Header list of 1w0b.pdb file
Complete list - y 2 2 Bytes
HEADER CHAPERONE 02-JUN-04 1W0B TITLE SOLUTION STRUCTURE OF THE HUMAN ALPHA-HEMOGLOBIN STABILIZING PROTEIN TITLE 2 (AHSP) P30A MUTANT COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-HEMOGLOBIN STABILIZING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ERYTHROID ASSOCIATED FACTOR, ERYTHROID DIFFERENTIATION COMPND 5 RELATED FACTOR; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 OTHER_DETAILS: PRO 30 OF HUMAN AHSP HAS BEEN MUTATED TO ALA 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 CHAPERONE, AHSP P30A MUTANT NMR STRUCTURE, PROLINE CIS/TRANS KEYWDS 2 ISOMERIZATION, ALPHA-THALASSAEMIA, ALPHA-HEMOGLOBIN BINDING 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 1W0B 1 JRNL REMARK REVDAT 4 24-JAN-18 1W0B 1 SOURCE REVDAT 3 24-FEB-09 1W0B 1 VERSN REVDAT 2 03-MAY-05 1W0B 1 JRNL REVDAT 1 10-JUN-04 1W0B 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 1W0B 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_1290020100. 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; HNCA; HNCOCA; CBCACONH; REMARK 210 DQF-COSY; TOCSY; NOESY; 3D-15N- REMARK 210 HSQC-NOESY; 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 ENGINEERED MUTATION IN CHAIN A, PRO 30 TO ALA REMARK 400 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 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 ALA A 2 -64.94 75.74 REMARK 500 1 LEU A 3 95.74 179.97 REMARK 500 1 GLN A 24 11.83 -60.75 REMARK 500 1 VAL A 26 50.00 -106.14 REMARK 500 1 PHE A 27 92.99 -63.42 REMARK 500 1 ASN A 28 -52.30 -161.16 REMARK 500 1 VAL A 32 155.05 84.25 REMARK 500 1 GLN A 55 38.65 -96.76 REMARK 500 1 GLU A 93 -10.22 94.73 REMARK 500 1 LEU A 94 106.94 178.45 REMARK 500 1 PRO A 95 67.02 -67.90 REMARK 500 1 HIS A 97 -35.44 166.77 REMARK 500 1 PRO A 100 86.71 -55.34 REMARK 500 1 SER A 101 -78.03 -163.80 REMARK 500 2 ALA A 2 25.45 -163.30 REMARK 500 2 LEU A 3 97.11 -39.24 REMARK 500 2 ASN A 28 -57.16 -153.06 REMARK 500 2 GLN A 55 43.45 -89.95 REMARK 500 2 LEU A 94 73.22 -106.36 REMARK 500 2 PRO A 100 -165.96 -79.32 REMARK 500 3 ALA A 2 82.16 65.46 REMARK 500 3 LEU A 3 119.44 -162.81 REMARK 500 3 GLN A 24 45.17 -83.03 REMARK 500 3 PHE A 27 86.08 -61.93 REMARK 500 3 ASN A 28 -20.60 178.63 REMARK 500 3 LEU A 31 148.23 -173.86 REMARK 500 3 VAL A 32 170.80 100.33 REMARK 500 3 GLN A 55 48.57 -72.42 REMARK 500 3 LEU A 94 85.84 -153.17 REMARK 500 3 HIS A 97 102.99 172.46 REMARK 500 3 PRO A 98 101.30 -44.03 REMARK 500 4 LEU A 3 -8.43 156.65 REMARK 500 4 LEU A 4 71.35 72.58 REMARK 500 4 VAL A 26 50.80 -103.21 REMARK 500 4 ASN A 28 -44.04 179.64 REMARK 500 4 LEU A 31 -50.64 -124.31 REMARK 500 4 VAL A 56 -83.99 -94.96 REMARK 500 4 THR A 57 7.62 90.64 REMARK 500 4 SER A 101 87.58 -170.15 REMARK 500 5 LEU A 3 88.34 -29.91 REMARK 500 5 LEU A 4 104.56 45.37 REMARK 500 5 GLN A 24 14.21 -61.51 REMARK 500 5 VAL A 26 50.65 -101.99 REMARK 500 5 PHE A 27 90.39 -62.82 REMARK 500 5 ASN A 28 -57.92 -156.96 REMARK 500 5 LEU A 31 50.40 -113.30 REMARK 500 5 VAL A 32 -86.48 -144.45 REMARK 500 5 SER A 33 137.04 176.90 REMARK 500 5 GLU A 59 121.18 157.11 REMARK 500 5 GLU A 93 167.68 82.45 REMARK 500 REMARK 500 THIS ENTRY HAS 234 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: 1W0A RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE TRANS FORM OF THE HUMAN ALPHA-HEMOGLOBIN REMARK 900 STABILIZING PROTEIN (AHSP) DBREF 1W0B A 1 102 UNP Q9NZD4 AHSP_HUMAN 1 102 SEQADV 1W0B ALA A 30 UNP Q9NZD4 PRO 30 ENGINEERED MUTATION SEQRES 1 A 102 SER ALA LEU LEU LYS ALA ASN LYS ASP LEU ILE SER ALA SEQRES 2 A 102 GLY LEU LYS GLU PHE SER VAL LEU LEU ASN GLN GLN VAL SEQRES 3 A 102 PHE ASN ASP ALA LEU VAL SER GLU GLU ASP MET VAL THR SEQRES 4 A 102 VAL VAL GLU ASP TRP MET ASN PHE TYR ILE ASN TYR TYR SEQRES 5 A 102 ARG GLN GLN VAL THR GLY GLU PRO GLN GLU ARG ASP LYS SEQRES 6 A 102 ALA LEU GLN GLU LEU ARG GLN GLU LEU ASN THR LEU ALA SEQRES 7 A 102 ASN PRO PHE LEU ALA LYS TYR ARG ASP PHE LEU LYS SER SEQRES 8 A 102 HIS GLU LEU PRO SER HIS PRO PRO PRO SER SER HELIX 1 1 LEU A 4 GLN A 24 1 21 HELIX 2 2 SER A 33 GLN A 55 1 23 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