Header list of 2b89.pdb file
Complete list - g 9 2 Bytes
HEADER PROTEIN BINDING 06-OCT-05 2B89
TITLE STRUCTURAL BASIS FOR MOLECULAR RECOGNITION IN AN AFFIBODY:AFFIBODY
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTI-ZTAQ AFFIBODY;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS PROTEIN-PROTEIN INTERACTIONS, PROTEIN ENGINEERING, MOLECULAR
KEYWDS 2 RECOGNITION, NMR SPECTROSCOPY, INDUCED FIT, AFFIBODY, PROTEIN
KEYWDS 3 BINDING
EXPDTA SOLUTION NMR
NUMMDL 40
AUTHOR C.LENDEL,J.DOGAN,T.HARD
REVDAT 5 14-JUN-23 2B89 1 REMARK
REVDAT 4 26-FEB-20 2B89 1 REMARK
REVDAT 3 24-FEB-09 2B89 1 VERSN
REVDAT 2 04-JUL-06 2B89 1 JRNL
REVDAT 1 23-MAY-06 2B89 0
JRNL AUTH C.LENDEL,J.DOGAN,T.HARD
JRNL TITL STRUCTURAL BASIS FOR MOLECULAR RECOGNITION IN AN
JRNL TITL 2 AFFIBODY:AFFIBODY COMPLEX.
JRNL REF J.MOL.BIOL. V. 359 1293 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16750222
JRNL DOI 10.1016/J.JMB.2006.04.043
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, X-PLOR
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2B89 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034798.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM [U-13C; U-15N] ANTI-ZTAQ;
REMARK 210 1.5MM [U-13C; U-15N] ANTI-ZTAQ
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 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 : NMRPIPE, ANSIG, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
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, GOOD
REMARK 210 RAMACHANDRAN PLOTS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 O LEU A 45 H LYS A 49 1.43
REMARK 500 O ARG A 9 H ILE A 13 1.52
REMARK 500 O LEU A 44 H ALA A 48 1.56
REMARK 500 O ALA A 48 H ASN A 52 1.57
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 ASP A 2 -54.50 -161.40
REMARK 500 1 LEU A 19 104.99 -45.67
REMARK 500 1 LEU A 22 150.40 -39.91
REMARK 500 1 ASP A 37 93.65 -172.63
REMARK 500 2 ASP A 2 -162.88 -78.67
REMARK 500 2 LEU A 19 108.86 -48.08
REMARK 500 2 ASP A 37 95.34 -173.68
REMARK 500 2 PRO A 57 95.05 -38.18
REMARK 500 3 LEU A 19 109.11 -49.75
REMARK 500 3 ASN A 21 -65.87 -92.24
REMARK 500 3 LEU A 22 145.93 -33.74
REMARK 500 3 ASP A 37 95.43 -171.84
REMARK 500 3 ALA A 56 50.18 37.70
REMARK 500 3 PRO A 57 110.59 -31.45
REMARK 500 4 LEU A 19 109.23 -48.96
REMARK 500 4 ASN A 21 -64.77 -92.07
REMARK 500 4 LEU A 22 148.67 -34.70
REMARK 500 4 ASP A 37 96.06 -172.79
REMARK 500 4 ALA A 56 51.37 37.58
REMARK 500 4 PRO A 57 98.41 -31.63
REMARK 500 5 LEU A 19 106.97 -45.31
REMARK 500 5 ASN A 21 -64.47 -92.41
REMARK 500 5 LEU A 22 148.31 -37.10
REMARK 500 5 ASP A 37 94.75 -171.94
REMARK 500 5 PRO A 57 123.56 -31.96
REMARK 500 6 LEU A 19 104.16 -43.59
REMARK 500 6 LEU A 22 151.43 -42.25
REMARK 500 6 ASP A 37 97.39 -169.60
REMARK 500 7 LEU A 19 106.32 -47.34
REMARK 500 7 ASN A 21 -63.44 -92.16
REMARK 500 7 LEU A 22 148.44 -38.08
REMARK 500 7 ASP A 37 97.87 -172.69
REMARK 500 7 PRO A 57 108.83 -31.69
REMARK 500 8 LEU A 19 106.49 -51.33
REMARK 500 8 ASP A 37 91.33 -171.31
REMARK 500 8 PRO A 57 103.46 -35.46
REMARK 500 9 LEU A 19 106.97 -44.58
REMARK 500 9 ASP A 37 88.04 -166.68
REMARK 500 9 PRO A 57 102.24 -37.59
