Header list of 1klq.pdb file
Complete list - 23 20 Bytes
HEADER CELL CYCLE 12-DEC-01 1KLQ
TITLE THE MAD2 SPINDLE CHECKPOINT PROTEIN UNDERGOES SIMILAR MAJOR
TITLE 2 CONFORMATIONAL CHANGES UPON BINDING TO EITHER MAD1 OR CDC20
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MISSING N-TERMINAL 10 RESIDUES;
COMPND 5 SYNONYM: MAD2; SPINDLE CHECKPOINT PROTEIN MAD2; MAD2-LIKE 1; HSMAD2;
COMPND 6 MITOTIC FEEDBACK CONTROL PROTEIN MADP2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: MAD2-BINDING PEPTIDE;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: MBP1;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: SYNTHETIC 12-MER
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15[PREP4];
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE-30;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: THIS SEQUENCE IS IDENTIFIED USING PHAGE DISPLAY
KEYWDS PROTEIN-PEPTIDE COMPLEX, MAD2 FAMILY, CELL CYCLE
EXPDTA SOLUTION NMR
AUTHOR X.LUO,Z.TANG,J.RIZO,H.YU
REVDAT 4 23-FEB-22 1KLQ 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1KLQ 1 VERSN
REVDAT 2 22-FEB-02 1KLQ 1 HELIX SHEET REMARK
REVDAT 1 25-JAN-02 1KLQ 0
JRNL AUTH X.LUO,Z.TANG,J.RIZO,H.YU
JRNL TITL THE MAD2 SPINDLE CHECKPOINT PROTEIN UNDERGOES SIMILAR MAJOR
JRNL TITL 2 CONFORMATIONAL CHANGES UPON BINDING TO EITHER MAD1 OR CDC20.
JRNL REF MOL.CELL V. 9 59 2002
JRNL REFN ISSN 1097-2765
JRNL PMID 11804586
JRNL DOI 10.1016/S1097-2765(01)00435-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9A, CNS 0.9A
REMARK 3 AUTHORS : BRUNGER, A.T. (CNS), BRUNGER, A.T. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 3124 RESTRAINTS, 2535 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 363 DIHEDRAL ANGLE RESTRAINTS,226 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1KLQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015085.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303; 303; 303; 303
REMARK 210 PH : 7.4; 7.4; 7.4; 7.4; 7.4; 7.4
REMARK 210 IONIC STRENGTH : 0.3M KCL; 0.3M KCL; 0.3M KCL;
REMARK 210 0.3M KCL; 0.3M KCL; 0.3M KCL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM MAD2 PROTEIN U-15N; 1MM
REMARK 210 MBP1 NA; 50MM PHOSPHATE BUFFER;
REMARK 210 0.3M KCL; 1MM DTT; 0.8MM MAD2
REMARK 210 PROTEIN U-15N, 13C, 2H; 1MM MBP1
REMARK 210 NA; 50MM PHOSPHATE BUFFER; 0.3M
REMARK 210 KCL; 1MM DTT; 0.8MM MAD2 PROTEIN
REMARK 210 U-15N, 13C; 1MM MBP1 NA; 50MM
REMARK 210 PHOSPHATE BUFFER; 0.3M KCL; 1MM
REMARK 210 DTT; 0.8MM MAD2 PROTEIN U-15N,
REMARK 210 13C, U-60% 2H; 1MM MBP1 NA; 50MM
REMARK 210 PHOSPHATE BUFFER; 0.3M KCL; 1MM
REMARK 210 DTT; 0.8MM MBP1 U-15N; 1MM MAD2
REMARK 210 PROTEIN NA; 50MM PHOSPHATE
REMARK 210 BUFFER; 0.3M KCL; 1MM DTT; 0.8MM
REMARK 210 MBP1 U-15N, 13C; 1MM MAD2
REMARK 210 PROTEIN NA; 50MM PHOSPHATE
REMARK 210 BUFFER; 0.3M KCL; 1MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNCA;
REMARK 210 3D_13C-SEPARATED_NOESY; 3D_H(CC)
REMARK 210 (CO)NH; HN(CO)CA; 3D_(H)C(C)(CO)
REMARK 210 NH; HN(COCA)CB; HN(CA)CB
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 ALA B 11
REMARK 465 VAL B 12
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 H THR A 46 O VAL A 57 1.49
REMARK 500 O VAL A 48 H LEU A 55 1.49
REMARK 500 O ARG A 135 H ALA A 139 1.51
