Header list of 1h0t.pdb file
Complete list - n 17 2 Bytes
HEADER IMMUNE SYSTEM 27-JUN-02 1H0T
TITLE AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND COUPLED
TITLE 2 FOLDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGLOBULIN G BINDING PROTEIN A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 213-269;
COMPND 5 SYNONYM: IGG BINDING PROTEIN A;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ZSPA-1 AFFIBODY;
COMPND 9 CHAIN: B;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28A(+);
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 10 ORGANISM_TAXID: 32630;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS IMMUNE SYSTEM, PROTEIN-PROTEIN INTERACTIONS, PROTEIN ENGINEERING,
KEYWDS 2 MOLECULAR RECOGNITION, NMR SPECTROSCOPY, MOLTEN GLOBULE, INDUCED
KEYWDS 3 FIT, COUPLED PROTEIN FOLDING, AFFIBODY, IGG BINDING PROTEIN A
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR E.WAHLBERG,C.LENDEL,M.HELGSTRAND,P.ALLARD,V.DINCBAS-RENQVIST,
AUTHOR 2 A.HEDQVIST,H.BERGLUND,P.-A.NYGREN,T.HARD
REVDAT 6 17-JAN-18 1H0T 1 JRNL
REVDAT 5 21-DEC-16 1H0T 1 SOURCE REMARK VERSN
REVDAT 4 24-FEB-09 1H0T 1 VERSN
REVDAT 3 25-FEB-04 1H0T 1 ATOM
REVDAT 2 20-MAR-03 1H0T 1 JRNL
REVDAT 1 27-FEB-03 1H0T 0
JRNL AUTH E.WAHLBERG,C.LENDEL,M.HELGSTRAND,P.ALLARD,
JRNL AUTH 2 V.DINCBAS-RENQVIST,A.HEDQVIST,H.BERGLUND,P.-A.NYGREN,T.HARD
JRNL TITL AN AFFIBODY IN COMPLEX WITH A TARGET PROTEIN: STRUCTURE AND
JRNL TITL 2 COUPLED FOLDING
JRNL REF PROC.NATL.ACAD.SCI.USA V. 100 3185 2003
JRNL REFN ISSN 0027-8424
JRNL PMID 12594333
JRNL DOI 10.1073/PNAS.0436086100
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1H0T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1290009976.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 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 : XWIN-NMR, NMR-PIPE, ANSIG FOR
REMARK 210 WINDOWS WINDOWS, XPLOR
REMARK 210 METHOD USED : SIMULATED ANEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 40
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 GOOD RAMACHANDRAN PLOTS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED PROTEINS. ONE OF THE SUBUNITS
REMARK 210 WAS LABELED THE OTHER SUBUNIT WAS KEPT UNLABELED.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 2 LYS B 4 42.27 -158.40
REMARK 500 3 LYS A 4 -77.54 -100.16
REMARK 500 4 LYS A 4 -38.90 -156.08
REMARK 500 4 ASN B 3 71.02 -107.03
REMARK 500 4 THR B 18 42.48 -145.07
REMARK 500 6 PHE B 5 46.94 -93.00
REMARK 500 8 LYS A 4 -74.74 -94.29
