Header list of 1w0a.pdb file
Complete list - y 2 2 Bytes
HEADER CHAPERONE 02-JUN-04 1W0A
TITLE SOLUTION STRUCTURE OF THE TRANS FORM OF THE HUMAN ALPHA-HEMOGLOBIN
TITLE 2 STABILIZING PROTEIN (AHSP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-HEMOGLOBIN STABILIZING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 3-94;
COMPND 5 SYNONYM: ERYTHROID ASSOCIATED FACTOR, ERYTHROID DIFFERENTIATION
COMPND 6 RELATED FACTOR;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: ASP 29-PRO 30 PEPTIDE BOND IN TRANS CONFORMATION
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSET (A)
KEYWDS AHSP NMR STRUCTURE, PROLINE CIS/TRANS ISOMERIZATION, ALPHA-
KEYWDS 2 THALASSAEMIA, ALPHA-HEMOGLOBIN BINDING, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.M.SANTIVERI,J.M.PEREZ-CANADILLAS,M.K.VADIVELU,M.D.ALLEN,
AUTHOR 2 T.J.RUTHERFORD,N.A.WATKINS,M.BYCROFT
REVDAT 5 02-MAY-18 1W0A 1 JRNL REMARK
REVDAT 4 24-JAN-18 1W0A 1 SOURCE
REVDAT 3 24-FEB-09 1W0A 1 VERSN
REVDAT 2 03-MAY-05 1W0A 1 JRNL
REVDAT 1 10-JUN-04 1W0A 0
JRNL AUTH C.M.SANTIVERI,J.M.PEREZ-CANADILLAS,M.K.VADIVELU,M.D.ALLEN,
JRNL AUTH 2 T.J.RUTHERFORD,N.A.WATKINS,M.BYCROFT
JRNL TITL NMR STRUCTURE OF THE ALPHA-HEMOGLOBIN STABILIZING PROTEIN:
JRNL TITL 2 INSIGHTS INTO CONFORMATIONAL HETEROGENEITY AND BINDING.
JRNL REF J. BIOL. CHEM. V. 279 34963 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15178680
JRNL DOI 10.1074/JBC.M405016200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1W0A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1290020099.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0; 298.0
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 120; 120
REMARK 210 PRESSURE : 1.0 ATM; 1.0 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC; HNCO; HNCACO; HNCACB;
REMARK 210 CBCACONH; HCCH-COSY; DQF- COSY;
REMARK 210 TOCSY; NOESY; 3D- 15N-HSQC-NOESY;
REMARK 210 3D-13C-HSQC- NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, ANSIG FOR WINDOWS
REMARK 210 WINDOWS
REMARK 210 METHOD USED : CNS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO DISTANCE VIOLATIONS WERE
REMARK 210 GREATER THAN 0.3 A, NO ANGLE
REMARK 210 VIOLATIONS WERE GREATER THAN 5.0
REMARK 210 DEGREES, AND NO RDC VIOLATIONS
REMARK 210 WERE GREATER THAN 2.5 HZ
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: 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 400
REMARK 400 COMPOUND
REMARK 400 ACTS AS A CHAPERONE TO PREVENT THE HARMFUL AGGREGATION OF
REMARK 400 ALPHA-HEMOGLOBIN DURING NORMAL ERYTHROID CELL DEVELOPMENT.