REMARK 500 10 LEU A 19 106.02 -47.40
REMARK 500 10 ASP A 37 96.25 -172.74
REMARK 500 10 PRO A 57 99.30 -36.57
REMARK 500 11 LEU A 19 106.70 -47.01
REMARK 500 11 LEU A 22 150.74 -40.80
REMARK 500 11 ASP A 37 96.15 -169.74
REMARK 500 11 ALA A 56 53.69 35.69
REMARK 500 11 PRO A 57 109.72 -31.47
REMARK 500 12 LEU A 19 106.31 -45.65
REMARK 500 12 ASN A 21 -65.43 -93.67
REMARK 500 12 LEU A 22 149.13 -34.14
REMARK 500
REMARK 500 THIS ENTRY HAS 173 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 9 0.31 SIDE CHAIN
REMARK 500 1 ARG A 18 0.31 SIDE CHAIN
REMARK 500 1 ARG A 35 0.30 SIDE CHAIN
REMARK 500 2 ARG A 9 0.31 SIDE CHAIN
REMARK 500 2 ARG A 18 0.27 SIDE CHAIN
REMARK 500 2 ARG A 35 0.31 SIDE CHAIN
REMARK 500 3 ARG A 9 0.31 SIDE CHAIN
REMARK 500 3 ARG A 18 0.31 SIDE CHAIN
REMARK 500 3 ARG A 35 0.26 SIDE CHAIN
REMARK 500 4 ARG A 9 0.29 SIDE CHAIN
REMARK 500 4 ARG A 18 0.30 SIDE CHAIN
REMARK 500 4 ARG A 35 0.27 SIDE CHAIN
REMARK 500 5 ARG A 9 0.31 SIDE CHAIN
REMARK 500 5 ARG A 18 0.30 SIDE CHAIN
REMARK 500 5 ARG A 35 0.29 SIDE CHAIN
REMARK 500 6 ARG A 9 0.26 SIDE CHAIN
REMARK 500 6 ARG A 18 0.31 SIDE CHAIN
REMARK 500 6 ARG A 35 0.30 SIDE CHAIN
REMARK 500 7 ARG A 9 0.26 SIDE CHAIN
REMARK 500 7 ARG A 18 0.21 SIDE CHAIN
REMARK 500 7 ARG A 35 0.30 SIDE CHAIN
REMARK 500 8 ARG A 9 0.29 SIDE CHAIN
REMARK 500 8 ARG A 18 0.25 SIDE CHAIN
REMARK 500 8 ARG A 35 0.30 SIDE CHAIN
REMARK 500 9 ARG A 9 0.28 SIDE CHAIN
REMARK 500 9 ARG A 18 0.30 SIDE CHAIN
REMARK 500 9 ARG A 35 0.30 SIDE CHAIN
REMARK 500 10 ARG A 9 0.29 SIDE CHAIN
REMARK 500 10 ARG A 18 0.31 SIDE CHAIN
REMARK 500 10 ARG A 35 0.30 SIDE CHAIN
REMARK 500 11 ARG A 9 0.29 SIDE CHAIN
REMARK 500 11 ARG A 18 0.20 SIDE CHAIN
REMARK 500 11 ARG A 35 0.26 SIDE CHAIN
REMARK 500 12 ARG A 9 0.28 SIDE CHAIN
REMARK 500 12 ARG A 18 0.30 SIDE CHAIN
REMARK 500 12 ARG A 35 0.31 SIDE CHAIN
REMARK 500 13 ARG A 9 0.27 SIDE CHAIN
REMARK 500 13 ARG A 18 0.30 SIDE CHAIN
REMARK 500 13 ARG A 35 0.30 SIDE CHAIN
REMARK 500 14 ARG A 9 0.31 SIDE CHAIN
REMARK 500 14 ARG A 18 0.26 SIDE CHAIN
REMARK 500 14 ARG A 35 0.23 SIDE CHAIN
REMARK 500 15 ARG A 9 0.26 SIDE CHAIN
REMARK 500 15 ARG A 18 0.25 SIDE CHAIN
REMARK 500 15 ARG A 35 0.26 SIDE CHAIN
REMARK 500 16 ARG A 9 0.29 SIDE CHAIN
REMARK 500 16 ARG A 18 0.31 SIDE CHAIN
REMARK 500 16 ARG A 35 0.30 SIDE CHAIN
REMARK 500 17 ARG A 9 0.31 SIDE CHAIN
REMARK 500 17 ARG A 18 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 120 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6805 RELATED DB: BMRB
REMARK 900 NMR ASSIGNMENT
REMARK 900 RELATED ID: 2B87 RELATED DB: PDB
REMARK 900 ZTAQ:ANTI-ZTAQ COMPLEX STRUCTURE
REMARK 900 RELATED ID: 2B88 RELATED DB: PDB
REMARK 900 STRUCTURE FREE ZTAQ SUBUNIT
DBREF 2B89 A 2 58 UNP Q70AB8 Q70AB8_STAAU 117 173
SEQRES 1 A 58 VAL ASP ASN LYS PHE ASN LYS GLU ARG VAL ILE ALA ILE
SEQRES 2 A 58 GLY GLU ILE MET ARG LEU PRO ASN LEU ASN SER LEU GLN
SEQRES 3 A 58 VAL VAL ALA PHE ILE ASN SER LEU ARG 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
HELIX 1 1 LYS A 4 LEU A 19 1 16
HELIX 2 2 ASN A 23 ASP A 37 1 15
HELIX 3 3 GLN A 40 ALA A 56 1 17
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 - g 9 2 Bytes