Header list of 1mdj.pdb file
Complete list - b 23 2 Bytes
HEADER COMPLEX (ELECTRON TRANSPORT/PEPTIDE) 27-FEB-95 1MDJ
TITLE HIGH RESOLUTION SOLUTION NMR STRUCTURE OF MIXED DISULFIDE INTERMEDIATE
TITLE 2 BETWEEN HUMAN THIOREDOXIN (C35A, C62A, C69A, C73A) MUTANT AND A 13
TITLE 3 RESIDUE PEPTIDE COMPRISING ITS TARGET SITE IN HUMAN NFKB (RESIDUES
TITLE 4 56-68 OF THE P50 SUBUNIT OF NFKB)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: TARGET SITE IN HUMAN NFKB;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2
KEYWDS COMPLEX (ELECTRON TRANSPORT-PEPTIDE), COMPLEX (ELECTRON TRANSPORT-
KEYWDS 2 PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.M.CLORE,J.QIN,A.M.GRONENBORN
REVDAT 5 23-FEB-22 1MDJ 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1MDJ 1 VERSN
REVDAT 3 01-APR-03 1MDJ 1 JRNL
REVDAT 2 20-JUL-95 1MDJ 1 COMPND EXPDTA
REVDAT 1 03-JUN-95 1MDJ 0
JRNL AUTH J.QIN,G.M.CLORE,W.M.KENNEDY,J.R.HUTH,A.M.GRONENBORN
JRNL TITL SOLUTION STRUCTURE OF HUMAN THIOREDOXIN IN A MIXED DISULFIDE
JRNL TITL 2 INTERMEDIATE COMPLEX WITH ITS TARGET PEPTIDE FROM THE
JRNL TITL 3 TRANSCRIPTION FACTOR NF KAPPA B.
JRNL REF STRUCTURE V. 3 289 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 7788295
JRNL DOI 10.1016/S0969-2126(01)00159-9
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE 3D STRUCTURE OF THE HUMAN THIOREDOXIN-NFKB PEPTIDE
REMARK 3 COMPLEX IN SOLUTION BY NMR IS BASED ON 3213 EXPERIMENTAL
REMARK 3 RESTRAINTS COMPRISING:
REMARK 3 2546 STRUCTURE USEFUL INTERPROTON DISTANCE RESTRAINTS
REMARK 3 36 RESTRAINTS FOR 18 BACKBONE H-BONDS
REMARK 3 44 RESTRAINTS FOR 6 BOUND WATER MOLECULES
REMARK 3 300 TORSION ANGLE RESTRAINTS (104 PHI, 76 PSI, 78 CHI1
REMARK 3 AND 31 CHI2 FOR HUMAN THIOREDOXIN, AND 7 CHI1 AND 4
REMARK 3 CHI2 RESTRAINTS FOR THE NFKB PEPTIDE)
REMARK 3 88 HN-HALPHA THREE-BOND COUPLING CONSTANTS
REMARK 3 102 13CALPHA AND 97 13CB CHEMICAL SHIFT RESTRAINTS.
REMARK 3
REMARK 3 THE BREAKDOWN OF THE INTERPROTON DISTANCE RESTRAINTS IS AS
REMARK 3 FOLLOWS:
REMARK 3 INTRAMOLECULAR HTRX RESTRAINTS:
REMARK 3 503 SEQUENTIAL
REMARK 3 437 SHORT RANGE (1 < |I-J|<=5)
REMARK 3 727 LONG RANGE (|I-J|>5)
REMARK 3 690 INTRARESIDUE
REMARK 3 INTRAMOLECULAR PEPTIDE RESTRAINTS: 115
REMARK 3 INTERMOLECULAR HTRX-NFKB: 74
REMARK 3
REMARK 3 THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC
REMARK 3 MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
REMARK 3 METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. &
REMARK 3 GRONENBORN, A.M. (1988) FEBS LETT 229, 317 - 324. ALL
REMARK 3 STRUCTURAL STATISTICS ARE GIVEN IN THE REFERENCE.