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 ASP A 29 H LEU A 31 1.55
REMARK 500 O ASP A 29 N LEU A 31 2.07
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 ASN A 28 -88.36 -66.24
REMARK 500 1 PRO A 30 -16.67 -20.66
REMARK 500 1 LEU A 31 -143.22 13.94
REMARK 500 1 GLN A 55 46.35 -105.72
REMARK 500 1 SER A 91 -70.52 -63.17
REMARK 500 1 HIS A 92 61.14 -65.77
REMARK 500 1 GLU A 93 -96.09 -111.10
REMARK 500 2 LEU A 4 -78.76 -66.87
REMARK 500 2 ASN A 28 -68.63 171.89
REMARK 500 2 LEU A 31 -132.38 -138.86
REMARK 500 2 GLU A 93 169.95 71.19
REMARK 500 3 ASN A 28 -50.27 160.42
REMARK 500 3 PRO A 30 -27.60 -38.79
REMARK 500 3 LEU A 31 173.65 38.62
REMARK 500 4 ASN A 28 -76.34 174.84
REMARK 500 4 LEU A 31 -132.11 -139.53
REMARK 500 4 HIS A 92 -77.23 -164.25
REMARK 500 4 GLU A 93 -112.42 167.98
REMARK 500 5 ASN A 28 -84.80 -124.82
REMARK 500 5 PRO A 30 -33.65 -36.22
REMARK 500 5 LEU A 31 -131.98 48.16
REMARK 500 5 SER A 91 -82.41 -61.66
REMARK 500 5 HIS A 92 30.23 37.13
REMARK 500 6 ASN A 28 -98.58 -154.66
REMARK 500 6 LEU A 31 -112.86 52.01
REMARK 500 6 GLN A 55 44.91 -77.78
REMARK 500 6 HIS A 92 61.05 -61.37
REMARK 500 7 LEU A 4 -58.44 69.36
REMARK 500 7 ASN A 28 -76.83 -173.01
REMARK 500 7 PRO A 30 109.07 -42.72
REMARK 500 7 LEU A 31 -150.78 -116.54
REMARK 500 7 VAL A 56 -103.51 -26.26
REMARK 500 8 ASN A 28 -83.41 -62.94
REMARK 500 8 LEU A 31 -103.53 -157.21
REMARK 500 8 GLU A 93 170.06 76.17
REMARK 500 9 ASN A 28 -67.56 -163.31
REMARK 500 9 PRO A 30 -82.70 -28.91
REMARK 500 9 LEU A 31 -170.32 74.09
REMARK 500 9 GLN A 55 56.73 -117.66
REMARK 500 9 HIS A 92 -140.82 87.31
REMARK 500 10 ASN A 28 -46.14 -164.10
REMARK 500 10 PRO A 30 -15.51 -47.59
REMARK 500 10 LEU A 31 -174.66 30.83
REMARK 500 10 HIS A 92 -148.10 -93.87
REMARK 500 10 GLU A 93 85.04 69.51
REMARK 500 11 ASN A 28 -83.30 -55.57
REMARK 500 11 PRO A 30 -9.99 -40.49
REMARK 500 11 LEU A 31 -119.62 6.51
REMARK 500 11 GLN A 55 48.95 -106.23
REMARK 500 11 HIS A 92 91.84 -53.17
REMARK 500
REMARK 500 THIS ENTRY HAS 104 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1W09 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE CIS FORM OF THE HUMAN ALPHA-HEMOGLOBIN
REMARK 900 STABILIZING PROTEIN (AHSP)
REMARK 900 RELATED ID: 1W0B RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING
REMARK 900 PROTEIN (AHSP) P30A MUTANT
DBREF 1W0A A 3 94 UNP Q9NZD4 AHSP_HUMAN 3 94
SEQRES 1 A 92 LEU LEU LYS ALA ASN LYS ASP LEU ILE SER ALA GLY LEU
SEQRES 2 A 92 LYS GLU PHE SER VAL LEU LEU ASN GLN GLN VAL PHE ASN
SEQRES 3 A 92 ASP PRO LEU VAL SER GLU GLU ASP MET VAL THR VAL VAL
SEQRES 4 A 92 GLU ASP TRP MET ASN PHE TYR ILE ASN TYR TYR ARG GLN
SEQRES 5 A 92 GLN VAL THR GLY GLU PRO GLN GLU ARG ASP LYS ALA LEU
SEQRES 6 A 92 GLN GLU LEU ARG GLN GLU LEU ASN THR LEU ALA ASN PRO
SEQRES 7 A 92 PHE LEU ALA LYS TYR ARG ASP PHE LEU LYS SER HIS GLU
SEQRES 8 A 92 LEU
HELIX 1 1 LEU A 4 GLN A 24 1 21
HELIX 2 2 SER A 33 GLN A 54 1 22
HELIX 3 3 GLU A 59 HIS A 92 1 34
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 - y 2 2 Bytes