Header list of 1yzc.pdb file
Complete list - r 2 2 Bytes
HEADER ELECTRON TRANSPORT 28-FEB-05 1YZC
TITLE THE SOLUTION STRUCTURE OF A REDESIGNED APOCYTOCHROME B562 (RD-APOCYT
TITLE 2 B562) WITH THE N- AND A PART OF THE C-TERMINAL HELICES UNFOLDED
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EDESIGNED APO-CYTOCHROME B562;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
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: BL21(DE3) PLYSS CELLS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: ET17B
KEYWDS FOLDING INTERMEDIATES, NATIVE-STATE HYDROGEN EXCHANGE, PROTEIN
KEYWDS 2 ENGINEERING, PROTEIN STRUCTURE, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, BERKELEY STRUCTURAL GENOMICS CENTER, BSGC,
KEYWDS 4 ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR H.FENG,Z.ZHOU,Y.BAI,BERKELEY STRUCTURAL GENOMICS CENTER (BSGC)
REVDAT 3 02-MAR-22 1YZC 1 REMARK
REVDAT 2 24-FEB-09 1YZC 1 VERSN
REVDAT 1 28-MAR-06 1YZC 0
JRNL AUTH H.FENG,Z.ZHOU,Y.BAI
JRNL TITL A PROTEIN FOLDING PATHWAY WITH MULTIPLE FOLDING
JRNL TITL 2 INTERMEDIATES AT ATOMIC RESOLUTION
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 5026 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15793003
JRNL DOI 10.1073/PNAS.0501372102
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 5.0.4, X-PLOR NIH-2.9
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YZC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032101.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.84
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 50MM SODIUM ACETATE; 92.5% H2O,
REMARK 210 7.5% D2O; 50MM SODIUM ACETATE;
REMARK 210 99% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D HSQC; 3D_15N-SEPARATED_NOESY;
REMARK 210 3D_13C-SEPARATED_NOESY; HNHA; 3D
REMARK 210 HNCACB, 3D CBCACONH; 3D HAHBCONH,
REMARK 210 3D HNCO, 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR NIH-2.9
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210 MATRIX RELAXATION TORSION ANGLE
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 LYS A 59 H HIS A 63 1.47
REMARK 500 O SER A 52 H ASP A 54 1.50
REMARK 500 O GLY A 101 H GLN A 103 1.53
REMARK 500 O ASP A 66 H GLY A 70 1.58
REMARK 500 O GLN A 41 H ALA A 43 1.58
REMARK 500 O ALA A 35 H ASP A 39 1.59
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 LEU A 3 -80.42 -89.84
REMARK 500 1 GLU A 4 -157.21 59.99
REMARK 500 1 ASP A 5 23.89 49.87
REMARK 500 1 ASP A 7 -37.44 -150.62
REMARK 500 1 THR A 9 34.23 -89.12
REMARK 500 1 ASN A 13 -33.56 -156.12
REMARK 500 1 LYS A 15 -81.34 -156.98
REMARK 500 1 LYS A 19 -85.40 47.18
REMARK 500 1 ASP A 21 -83.57 -85.65
REMARK 500 1 ASN A 22 95.61 -161.87
REMARK 500 1 ALA A 23 -23.34 79.21
REMARK 500 1 GLN A 41 -148.65 -69.41
REMARK 500 1 ALA A 43 -51.82 -141.89
REMARK 500 1 PRO A 45 97.47 -33.27
REMARK 500 1 LYS A 47 25.27 -148.89
REMARK 500 1 LEU A 48 -91.94 -73.30
REMARK 500 1 GLU A 49 26.45 44.67
REMARK 500 1 ASP A 50 26.86 -172.35
REMARK 500 1 LYS A 51 -61.35 -146.62
REMARK 500 1 SER A 52 -174.20 55.20
REMARK 500 1 PRO A 53 58.65 -59.14
REMARK 500 1 SER A 55 -172.46 82.03
REMARK 500 1 PRO A 56 2.55 -53.63
REMARK 500 1 LYS A 83 -162.30 -78.61
REMARK 500 1 THR A 97 -78.97 -87.18
REMARK 500 1 ALA A 100 -62.00 -162.91
REMARK 500 1 ASN A 102 -40.70 65.86
REMARK 500 1 GLN A 103 -152.05 -97.66
REMARK 500 1 LYS A 104 120.01 52.80
REMARK 500 2 GLU A 4 -70.15 -85.08
REMARK 500 2 ASN A 6 43.30 -146.63
REMARK 500 2 GLU A 8 -16.48 58.82
REMARK 500 2 THR A 9 25.39 38.48
REMARK 500 2 ASN A 13 -6.43 60.53
REMARK 500 2 GLU A 18 17.32 -147.75
REMARK 500 2 LYS A 19 -88.83 53.41
REMARK 500 2 ALA A 20 88.79 52.01
REMARK 500 2 ASP A 21 -56.87 -148.55
REMARK 500 2 ASN A 22 65.18 -155.28
REMARK 500 2 ALA A 23 -3.17 65.37
REMARK 500 2 GLN A 41 -137.30 -73.73
REMARK 500 2 ALA A 43 -52.02 -139.18
REMARK 500 2 PRO A 45 88.28 -25.76
REMARK 500 2 PRO A 46 -62.42 -90.92
REMARK 500 2 ASP A 50 51.04 -170.26
REMARK 500 2 LYS A 51 -65.54 -140.87
REMARK 500 2 SER A 52 -174.48 52.72
REMARK 500 2 PRO A 53 49.64 -58.22
REMARK 500 2 ASP A 54 -74.73 -107.80
REMARK 500 2 PRO A 56 -0.05 -57.61
REMARK 500
REMARK 500 THIS ENTRY HAS 248 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YZA RELATED DB: PDB
REMARK 900 REDESIGNED APOCYTOCHROME B562 (RD-APOCYT B562) WITH THE N-TERMINAL
REMARK 900 HELIX UNFOLDED
DBREF 1YZC A 1 106 PDB 1YZC 1YZC 1 106
SEQRES 1 A 106 ALA ASP LEU GLU ASP ASN ASP GLU THR GLY ASN ASP ASN
SEQRES 2 A 106 GLY LYS GLY GLY GLU LYS ALA ASP ASN ALA ALA GLN VAL
SEQRES 3 A 106 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP
SEQRES 4 A 106 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER
SEQRES 5 A 106 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE
SEQRES 6 A 106 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU
SEQRES 7 A 106 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA
SEQRES 8 A 106 GLU GLN LEU LYS THR THR GLY ARG ALA GLY ASN GLN LYS
SEQRES 9 A 106 GLY GLY
HELIX 1 1 ALA A 23 GLN A 41 1 19
HELIX 2 2 PRO A 56 GLY A 82 1 27
HELIX 3 3 LYS A 83 GLY A 98 1 16
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 - r 2 2 Bytes