REMARK 3
REMARK 3 THE STRUCTURE FOUND IN PDB ENTRY 1MDI IS THE RESTRAINED
REMARK 3 MINIMIZED AVERAGE STRUCTURE: (SA)R. THIS IS OBTAINED
REMARK 3 BY FIRST AVERAGING THE COORDINATES OF THE INDIVIDUAL 60
REMARK 3 DYNAMICAL SIMULATED ANNEALING SA STRUCTURES BEST FITTED TO
REMARK 3 RESIDUES 1 - 105 OF HTRX AND RESIDUES 57 - 67 OF THE
REMARK 3 PEPTIDE AND SUBJECTING THE RESULTING COORDINATES TO
REMARK 3 RESTRAINED MINIMIZATION. THE LAST NUMBER COLUMN IN THIS
REMARK 3 SET OF COORDINATES (THE B-FACTOR COLUMN IN X-RAY
REMARK 3 STRUCTURES) GIVES THE AVERAGE RMS DIFFERENCE BETWEEN THE
REMARK 3 INDIVIDUAL SA STRUCTURES AND THE MEAN STRUCTURE. THE
REMARK 3 NUMBERS IN THE LAST COLUMN OF THE INDIVIDUAL STRUCTURES
REMARK 3 HAVE NO MEANING.
REMARK 4
REMARK 4 1MDJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174960.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 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 SER A 28 -162.67 -110.51
REMARK 500 1 PHE A 41 -76.94 -110.10
REMARK 500 1 SER A 90 -169.70 -102.77
REMARK 500 1 ALA A 92 94.35 -57.01
REMARK 500 1 ARG B 4 -105.00 -142.08
REMARK 500 1 TYR B 5 -169.81 -109.74
REMARK 500 1 GLU B 8 44.63 -83.17
REMARK 500 1 PRO B 10 25.76 -67.33
REMARK 500 1 HIS B 12 -94.79 -58.63
REMARK 500 2 PRO A 40 -8.16 -59.68
REMARK 500 2 PHE A 41 -70.30 -108.19
REMARK 500 2 SER A 90 -163.83 -103.97
REMARK 500 2 ALA A 92 94.36 -53.18
REMARK 500 2 ARG B 4 -86.48 -138.70
REMARK 500 2 GLU B 8 45.00 -83.92
REMARK 500 2 PRO B 10 22.99 -66.47
REMARK 500 3 SER A 28 -162.46 -107.33
REMARK 500 3 PHE A 41 -78.23 -108.77
REMARK 500 3 LEU A 45 -13.27 -49.74
REMARK 500 3 LYS A 82 17.19 56.55
REMARK 500 3 SER A 90 -167.95 -103.36
REMARK 500 3 ALA A 92 96.44 -56.28
REMARK 500 3 ARG B 2 62.64 -164.27
REMARK 500 3 ARG B 4 -110.43 -145.69
REMARK 500 3 GLU B 8 47.57 -83.25
REMARK 500 3 PRO B 10 26.94 -68.38
REMARK 500 4 PHE A 41 -80.61 -111.20
REMARK 500 4 VAL A 59 -0.58 -52.06
REMARK 500 4 GLU A 88 147.45 -173.71
REMARK 500 4 SER A 90 -167.88 -102.76
REMARK 500 4 ALA A 92 95.11 -60.81
REMARK 500 4 ARG B 2 21.92 -167.74
REMARK 500 4 ARG B 4 -105.27 -150.68
REMARK 500 4 GLU B 8 44.18 -83.00
REMARK 500 4 PRO B 10 23.13 -66.34
REMARK 500 4 HIS B 12 -122.04 -156.17
REMARK 500 5 PHE A 41 -70.21 -103.54
REMARK 500 5 VAL A 59 -2.06 -56.87
REMARK 500 5 ALA A 92 94.69 -56.55
REMARK 500 5 ARG B 4 -93.20 -149.17
REMARK 500 5 TYR B 5 -166.29 -116.03
REMARK 500 5 GLU B 8 42.91 -84.54
REMARK 500 5 PRO B 10 24.36 -66.39
REMARK 500 6 PHE A 41 -72.19 -110.39
REMARK 500 6 VAL A 59 -6.86 -54.14
REMARK 500 6 SER A 90 -163.70 -103.07
REMARK 500 6 ALA A 92 94.53 -53.09
REMARK 500 6 ARG B 4 -99.88 -150.23
REMARK 500 6 GLU B 8 46.01 -82.97
REMARK 500 6 PRO B 10 25.52 -68.24
REMARK 500
REMARK 500 THIS ENTRY HAS 247 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MDI RELATED DB: PDB
REMARK 900 RELATED ID: 1MDK RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AT POSITION 74 THR WAS FOUND BY WOLMAN ET AL., JOURNAL OF
REMARK 999 BIOCHEMISTRY 263, 15506 (1988).
