Header list of 1ppq.pdb file
Complete list - t 27 2 Bytes
HEADER IMMUNE SYSTEM 17-JUN-03 1PPQ TITLE NMR STRUCTURE OF 16TH MODULE OF IMMUNE ADHERENCE RECEPTOR, CR1 (CD35) COMPND MOL_ID: 1; COMPND 2 MOLECULE: COMPLEMENT RECEPTOR TYPE 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: MODULE 16, SUSHI C2; COMPND 5 SYNONYM: C3B/C4B RECEPTOR, CD35 ANTIGEN; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: MIDDLE MODULE OF SECOND COPY OF FUNCTIONAL SITE 2 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CR1 OR C3BR; SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922 KEYWDS COMPLEMENT, MODULE, CCP, SCR, SUSHI, IMMUNE SYSTEM EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.M.O'LEARY,K.BROMEK,G.M.BLACK,S.UHRINOVA,C.SCHMITZ,M.KRYCH, AUTHOR 2 J.P.ATKINSON,D.UHRIN,P.N.BARLOW REVDAT 3 27-OCT-21 1PPQ 1 REMARK SEQADV REVDAT 2 24-FEB-09 1PPQ 1 VERSN REVDAT 1 04-MAY-04 1PPQ 0 JRNL AUTH J.M.O'LEARY,K.BROMEK,G.M.BLACK,S.UHRINOVA,C.SCHMITZ,X.WANG, JRNL AUTH 2 M.KRYCH,J.P.ATKINSON,D.UHRIN,P.N.BARLOW JRNL TITL BACKBONE DYNAMICS OF COMPLEMENT CONTROL PROTEIN (CCP) JRNL TITL 2 MODULES REVEALS MOBILITY IN BINDING SURFACES. JRNL REF PROTEIN SCI. V. 13 1238 2004 JRNL REFN ISSN 0961-8368 JRNL PMID 15096630 JRNL DOI 10.1110/PS.03582704 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR, CNS 1.0 REMARK 3 AUTHORS : BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 6 ROUNDS, INCLUDING FILTERING AND REMARK 3 CHECKING REMARK 4 REMARK 4 1PPQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-03. REMARK 100 THE DEPOSITION ID IS D_1000019478. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 25 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1 MM CR1 MODULE 16 15N,13C; 25 REMARK 210 MM PHOSPHATE BUFFER; 90% H2O, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N HSQC; 2D NOESY; 2D TOCSY; 2D REMARK 210 RSCUBACOSY; 3D 15N HSQC-TOCSY; REMARK 210 3D 15N HSQC-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AZARA 2.6, ANSIG 3.3, CNS 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING AND REMARK 210 MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 60 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4 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 GLU A 959 -8.47 69.24 REMARK 500 1 ALA A 960 -177.87 59.81 REMARK 500 1 LYS A 961 115.64 62.11 REMARK 500 1 SER A 962 -8.99 -159.10 REMARK 500 1 THR A 978 -63.17 -142.53 REMARK 500 1 ILE A 980 32.20 -96.99 REMARK 500 1 CYS A1004 99.73 -63.32 REMARK 500 1 PRO A1017 107.40 -50.61 REMARK 500 1 ARG A1022 114.22 63.16 REMARK 500 2 LYS A 961 -163.93 -100.87 REMARK 500 2 SER A 962 82.46 61.25 REMARK 500 2 LYS A 964 -168.20 -72.64 REMARK 500 2 ILE A 977 -70.84 -60.25 REMARK 500 2 THR A 978 -91.39 -112.65 REMARK 500 2 HIS A 999 9.90 -150.17 REMARK 500 2 SER A1000 29.18 48.70 REMARK 500 2 PRO A1017 108.24 -48.21 REMARK 500 2 GLN A1021 99.37 -66.58 REMARK 500 3 ALA A 958 86.51 56.86 REMARK 500 3 SER A 962 -35.64 -153.40 REMARK 500 3 LYS A 964 71.68 -158.02 REMARK 500 3 THR A 965 -56.77 -122.04 REMARK 500 3 PRO A 966 106.96 -51.98 REMARK 500 3 THR A 978 -50.10 -157.00 REMARK 500 3 ILE A 980 34.79 -147.36 REMARK 500 3 THR A 992 -40.70 -136.03 REMARK 500 3 SER A1000 30.39 -83.96 REMARK 500 3 SER A1007 -49.84 -150.11 REMARK 500 3 SER A1014 30.97 -83.51 REMARK 500 3 ARG A1022 113.29 64.06 REMARK 500 4 ALA A 960 -178.58 60.59 REMARK 500 4 SER A 962 117.94 -168.35 REMARK 500 4 THR A 978 -70.30 -135.30 REMARK 500 4 THR A 991 -179.73 -59.12 REMARK 500 4 SER A1000 18.49 59.38 REMARK 500 4 ASN A1009 -8.44 -157.61 REMARK 500 4 PRO A1017 102.31 -39.78 REMARK 500 5 ALA A 958 16.71 -154.53 REMARK 500 5 GLU A 959 -36.18 -136.63 REMARK 500 5 LYS A 961 160.31 64.83 REMARK 500 5 SER A 962 90.56 60.82 REMARK 500 5 ASN A 971 74.43 50.23 REMARK 500 5 THR A 978 -68.08 -96.90 REMARK 500 5 THR A 992 -50.83 -134.44 REMARK 500 5 SER A1000 44.29 -76.56 REMARK 500 5 ASN A1009 13.53 -156.43 REMARK 500 5 PRO A1017 108.05 -49.65 REMARK 500 6 SER A 962 87.36 51.05 REMARK 500 6 ASN A 971 -29.46 73.29 REMARK 500 6 THR A 978 -59.14 -152.07 REMARK 500 REMARK 500 THIS ENTRY HAS 233 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1GKG RELATED DB: PDB REMARK 900 MODULE 16 AND 17 PAIR REMARK 900 RELATED ID: 1GKN RELATED DB: PDB REMARK 900 MODULE 15 AND 16 PAIR DBREF 1PPQ A 961 1024 UNP P17927 CR1_HUMAN 1002 1065 SEQADV 1PPQ GLU A 957 UNP P17927 CLONING ARTIFACT SEQADV 1PPQ ALA A 958 UNP P17927 CLONING ARTIFACT SEQADV 1PPQ GLU A 959 UNP P17927 CLONING ARTIFACT SEQADV 1PPQ ALA A 960 UNP P17927 CLONING ARTIFACT SEQADV 1PPQ THR A 987 UNP P17927 ASN 1028 ENGINEERED MUTATION SEQRES 1 A 68 GLU ALA GLU ALA LYS SER CYS LYS THR PRO PRO ASP PRO SEQRES 2 A 68 VAL ASN GLY MET VAL HIS VAL ILE THR ASP ILE GLN VAL SEQRES 3 A 68 GLY SER ARG ILE THR TYR SER CYS THR THR GLY HIS ARG SEQRES 4 A 68 LEU ILE GLY HIS SER SER ALA GLU CYS ILE LEU SER GLY SEQRES 5 A 68 ASN THR ALA HIS TRP SER THR LYS PRO PRO ILE CYS GLN SEQRES 6 A 68 ARG ILE PRO SHEET 1 A 2 GLY A 972 HIS A 975 0 SHEET 2 A 2 THR A 987 CYS A 990 -1 O THR A 987 N HIS A 975 SHEET 1 B 2 CYS A1004 LEU A1006 0 SHEET 2 B 2 ALA A1011 TRP A1013 -1 O HIS A1012 N ILE A1005 SSBOND 1 CYS A 963 CYS A 1004 1555 1555 2.03 SSBOND 2 CYS A 990 CYS A 1020 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 - t 27 2 Bytes