Header list of 1o6x.pdb file
Complete list - n 15 2 Bytes
HEADER HYDROLASE 17-OCT-02 1O6X TITLE NMR SOLUTION STRUCTURE OF THE ACTIVATION DOMAIN OF HUMAN TITLE 2 PROCARBOXYPEPTIDASE A2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROCARBOXYPEPTIDASE A2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ACTIVATION DOMAIN, RESIDUES 17-94; COMPND 5 EC: 3.4.17.15; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333; SOURCE 7 EXPRESSION_SYSTEM_VARIANT: XL-1-BLUE KEYWDS ACTIVATION DOMAIN, HYDROLASE, CARBOXYPEPTIDASE, METALLOPROTE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.A.JIMENEZ,V.VILLEGAS,J.SANTORO,L.SERRANO,J.VENDRELL,F.X.AVILES, AUTHOR 2 M.RICO REVDAT 4 15-JAN-20 1O6X 1 REMARK REVDAT 3 07-FEB-18 1O6X 1 SOURCE REVDAT 2 24-FEB-09 1O6X 1 VERSN REVDAT 1 30-JAN-03 1O6X 0 JRNL AUTH M.A.JIMENEZ,V.VILLEGAS,J.SANTORO,L.SERRANO,J.VENDRELL, JRNL AUTH 2 F.X.AVILES,M.RICO JRNL TITL NMR SOLUTION STRUCTURE OF THE ACTIVATION DOMAIN OF HUMAN JRNL TITL 2 PROCARBOXYPEPTIDASE A2 JRNL REF PROTEIN SCI. V. 12 296 2003 JRNL REFN ISSN 0961-8368 JRNL PMID 12538893 JRNL DOI 10.1110/PS.0227303 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA REMARK 3 AUTHORS : GUNTERT,WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE CHEMICAL SHIFTS FOR THIS ENTRY ARE REMARK 3 DEPOSITED AT BIOMAGRESBANK: ENTRY NUMBER 5561 REMARK 4 REMARK 4 1O6X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-OCT-02. REMARK 100 THE DEPOSITION ID IS D_1290011191. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D NOESY-15N-HSQC; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 3D NMR SPECTRA ON A 15N REMARK 210 -LABELED PROTEIN AND 2D SPECTRA ON NON-LABELED PROTEIN. NOESY REMARK 210 SPECTRA IN WATER AND IN D2O WERE USED. 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 SER A 3 149.15 -179.78 REMARK 500 1 PHE A 7 -175.84 -172.38 REMARK 500 1 GLN A 11 131.06 -172.20 REMARK 500 1 SER A 18 -39.21 -174.05 REMARK 500 1 GLN A 32 94.21 -48.73 REMARK 500 1 GLU A 33 88.61 -54.31 REMARK 500 1 HIS A 34 -56.14 -176.44 REMARK 500 1 SER A 42 99.25 -38.91 REMARK 500 1 TYR A 73 -169.86 -128.20 REMARK 500 1 GLU A 78 -141.71 -93.62 REMARK 500 2 ARG A 2 131.54 -179.35 REMARK 500 2 THR A 6 -169.72 -127.29 REMARK 500 2 VAL A 8 -80.99 -98.97 REMARK 500 2 ASP A 10 -175.90 -57.66 REMARK 500 2 SER A 18 -45.38 -152.89 REMARK 500 2 ASN A 19 -165.70 -107.86 REMARK 500 2 GLN A 32 85.41 -57.76 REMARK 500 2 GLU A 33 94.95 -57.14 REMARK 500 2 HIS A 34 -58.80 -175.62 REMARK 500 2 SER A 42 101.20 -41.47 REMARK 500 2 MET A 76 -67.33 -96.06 REMARK 500 2 GLU A 78 -144.19 -137.35 REMARK 500 2 VAL A 80 106.33 -40.47 REMARK 500 3 VAL A 8 -150.32 -127.35 REMARK 500 3 GLN A 11 136.89 -171.00 REMARK 500 3 SER A 18 -36.23 179.15 REMARK 500 3 GLN A 32 93.15 -51.13 REMARK 500 3 LEU A 35 -94.74 -83.64 REMARK 500 3 GLN A 36 69.89 81.45 REMARK 500 3 SER A 42 100.31 -40.12 REMARK 500 3 THR A 44 -30.09 -38.56 REMARK 500 3 PHE A 56 -31.50 -38.35 REMARK 500 3 GLN A 60 -70.06 -62.20 REMARK 500 3 GLU A 78 -144.22 -137.42 REMARK 500 4 ARG A 2 -175.88 172.18 REMARK 500 4 GLN A 11 130.07 -170.20 REMARK 500 4 SER A 18 -45.26 -152.33 REMARK 500 4 GLN A 32 104.39 -43.56 REMARK 500 4 LEU A 35 46.50 -97.41 REMARK 500 4 GLN A 36 64.61 -68.33 REMARK 500 4 SER A 42 100.55 -40.40 REMARK 500 4 PRO A 46 -166.27 -75.02 REMARK 500 4 TYR A 73 -169.70 -126.76 REMARK 500 4 GLU A 78 -142.23 -96.94 REMARK 500 4 VAL A 80 106.34 -40.46 REMARK 500 5 ARG A 2 75.87 171.31 REMARK 500 5 LEU A 4 -154.21 -133.05 REMARK 500 5 THR A 6 -169.42 -115.21 REMARK 500 5 VAL A 8 -150.35 -74.87 REMARK 500 5 ASP A 10 -176.15 -61.35 REMARK 500 REMARK 500 THIS ENTRY HAS 216 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AYE RELATED DB: PDB REMARK 900 HUMAN PROCARBOXYPEPTIDASE A2 REMARK 900 RELATED ID: 1DTD RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE LEECH CARBOXYPEPTIDASE REMARK 900 INHIBITOR AND THE HUMAN CARBOXYPEPTIDASE A2 (LCI-CPA2) REMARK 900 RELATED ID: 5561 RELATED DB: BMRB DBREF 1O6X A 1 3 PDB 1O6X 1O6X 1 3 DBREF 1O6X A 4 81 UNP P48052 CPB2_HUMAN 17 94 SEQRES 1 A 81 MET ARG SER LEU GLU THR PHE VAL GLY ASP GLN VAL LEU SEQRES 2 A 81 GLU ILE VAL PRO SER ASN GLU GLU GLN ILE LYS ASN LEU SEQRES 3 A 81 LEU GLN LEU GLU ALA GLN GLU HIS LEU GLN LEU ASP PHE SEQRES 4 A 81 TRP LYS SER PRO THR THR PRO GLY GLU THR ALA HIS VAL SEQRES 5 A 81 ARG VAL PRO PHE VAL ASN VAL GLN ALA VAL LYS VAL PHE SEQRES 6 A 81 LEU GLU SER GLN GLY ILE ALA TYR SER ILE MET ILE GLU SEQRES 7 A 81 ASP VAL GLN HELIX 1 1 ASN A 19 GLN A 32 1 14 HELIX 2 2 ASN A 58 GLN A 69 1 12 SHEET 1 AA 3 ALA A 50 PRO A 55 0 SHEET 2 AA 3 ASP A 10 ILE A 15 -1 O GLN A 11 N VAL A 54 SHEET 3 AA 3 TYR A 73 ILE A 75 -1 O SER A 74 N GLU A 14 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 - n 15 2 Bytes