DBREF 1MDJ A 2 105 UNP P10599 THIO_HUMAN 1 104
DBREF 1MDJ B 1 13 UNP P19838 NFKB1_HUMAN 53 65
SEQADV 1MDJ ALA A 35 UNP P10599 CYS 34 CONFLICT
SEQADV 1MDJ ALA A 62 UNP P10599 CYS 61 CONFLICT
SEQADV 1MDJ ALA A 69 UNP P10599 CYS 68 CONFLICT
SEQADV 1MDJ ALA A 73 UNP P10599 CYS 72 CONFLICT
SEQADV 1MDJ THR A 74 UNP P10599 MET 73 CONFLICT
SEQRES 1 A 105 MET VAL LYS GLN ILE GLU SER LYS THR ALA PHE GLN GLU
SEQRES 2 A 105 ALA LEU ASP ALA ALA GLY ASP LYS LEU VAL VAL VAL ASP
SEQRES 3 A 105 PHE SER ALA THR TRP CYS GLY PRO ALA LYS MET ILE LYS
SEQRES 4 A 105 PRO PHE PHE HIS SER LEU SER GLU LYS TYR SER ASN VAL
SEQRES 5 A 105 ILE PHE LEU GLU VAL ASP VAL ASP ASP ALA GLN ASP VAL
SEQRES 6 A 105 ALA SER GLU ALA GLU VAL LYS ALA THR PRO THR PHE GLN
SEQRES 7 A 105 PHE PHE LYS LYS GLY GLN LYS VAL GLY GLU PHE SER GLY
SEQRES 8 A 105 ALA ASN LYS GLU LYS LEU GLU ALA THR ILE ASN GLU LEU
SEQRES 9 A 105 VAL
SEQRES 1 B 13 PHE ARG PHE ARG TYR VAL CYS GLU GLY PRO SER HIS GLY
FORMUL 3 HOH *6(H2 O)
HELIX 1 1 LYS A 8 ALA A 17 1 10
HELIX 2 2 GLY A 33 PHE A 42 1 10
HELIX 3 3 SER A 44 LYS A 48 5 5
HELIX 4 4 GLN A 63 ALA A 69 1 7
HELIX 5 5 LYS A 94 LEU A 104 1 11
SHEET 1 A 5 VAL A 2 ILE A 5 0
SHEET 2 A 5 ILE A 53 VAL A 57 1 N PHE A 54 O LYS A 3
SHEET 3 A 5 VAL A 23 PHE A 27 1 N VAL A 24 O ILE A 53
SHEET 4 A 5 THR A 76 LYS A 81 -1 N PHE A 80 O VAL A 23
SHEET 5 A 5 GLN A 84 SER A 90 -1 N PHE A 89 O PHE A 77
SSBOND 1 CYS A 32 CYS B 7 1555 1555 2.02
CISPEP 1 THR A 74 PRO A 75 1 -1.41
CISPEP 2 THR A 74 PRO A 75 2 -2.15
CISPEP 3 THR A 74 PRO A 75 3 -1.27
CISPEP 4 THR A 74 PRO A 75 4 -1.92
CISPEP 5 THR A 74 PRO A 75 5 -2.38
CISPEP 6 THR A 74 PRO A 75 6 -1.59
CISPEP 7 THR A 74 PRO A 75 7 -1.58
CISPEP 8 THR A 74 PRO A 75 8 -1.97
CISPEP 9 THR A 74 PRO A 75 9 -2.03
CISPEP 10 THR A 74 PRO A 75 10 -1.76
CISPEP 11 THR A 74 PRO A 75 11 -1.54
CISPEP 12 THR A 74 PRO A 75 12 -1.71
CISPEP 13 THR A 74 PRO A 75 13 -1.88
CISPEP 14 THR A 74 PRO A 75 14 -1.80
CISPEP 15 THR A 74 PRO A 75 15 -1.84
CISPEP 16 THR A 74 PRO A 75 16 -1.94
CISPEP 17 THR A 74 PRO A 75 17 -1.77
CISPEP 18 THR A 74 PRO A 75 18 -1.42
CISPEP 19 THR A 74 PRO A 75 19 -1.72
CISPEP 20 THR A 74 PRO A 75 20 -1.30
CISPEP 21 THR A 74 PRO A 75 21 -2.19
CISPEP 22 THR A 74 PRO A 75 22 -1.69
CISPEP 23 THR A 74 PRO A 75 23 -1.80
CISPEP 24 THR A 74 PRO A 75 24 -1.81
CISPEP 25 THR A 74 PRO A 75 25 -1.96
CISPEP 26 THR A 74 PRO A 75 26 -2.03
CISPEP 27 THR A 74 PRO A 75 27 -1.63
CISPEP 28 THR A 74 PRO A 75 28 -2.20
CISPEP 29 THR A 74 PRO A 75 29 -1.78
CISPEP 30 THR A 74 PRO A 75 30 -1.78
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