Header list of 1fcl.pdb file
Complete list - v 3 2 Bytes
HEADER PROTEIN BINDING 18-JUL-00 1FCL TITLE DELTA1.5: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF TITLE 2 STREPTOCOCCAL PROTEIN G COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN G BINDING PROTEIN G; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: GB1_DELTA1.5; COMPND 5 SYNONYM: IGG BINDING PROTEIN G; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP.; SOURCE 3 ORGANISM_TAXID: 1306; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS DESIGNED CORE MUTANT, STREPTOCOCCAL PROTEIN G, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 40 AUTHOR S.A.ROSS,C.A.SARISKY,A.SU,S.L.MAYO REVDAT 3 03-NOV-21 1FCL 1 REMARK SEQADV REVDAT 2 24-FEB-09 1FCL 1 VERSN REVDAT 1 19-SEP-01 1FCL 0 JRNL AUTH S.A.ROSS,C.A.SARISKY,A.SU,S.L.MAYO JRNL TITL DESIGNED PROTEIN G CORE VARIANTS FOLD TO NATIVE-LIKE JRNL TITL 2 STRUCTURES: SEQUENCE SELECTION BY ORBIT TOLERATES VARIATION JRNL TITL 3 IN BACKBONE SPECIFICATION. JRNL REF PROTEIN SCI. V. 10 450 2001 JRNL REFN ISSN 0961-8368 JRNL PMID 11266631 JRNL DOI 10.1110/PS.32501 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 5.2F, 5.3A, 6.1B, X-PLOR 3.1 REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1FCL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-00. REMARK 100 THE DEPOSITION ID IS D_1000011479. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE REMARK 210 PRESSURE : ATMOSPHERIC ATM REMARK 210 SAMPLE CONTENTS : 1 MM UNLABELED PROTEIN IN 50 MM REMARK 210 SODIUM PHOSPHATE, PH 6.0 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; E-COSY; REMARK 210 TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRCOMPASS 2.5, ANSIG 3.3 REMARK 210 METHOD USED : STANDARD DISTANCE REMARK 210 GEOMETRY/SIMULATED ANNEALING REMARK 210 METHODS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NONE 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 ASN A 8 52.09 -109.63 REMARK 500 1 ILE A 39 73.11 -115.60 REMARK 500 1 ALA A 48 -72.48 -56.78 REMARK 500 1 VAL A 54 88.15 -171.62 REMARK 500 2 ASN A 8 53.30 -113.79 REMARK 500 2 ALA A 48 -72.38 -56.76 REMARK 500 2 VAL A 54 88.24 -172.47 REMARK 500 3 ASN A 8 52.93 -110.85 REMARK 500 3 ILE A 39 69.38 -111.91 REMARK 500 3 ALA A 48 -70.14 -54.34 REMARK 500 3 VAL A 54 90.15 -172.45 REMARK 500 4 ASN A 8 54.28 -110.39 REMARK 500 4 THR A 11 -43.70 -134.37 REMARK 500 4 ILE A 39 73.20 -115.92 REMARK 500 4 ALA A 48 -70.91 -55.09 REMARK 500 4 VAL A 54 86.95 -170.57 REMARK 500 5 ASN A 8 50.91 -110.64 REMARK 500 5 ILE A 39 68.50 -115.46 REMARK 500 5 ALA A 48 -71.30 -56.94 REMARK 500 5 VAL A 54 87.62 -171.38 REMARK 500 6 ASN A 8 51.35 -110.05 REMARK 500 6 ALA A 48 -71.36 -56.11 REMARK 500 6 VAL A 54 74.26 -177.00 REMARK 500 7 ASN A 8 53.09 -109.98 REMARK 500 7 ILE A 39 73.07 -113.66 REMARK 500 7 ALA A 48 -73.50 -56.88 REMARK 500 7 VAL A 54 87.37 -171.99 REMARK 500 8 ASN A 8 51.60 -107.30 REMARK 500 8 ILE A 39 72.51 -114.47 REMARK 500 8 ALA A 48 -72.15 -58.95 REMARK 500 8 VAL A 54 78.34 -171.48 REMARK 500 9 ASN A 8 51.77 -100.57 REMARK 500 9 ILE A 39 74.19 -113.42 REMARK 500 9 ALA A 48 -70.10 -54.75 REMARK 500 9 VAL A 54 78.97 -170.86 REMARK 500 10 ASN A 8 51.66 -107.31 REMARK 500 10 ILE A 39 67.69 -116.94 REMARK 500 10 ALA A 48 -73.09 -57.48 REMARK 500 10 VAL A 54 80.31 -171.93 REMARK 500 11 ASN A 8 53.41 -109.25 REMARK 500 11 ILE A 39 70.93 -115.68 REMARK 500 11 ALA A 48 -72.63 -58.84 REMARK 500 11 VAL A 54 91.29 -170.60 REMARK 500 12 ASN A 8 52.82 -116.18 REMARK 500 12 ILE A 39 73.99 -117.22 REMARK 500 12 ALA A 48 -71.00 -56.62 REMARK 500 12 VAL A 54 83.87 -170.31 REMARK 500 13 ASN A 8 53.10 -116.33 REMARK 500 13 ALA A 48 -72.01 -56.69 REMARK 500 13 VAL A 54 83.60 -170.28 REMARK 500 REMARK 500 THIS ENTRY HAS 157 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FD6 RELATED DB: PDB REMARK 900 DELTA0: A COMPUTATIONALLY DESIGNED CORE VARIANT OF THE B1 DOMAIN OF REMARK 900 STREPTOCOCCAL PROTEIN G REMARK 900 RELATED ID: 1GB1 RELATED DB: PDB REMARK 900 PROTEIN G (B1 DOMAIN) REMARK 900 RELATED ID: 1GB4 RELATED DB: PDB REMARK 900 HYPERTHERMOPHILIC VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL REMARK 900 PROTEIN G DBREF 1FCL A 1 56 UNP P19909 SPG2_STRSG 302 357 SEQADV 1FCL THR A 1 UNP P19909 ASP 302 ENGINEERED MUTATION SEQADV 1FCL PHE A 3 UNP P19909 TYR 304 ENGINEERED MUTATION SEQADV 1FCL ILE A 7 UNP P19909 VAL 308 ENGINEERED MUTATION SEQADV 1FCL LEU A 30 UNP P19909 PHE 331 ENGINEERED MUTATION SEQADV 1FCL ILE A 34 UNP P19909 ALA 335 ENGINEERED MUTATION SEQADV 1FCL ILE A 39 UNP P19909 VAL 340 ENGINEERED MUTATION SEQADV 1FCL TRP A 52 UNP P19909 PHE 353 ENGINEERED MUTATION SEQRES 1 A 56 THR THR PHE LYS LEU ILE ILE ASN GLY LYS THR LEU LYS SEQRES 2 A 56 GLY GLU THR THR THR GLU ALA VAL ASP ALA ALA THR ALA SEQRES 3 A 56 GLU LYS VAL LEU LYS GLN TYR ILE ASN ASP ASN GLY ILE SEQRES 4 A 56 ASP GLY GLU TRP THR TYR ASP ASP ALA THR LYS THR TRP SEQRES 5 A 56 THR VAL THR GLU HELIX 1 1 ASP A 22 GLY A 38 1 17 SHEET 1 A 3 LYS A 13 THR A 18 0 SHEET 2 A 3 PHE A 3 ASN A 8 -1 N PHE A 3 O THR A 18 SHEET 3 A 3 THR A 53 THR A 55 1 O VAL A 54 N ASN A 8 CRYST1 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 3 2 Bytes