Header list of 1k09.pdb file
Complete list - b 23 2 Bytes
HEADER DE NOVO PROTEIN 18-SEP-01 1K09
TITLE SOLUTION STRUCTURE OF BETACORE, A DESIGNED WATER SOLUBLE FOUR-STRANDED
TITLE 2 ANTIPARALLEL B-SHEET PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CORE MODULE I;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CM I;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CORE MODULE II;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: CM II;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED BY SOLID-PHASE
SOURCE 4 PEPTIDE CHEMISTRY. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN
SOURCE 5 BOS TAURUS (BOVINE).;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED BY SOLID-PHASE
SOURCE 9 PEPTIDE CHEMISTRY. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN
SOURCE 10 BOS TAURUS (BOVINE).
KEYWDS FOUR-STRANDED ANTIPARALLEL BETA-SHEET, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.CARULLA,C.WOODWARD,G.BARANY
REVDAT 4 23-FEB-22 1K09 1 REMARK LINK
REVDAT 3 24-FEB-09 1K09 1 VERSN
REVDAT 2 01-APR-03 1K09 1 JRNL
REVDAT 1 10-JUL-02 1K09 0
JRNL AUTH N.CARULLA,C.WOODWARD,G.BARANY
JRNL TITL BETACORE, A DESIGNED WATER SOLUBLE FOUR-STRANDED
JRNL TITL 2 ANTIPARALLEL BETA-SHEET PROTEIN.
JRNL REF PROTEIN SCI. V. 11 1539 2002
JRNL REFN ISSN 0961-8368
JRNL PMID 12021452
JRNL DOI 10.1110/PS.4440102
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 195 RESTRAINTS, 172 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 14 DIHEDRAL ANGLE RESTRAINTS, 9 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1K09 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014397.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278; 288
REMARK 210 PH : 3; 3
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.4 MM BETACORE SELECTIVELY-15N;
REMARK 210 PH3; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N-HSQC-NOESY;
REMARK 210 3D_15N-HSQC-TOCSY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMERS ARE
REMARK 210 THOSE WITH NO CONSTRAINT
REMARK 210 VIOLATIONS GREATER THAN 0.5
REMARK 210 ANGSTROMS FOR NOES AND 5 DEGREES
REMARK 210 FOR DIHEDRALS. THEY ARE ALSO THE
REMARK 210 ONES WITH BEST COVALENT GEOMETRY.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
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: 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 CLH B 16 OM
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 NM CLG A 4 CL CLH B 16 1.31
REMARK 500 O ALA A 12 H LEU A 16 1.51
REMARK 500 SG MPT B 1 SG CYS B 25 2.02
REMARK 500 SG MPT A 1 SG CYS A 25 2.02
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 LYS A 2 93.96 62.95
REMARK 500 1 CLG A 4 105.32 -174.70
REMARK 500 1 ILE A 5 -165.00 -54.90
REMARK 500 1 ARG A 7 88.52 -154.67
REMARK 500 1 TYR A 10 170.59 48.22
REMARK 500 1 ASN A 11 67.24 162.35
REMARK 500 1 ALA A 12 -103.47 -44.13
REMARK 500 1 LYS A 13 84.84 45.74
REMARK 500 1 ABA A 17 90.28 175.55
REMARK 500 1 GLN A 18 102.65 -43.80
REMARK 500 1 LYS B 2 47.39 -83.41
REMARK 500 1 ALA B 3 -161.25 -108.68
REMARK 500 1 ARG B 4 64.69 63.76
REMARK 500 1 ARG B 7 91.92 -56.05
REMARK 500 1 PHE B 9 67.89 -150.22
REMARK 500 1 TYR B 10 102.60 -42.56
REMARK 500 1 CLH B 16 73.15 176.88
REMARK 500 1 ABA B 17 -162.09 39.14
REMARK 500 1 GLN B 18 155.27 169.61
REMARK 500 1 THR B 19 117.25 -162.53
REMARK 500 1 TYR B 22 24.40 -165.42
REMARK 500 2 ALA A 3 -120.68 -110.33