REMARK 500 9 PHE B 5 43.83 -91.19
REMARK 500 10 ASN B 3 67.89 -104.80
REMARK 500 10 THR B 18 41.78 -144.50
REMARK 500 11 PHE B 5 31.69 -98.70
REMARK 500 13 ASP A 2 -56.68 -136.62
REMARK 500 14 THR B 18 33.77 -142.82
REMARK 500 15 ASN A 23 -166.13 51.68
REMARK 500 15 LYS B 4 47.18 -91.32
REMARK 500 16 PHE B 5 53.55 -97.30
REMARK 500 17 LYS B 4 -41.85 -149.06
REMARK 500 17 PHE B 5 98.38 -58.05
REMARK 500 18 LYS A 4 -79.27 -99.74
REMARK 500 18 PHE B 5 50.77 -104.59
REMARK 500 18 THR B 18 39.11 -140.36
REMARK 500 20 PHE B 5 38.96 -97.27
REMARK 500 20 THR B 18 37.67 -140.20
REMARK 500 21 ASN B 3 58.97 -105.69
REMARK 500 22 LYS A 4 -67.66 -164.97
REMARK 500 22 PHE B 5 30.47 -99.13
REMARK 500 22 THR B 18 38.42 -140.01
REMARK 500 24 ASN B 6 -43.65 -135.39
REMARK 500 25 ASN A 3 -67.30 -99.17
REMARK 500 25 LYS A 4 -46.36 -148.00
REMARK 500 26 LYS A 4 -46.52 -135.36
REMARK 500 26 ASN B 3 48.48 -100.35
REMARK 500 26 PHE B 5 36.92 -86.36
REMARK 500 28 PHE B 5 53.44 -100.80
REMARK 500 29 PHE A 5 -41.54 -141.56
REMARK 500 29 THR B 18 35.36 -141.04
REMARK 500 30 THR B 18 37.96 -145.06
REMARK 500 31 ASN B 3 59.78 -110.99
REMARK 500 32 LYS B 4 63.89 -103.32
REMARK 500 33 ASP A 2 -168.73 -120.14
REMARK 500 33 LYS A 4 -75.24 -80.29
REMARK 500 33 ASN B 3 49.62 -109.79
REMARK 500 33 LYS B 4 86.99 55.24
REMARK 500 33 PHE B 5 42.52 -85.85
REMARK 500 34 LYS A 4 -74.19 -77.18
REMARK 500 35 ASN A 3 -62.81 -92.96
REMARK 500 35 LYS A 4 -56.65 -151.78
REMARK 500 35 ASN B 3 89.14 57.59
REMARK 500 37 ASN A 23 -165.87 -115.52
REMARK 500 38 LYS A 4 -61.78 -144.12
REMARK 500
REMARK 500 THIS ENTRY HAS 52 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 27 0.21 SIDE CHAIN
REMARK 500 1 ARG B 14 0.30 SIDE CHAIN
REMARK 500 2 ARG A 27 0.12 SIDE CHAIN
REMARK 500 2 ARG B 14 0.31 SIDE CHAIN
REMARK 500 3 ARG A 27 0.27 SIDE CHAIN
REMARK 500 3 ARG B 14 0.32 SIDE CHAIN
REMARK 500 4 ARG A 27 0.26 SIDE CHAIN
REMARK 500 4 ARG B 14 0.30 SIDE CHAIN
REMARK 500 5 ARG A 27 0.27 SIDE CHAIN
REMARK 500 5 ARG B 14 0.31 SIDE CHAIN
REMARK 500 6 ARG A 27 0.31 SIDE CHAIN
REMARK 500 6 ARG B 14 0.32 SIDE CHAIN
REMARK 500 7 ARG A 27 0.20 SIDE CHAIN
REMARK 500 7 ARG B 14 0.32 SIDE CHAIN
REMARK 500 8 ARG A 27 0.25 SIDE CHAIN
REMARK 500 8 ARG B 14 0.31 SIDE CHAIN
REMARK 500 9 ARG A 27 0.22 SIDE CHAIN
REMARK 500 9 ARG B 14 0.31 SIDE CHAIN
REMARK 500 10 ARG A 27 0.27 SIDE CHAIN
REMARK 500 10 ARG B 14 0.31 SIDE CHAIN
REMARK 500 11 ARG A 27 0.21 SIDE CHAIN
