 104.53 -46.80
REMARK 500 1 CYS A1636 -32.96 -145.63
REMARK 500 1 SER A1638 17.41 59.15
REMARK 500 1 CYS A1639 -73.64 -103.72
REMARK 500 1 GLN A1640 80.78 49.11
REMARK 500 1 ALA A1641 -48.28 -143.63
REMARK 500 1 LEU A1655 -71.54 -91.92
REMARK 500 1 ASN A1656 -74.76 -54.27
REMARK 500 2 SER A1509 99.59 59.15
REMARK 500 2 ALA A1512 -77.92 -169.86
REMARK 500 2 ASP A1513 -73.38 -138.84
REMARK 500 2 CYS A1514 95.88 51.23
REMARK 500 2 LEU A1521 97.75 59.49
REMARK 500 2 ASP A1522 89.16 -160.73
REMARK 500 2 LEU A1523 101.21 -56.36
REMARK 500 2 THR A1524 -26.43 -173.44
REMARK 500 2 GLU A1553 -75.92 -100.10
REMARK 500 2 ASN A1554 -51.63 -145.11
REMARK 500 2 VAL A1555 -54.39 -124.26
REMARK 500 2 ALA A1572 -157.88 -86.44
REMARK 500 2 VAL A1573 42.74 -84.15
REMARK 500 2 THR A1589 11.34 -148.51
REMARK 500 2 LYS A1595 108.78 -45.97
REMARK 500 2 GLU A1605 178.85 -59.95
REMARK 500 2 LEU A1607 -168.28 -123.14
REMARK 500 2 GLN A1608 85.10 -172.48
REMARK 500 2 TYR A1611 -33.71 -147.42
REMARK 500 2 ALA A1613 -76.27 66.10
REMARK 500 2 THR A1634 12.64 -142.48
REMARK 500 2 CYS A1639 -155.80 -80.41
REMARK 500 2 ASP A1652 -73.47 -50.99
REMARK 500
REMARK 500 THIS ENTRY HAS 900 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XWE A 1512 1658 UNP P01031 CO5_HUMAN 1530 1676
SEQADV 1XWE GLY A 1508 UNP P01031 CLONING ARTIFACT
SEQADV 1XWE SER A 1509 UNP P01031 CLONING ARTIFACT
SEQADV 1XWE HIS A 1510 UNP P01031 CLONING ARTIFACT
SEQADV 1XWE MET A 1511 UNP P01031 CLONING ARTIFACT
SEQADV 1XWE ALA A 1613 UNP P01031 PHE 1631 ENGINEERED MUTATION
SEQRES 1 A 151 GLY SER HIS MET ALA ASP CYS GLY GLN MET GLN GLU GLU
SEQRES 2 A 151 LEU ASP LEU THR ILE SER ALA GLU THR ARG LYS GLN THR
SEQRES 3 A 151 ALA CYS LYS PRO GLU ILE ALA TYR ALA TYR LYS VAL SER
SEQRES 4 A 151 ILE THR SER ILE THR VAL GLU ASN VAL PHE VAL LYS TYR
SEQRES 5 A 151 LYS ALA THR LEU LEU ASP ILE TYR LYS THR GLY GLU ALA
SEQRES 6 A 151 VAL ALA GLU LYS ASP SER GLU ILE THR PHE ILE LYS LYS
SEQRES 7 A 151 VAL THR CYS THR ASN ALA GLU LEU VAL LYS GLY ARG GLN
SEQRES 8 A 151 TYR LEU ILE MET GLY LYS GLU ALA LEU GLN ILE LYS TYR
SEQRES 9 A 151 ASN ALA SER PHE ARG TYR ILE TYR PRO LEU ASP SER LEU
SEQRES 10 A 151 THR TRP ILE GLU TYR TRP PRO ARG ASP THR THR CYS SER
SEQRES 11 A 151 SER CYS GLN ALA PHE LEU ALA ASN LEU ASP GLU PHE ALA
SEQRES 12 A 151 GLU ASP ILE PHE LEU ASN GLY CYS
HELIX 1 1 PHE A 1642 ASN A 1656 1 15
SHEET 1 A 5 GLU A1579 LYS A1585 0
SHEET 2 A 5 PHE A1556 LYS A1568 -1 N VAL A1557 O LYS A1584
SHEET 3 A 5 TYR A1541 VAL A1552 -1 N SER A1546 O THR A1562
SHEET 4 A 5 GLN A1598 GLY A1603 -1 O GLY A1603 N TYR A1541
SHEET 5 A 5 TRP A1626 TRP A1630 -1 O GLU A1628 N LEU A1600
SSBOND 1 CYS A 1514 CYS A 1588 1555 1555 2.03
SSBOND 2 CYS A 1535 CYS A 1658 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 - v 10 2 Bytes