REMARK 500 O GLN A 73 H TRP A 77 1.57
REMARK 500 O THR A 46 H VAL A 57 1.59
REMARK 500 O SER A 132 H GLN A 136 1.59
REMARK 500 O LEU A 67 H VAL A 71 1.59
REMARK 500 OH TYR A 40 OG1 THR A 58 2.19
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 THR A 14 -67.84 -144.75
REMARK 500 GLU A 43 1.10 -68.82
REMARK 500 TYR A 51 15.38 59.29
REMARK 500 SER A 82 115.05 80.39
REMARK 500 SER A 95 60.28 165.00
REMARK 500 GLU A 97 -163.83 46.79
REMARK 500 ASP A 109 116.18 68.28
REMARK 500 THR A 111 99.10 59.85
REMARK 500 ALA A 112 46.02 -161.78
REMARK 500 ARG A 119 110.06 60.78
REMARK 500 LEU A 146 149.33 61.62
REMARK 500 LEU A 147 141.70 177.66
REMARK 500 GLU A 148 73.16 176.74
REMARK 500 THR A 159 -162.59 -112.54
REMARK 500 ASP A 160 -74.05 -126.40
REMARK 500 PRO A 166 -128.69 -91.95
REMARK 500 SER A 172 -124.08 178.37
REMARK 500 PRO A 174 -14.08 -49.43
REMARK 500 PHE A 176 52.43 23.75
REMARK 500 ILE A 177 -164.91 45.23
REMARK 500 PRO A 204 -179.38 -64.43
REMARK 500 VAL A 205 68.60 64.69
REMARK 500 PRO B 8 -157.75 -61.90
REMARK 500 GLN B 9 -66.06 -140.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DUJ RELATED DB: PDB
REMARK 900 THE SOLUTION STRUCTURE OF THE FREE MAD2 PROTEIN
DBREF 1KLQ A 11 207 UNP Q13257 MD2L1_HUMAN 9 205
DBREF 1KLQ B 1 12 PDB 1KLQ 1KLQ 1 12
SEQADV 1KLQ GLY A 11 UNP Q13257 GLN 9 EXPRESSION TAG
SEQADV 1KLQ SER A 12 UNP Q13257 GLY 10 EXPRESSION TAG
SEQRES 1 A 197 GLY SER ILE THR LEU ARG GLY SER ALA GLU ILE VAL ALA
SEQRES 2 A 197 GLU PHE PHE SER PHE GLY ILE ASN SER ILE LEU TYR GLN
SEQRES 3 A 197 ARG GLY ILE TYR PRO SER GLU THR PHE THR ARG VAL GLN
SEQRES 4 A 197 LYS TYR GLY LEU THR LEU LEU VAL THR THR ASP LEU GLU
SEQRES 5 A 197 LEU ILE LYS TYR LEU ASN ASN VAL VAL GLU GLN LEU LYS
SEQRES 6 A 197 ASP TRP LEU TYR LYS CYS SER VAL GLN LYS LEU VAL VAL
SEQRES 7 A 197 VAL ILE SER ASN ILE GLU SER GLY GLU VAL LEU GLU ARG
SEQRES 8 A 197 TRP GLN PHE ASP ILE GLU CYS ASP LYS THR ALA LYS ASP
SEQRES 9 A 197 ASP SER ALA PRO ARG GLU LYS SER GLN LYS ALA ILE GLN
SEQRES 10 A 197 ASP GLU ILE ARG SER VAL ILE ARG GLN ILE THR ALA THR
SEQRES 11 A 197 VAL THR PHE LEU PRO LEU LEU GLU VAL SER CYS SER PHE
SEQRES 12 A 197 ASP LEU LEU ILE TYR THR ASP LYS ASP LEU VAL VAL PRO
SEQRES 13 A 197 GLU LYS TRP GLU GLU SER GLY PRO GLN PHE ILE THR ASN
SEQRES 14 A 197 SER GLU GLU VAL ARG LEU ARG SER PHE THR THR THR ILE
SEQRES 15 A 197 HIS LYS VAL ASN SER MET VAL ALA TYR LYS ILE PRO VAL
SEQRES 16 A 197 ASN ASP
SEQRES 1 B 12 SER TRP TYR SER TYR PRO PRO PRO GLN ARG ALA VAL
HELIX 1 1 THR A 14 GLY A 38 125 25
HELIX 2 2 PRO A 41 GLU A 43 53 3
HELIX 3 3 ASP A 60 TYR A 79 120 20
HELIX 4 4 GLN A 123 LEU A 144 122 22
SHEET 1 A 2 PHE A 45 LYS A 50 0
SHEET 2 A 2 LEU A 53 THR A 58 -1 O LEU A 55 N VAL A 48
SHEET 1 B 7 GLU A 181 THR A 190 0
SHEET 2 B 7 HIS A 193 LYS A 202 -1 O VAL A 199 N VAL A 183
SHEET 3 B 7 GLU A 97 CYS A 108 -1 N ARG A 101 O ALA A 200
SHEET 4 B 7 GLN A 84 ASN A 92 -1 N ILE A 90 O GLU A 100
SHEET 5 B 7 CYS A 151 THR A 159 -1 O TYR A 158 N LYS A 85
SHEET 6 B 7 TRP B 2 TYR B 5 -1 O TYR B 5 N LEU A 155
SHEET 7 B 7 GLU A 170 GLU A 171 -1 N GLU A 170 O SER B 4
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
Complete list - 23 20 Bytes