REMARK 500 2 CLG A 4 104.37 51.55
REMARK 500 2 ARG A 7 103.92 173.68
REMARK 500 2 LYS A 13 -82.07 -47.95
REMARK 500 2 VAL A 21 -79.31 -98.01
REMARK 500 2 TYR A 22 116.75 69.56
REMARK 500 2 ILE B 6 140.72 -170.46
REMARK 500 2 ARG B 7 147.71 -172.23
REMARK 500 2 TYR B 10 -86.36 -114.76
REMARK 500 2 ASN B 11 -34.08 175.28
REMARK 500 2 LYS B 13 -78.05 -41.88
REMARK 500 2 CLH B 16 140.10 64.67
REMARK 500 2 GLN B 18 87.83 -25.59
REMARK 500 2 VAL B 21 -148.85 -106.79
REMARK 500 2 TYR B 22 -165.79 40.25
REMARK 500 3 LYS A 2 -119.39 -128.76
REMARK 500 3 CLG A 4 103.82 -37.05
REMARK 500 3 ALA A 12 -116.93 -58.22
REMARK 500 3 LYS A 13 80.52 51.53
REMARK 500 3 LEU A 16 53.96 -150.25
REMARK 500 3 ABA A 17 108.15 -42.55
REMARK 500 3 ALA B 3 61.97 -110.89
REMARK 500 3 ARG B 4 -135.79 -131.09
REMARK 500 3 TYR B 10 107.51 -50.46
REMARK 500 3 CLH B 16 125.89 -38.31
REMARK 500 3 TYR B 22 51.29 -178.85
REMARK 500 4 ALA A 3 55.83 -105.68
REMARK 500 4 LYS A 13 -80.33 -49.77
REMARK 500 4 ALA B 3 -166.86 -110.34
REMARK 500
REMARK 500 THIS ENTRY HAS 274 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 7 0.27 SIDE CHAIN
REMARK 500 1 ARG B 4 0.32 SIDE CHAIN
REMARK 500 1 ARG B 7 0.17 SIDE CHAIN
REMARK 500 2 ARG A 7 0.22 SIDE CHAIN
REMARK 500 2 ARG B 4 0.15 SIDE CHAIN
REMARK 500 2 ARG B 7 0.31 SIDE CHAIN
REMARK 500 3 ARG A 7 0.14 SIDE CHAIN
REMARK 500 3 ARG B 4 0.08 SIDE CHAIN
REMARK 500 3 ARG B 7 0.18 SIDE CHAIN
REMARK 500 4 ARG A 7 0.32 SIDE CHAIN
REMARK 500 4 ARG B 4 0.21 SIDE CHAIN
REMARK 500 4 ARG B 7 0.19 SIDE CHAIN
REMARK 500 5 ARG A 7 0.30 SIDE CHAIN
REMARK 500 5 ARG B 4 0.29 SIDE CHAIN
REMARK 500 5 ARG B 7 0.22 SIDE CHAIN
REMARK 500 6 ARG A 7 0.26 SIDE CHAIN
REMARK 500 6 ARG B 4 0.29 SIDE CHAIN
REMARK 500 6 ARG B 7 0.25 SIDE CHAIN
REMARK 500 7 ARG A 7 0.30 SIDE CHAIN
REMARK 500 7 ARG B 4 0.31 SIDE CHAIN
REMARK 500 7 ARG B 7 0.20 SIDE CHAIN
REMARK 500 8 ARG A 7 0.24 SIDE CHAIN
REMARK 500 8 ARG B 4 0.13 SIDE CHAIN
REMARK 500 8 ARG B 7 0.23 SIDE CHAIN
REMARK 500 9 ARG A 7 0.32 SIDE CHAIN
REMARK 500 9 ARG B 4 0.30 SIDE CHAIN
REMARK 500 9 ARG B 7 0.23 SIDE CHAIN
REMARK 500 10 ARG A 7 0.11 SIDE CHAIN
REMARK 500 10 ARG B 4 0.31 SIDE CHAIN
REMARK 500 10 ARG B 7 0.32 SIDE CHAIN
REMARK 500 11 ARG A 7 0.29 SIDE CHAIN
REMARK 500 11 ARG B 4 0.30 SIDE CHAIN
REMARK 500 11 ARG B 7 0.27 SIDE CHAIN
REMARK 500 12 ARG A 7 0.30 SIDE CHAIN
REMARK 500 12 ARG B 4 0.26 SIDE CHAIN
REMARK 500 12 ARG B 7 0.31 SIDE CHAIN
REMARK 500 13 ARG A 7 0.11 SIDE CHAIN
REMARK 500 13 ARG B 4 0.15 SIDE CHAIN
REMARK 500 13 ARG B 7 0.32 SIDE CHAIN
REMARK 500 14 ARG A 7 0.23 SIDE CHAIN
REMARK 500 14 ARG B 4 0.25 SIDE CHAIN
REMARK 500 14 ARG B 7 0.29 SIDE CHAIN
REMARK 500 15 ARG A 7 0.09 SIDE CHAIN
REMARK 500 15 ARG B 4 0.25 SIDE CHAIN
REMARK 500 15 ARG B 7 0.17 SIDE CHAIN
REMARK 500 16 ARG A 7 0.10 SIDE CHAIN
REMARK 500 16 ARG B 4 0.20 SIDE CHAIN
REMARK 500 16 ARG B 7 0.26 SIDE CHAIN
REMARK 500 17 ARG A 7 0.26 SIDE CHAIN
REMARK 500 17 ARG B 4 0.15 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 60 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 26
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 B 26
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THESE SYNTHETIC PEPTIDE (MINUS THE
REMARK 999 MODIFIED AMINO ACIDS AND RESIDUE ASP 14) IS NATURALLY
REMARK 999 FOUND IN BOVINE PANCREATIC TRYPSIN INHIBITOR.