REMARK 500 11 ARG B 14 0.31 SIDE CHAIN
REMARK 500 12 ARG A 27 0.17 SIDE CHAIN
REMARK 500 12 ARG B 14 0.16 SIDE CHAIN
REMARK 500 13 ARG A 27 0.13 SIDE CHAIN
REMARK 500 13 ARG B 14 0.31 SIDE CHAIN
REMARK 500 14 ARG A 27 0.21 SIDE CHAIN
REMARK 500 14 ARG B 14 0.31 SIDE CHAIN
REMARK 500 15 ARG A 27 0.21 SIDE CHAIN
REMARK 500 15 ARG B 14 0.29 SIDE CHAIN
REMARK 500 16 ARG A 27 0.20 SIDE CHAIN
REMARK 500 16 ARG B 14 0.31 SIDE CHAIN
REMARK 500 17 ARG A 27 0.10 SIDE CHAIN
REMARK 500 17 ARG B 14 0.32 SIDE CHAIN
REMARK 500 18 ARG A 27 0.15 SIDE CHAIN
REMARK 500 18 ARG B 14 0.31 SIDE CHAIN
REMARK 500 19 ARG A 27 0.25 SIDE CHAIN
REMARK 500 19 ARG B 14 0.32 SIDE CHAIN
REMARK 500 20 ARG A 27 0.21 SIDE CHAIN
REMARK 500 20 ARG B 14 0.30 SIDE CHAIN
REMARK 500 21 ARG A 27 0.23 SIDE CHAIN
REMARK 500 21 ARG B 14 0.31 SIDE CHAIN
REMARK 500 22 ARG A 27 0.23 SIDE CHAIN
REMARK 500 22 ARG B 14 0.31 SIDE CHAIN
REMARK 500 23 ARG A 27 0.22 SIDE CHAIN
REMARK 500 23 ARG B 14 0.31 SIDE CHAIN
REMARK 500 24 ARG B 14 0.31 SIDE CHAIN
REMARK 500 25 ARG A 27 0.22 SIDE CHAIN
REMARK 500 25 ARG B 14 0.31 SIDE CHAIN
REMARK 500 26 ARG A 27 0.20 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 79 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DEE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE AT 2.7A RESOLUTION OF A COMPLEX BETWEEN A
REMARK 900 STAPHYLOCOCCUS AUREUS DOMAIN AND A FAB FRAGMENT OF A HUMAN IGM
REMARK 900 ANTIBODY
DBREF 1H0T A 1 1 PDB 1H0T 1H0T 1 1
DBREF 1H0T A 2 58 UNP P02976 SPA1_STAAU 213 269
DBREF 1H0T B 1 58 PDB 1H0T 1H0T 1 58
SEQRES 1 A 58 VAL ASP ASN LYS PHE ASN LYS GLU GLN GLN ASN ALA PHE
SEQRES 2 A 58 TYR GLU ILE LEU HIS LEU PRO ASN LEU ASN GLU GLU GLN
SEQRES 3 A 58 ARG ASN ALA PHE ILE GLN SER LEU LYS ASP ASP PRO SER
SEQRES 4 A 58 GLN SER ALA ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN
SEQRES 5 A 58 ASP ALA GLN ALA PRO LYS
SEQRES 1 B 58 VAL ASP ASN LYS PHE ASN LYS GLU LEU SER VAL ALA GLY
SEQRES 2 B 58 ARG GLU ILE VAL THR LEU PRO ASN LEU ASN ASP PRO GLN
SEQRES 3 B 58 LYS LYS ALA PHE ILE PHE SER LEU TRP ASP ASP PRO SER
SEQRES 4 B 58 GLN SER ALA ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN
SEQRES 5 B 58 ASP ALA GLN ALA PRO LYS
HELIX 1 1 LYS A 4 HIS A 18 1 15
HELIX 2 2 GLU A 24 ASP A 36 1 13
HELIX 3 3 SER A 41 ALA A 54 1 14
HELIX 4 4 ASN B 6 THR B 18 1 13
HELIX 5 5 ASP B 24 ASP B 36 1 13
HELIX 6 6 PRO B 38 GLN B 40 5 3
HELIX 7 7 SER B 41 GLN B 55 1 15
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 17 2 Bytes