DBREF 1K09 A 2 25 UNP P00974 BPT1_BOVIN 42 65
DBREF 1K09 B 2 25 UNP P00974 BPT1_BOVIN 42 65
SEQADV 1K09 MPT A 1 UNP P00974 SEE REMARK 999
SEQADV 1K09 CLG A 4 UNP P00974 ARG 44 SEE REMARK 999
SEQADV 1K09 ASP A 14 UNP P00974 ALA 54 SEE REMARK 999
SEQADV 1K09 ABA A 17 UNP P00974 CYS 57 SEE REMARK 999
SEQADV 1K09 MPT B 1 UNP P00974 SEE REMARK 999
SEQADV 1K09 ASP B 14 UNP P00974 ALA 54 SEE REMARK 999
SEQADV 1K09 CLH B 16 UNP P00974 LEU 56 SEE REMARK 999
SEQADV 1K09 ABA B 17 UNP P00974 CYS 57 SEE REMARK 999
SEQRES 1 A 26 MPT LYS ALA CLG ILE ILE ARG TYR PHE TYR ASN ALA LYS
SEQRES 2 A 26 ASP GLY LEU ABA GLN THR PHE VAL TYR GLY GLY CYS NH2
SEQRES 1 B 26 MPT LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS
SEQRES 2 B 26 ASP GLY CLH ABA GLN THR PHE VAL TYR GLY GLY CYS NH2
MODRES 1K09 CLG A 4 LYS
MODRES 1K09 ABA A 17 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 1K09 CLH B 16 LYS
MODRES 1K09 ABA B 17 ALA ALPHA-AMINOBUTYRIC ACID
HET MPT A 1 9
HET CLG A 4 34
HET ABA A 17 13
HET NH2 A 26 3
HET MPT B 1 9
HET CLH B 16 31
HET ABA B 17 13
HET NH2 B 26 3
HETNAM MPT BETA-MERCAPTOPROPIONIC ACID
HETNAM CLG 2-AMINO-6-[2-(2-AMINOOXY-ACETYLAMINO)-ACETYLAMINO]-
HETNAM 2 CLG HEXANOIC ACID
HETNAM ABA ALPHA-AMINOBUTYRIC ACID
HETNAM NH2 AMINO GROUP
HETNAM CLH 2-AMINO-6-[2-(2-OXO-ACETYLAMINO)-ACETYLAMINO]-HEXANOIC
HETNAM 2 CLH ACID
FORMUL 1 MPT 2(C3 H6 O2 S)
FORMUL 1 CLG C10 H20 N4 O5
FORMUL 1 ABA 2(C4 H9 N O2)
FORMUL 1 NH2 2(H2 N)
FORMUL 2 CLH C10 H17 N3 O5
LINK C MPT A 1 N LYS A 2 1555 1555 1.31
LINK C ALA A 3 N CLG A 4 1555 1555 1.30
LINK C CLG A 4 N ILE A 5 1555 1555 1.31
LINK C LEU A 16 N ABA A 17 1555 1555 1.31
LINK C ABA A 17 N GLN A 18 1555 1555 1.31
LINK C CYS A 25 N NH2 A 26 1555 1555 1.31
LINK C MPT B 1 N LYS B 2 1555 1555 1.31
LINK C GLY B 15 N CLH B 16 1555 1555 1.30
LINK C CLH B 16 N ABA B 17 1555 1555 1.31
LINK C ABA B 17 N GLN B 18 1555 1555 1.31
LINK C CYS B 25 N NH2 B 26 1555 1555 1.31
SITE 1 AC1 2 GLY A 24 CYS A 25
SITE 1 AC2 1 CYS B 25
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 - b 23 2 Bytes