Header list of 2go0.pdb file
Complete list - b 26 2 Bytes
HEADER PROTEIN BINDING 12-APR-06 2GO0 TITLE NMR SOLUTION STRUCTURE OF HUMAN PANCREATITIS-ASSOCIATED PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: REGENERATING ISLET-DERIVED PROTEIN 3 ALPHA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-137; COMPND 5 SYNONYM: REG III-ALPHA, PANCREATITIS-ASSOCIATED PROTEIN 1; COMPND 6 ENGINEERED: 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 KEYWDS C-TYPE LECTIN, FIBRIL, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.P.CHEN,M.R.HO,Y.C.LOU REVDAT 3 26-FEB-20 2GO0 1 REMARK REVDAT 2 24-FEB-09 2GO0 1 VERSN REVDAT 1 12-SEP-06 2GO0 0 JRNL AUTH M.R.HO,Y.C.LOU,W.C.LIN,P.C.LYU,C.P.CHEN JRNL TITL HUMAN PANCREATITIS-ASSOCIATED PROTEIN FORMS FIBRILLAR JRNL TITL 2 AGGREGATE WITH NATIVE-LIKE CONFORMATION. JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, X-PLOR 2.9.4A REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2GO0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-APR-06. REMARK 100 THE DEPOSITION ID IS D_1000037346. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 4 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.5MM HUMAN PANCREATITIS REMARK 210 -ASSOCIATED PROTEIN U-15N,13C; REMARK 210 20MM PHOSPHATE AND 50MM NACL REMARK 210 BUFFER; 90% H2O, 10% D2O; 1.5MM REMARK 210 HUMAN PANCREATITIS-ASSOCIATED REMARK 210 PROTEIN U-15N,13C; 20MM REMARK 210 PHOSPHATE AND 50MM NACL BUFFER; REMARK 210 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 5.0, AURELIA 3.1.6, X REMARK 210 -PLOR 2.9.4A, XWINNMR 3.5 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 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 HG SER A 22 H THR A 24 1.25 REMARK 500 O SER A 103 HG SER A 104 1.46 REMARK 500 HE1 TRP A 65 O VAL A 127 1.48 REMARK 500 HE1 TRP A 84 O VAL A 89 1.57 REMARK 500 O GLU A 76 H ASN A 78 1.57 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 11 37.89 -172.51 REMARK 500 1 LEU A 18 11.97 -69.95 REMARK 500 1 SER A 22 152.25 -46.22 REMARK 500 1 LYS A 32 0.02 -65.17 REMARK 500 1 PRO A 34 83.82 -46.86 REMARK 500 1 ASN A 37 148.29 164.57 REMARK 500 1 LEU A 38 134.02 -23.77 REMARK 500 1 VAL A 39 154.50 -35.47 REMARK 500 1 VAL A 41 85.92 -162.65 REMARK 500 1 SER A 60 9.10 -65.14 REMARK 500 1 THR A 75 -60.50 -151.97 REMARK 500 1 GLU A 76 108.46 -43.65 REMARK 500 1 PRO A 77 33.22 -63.16 REMARK 500 1 ASN A 78 -45.91 -158.91 REMARK 500 1 GLU A 80 39.17 -152.07 REMARK 500 1 TRP A 82 104.27 49.59 REMARK 500 1 SER A 86 10.44 -140.93 REMARK 500 1 SER A 87 -52.05 -121.08 REMARK 500 1 ASP A 88 -110.91 148.86 REMARK 500 1 MET A 90 87.34 -63.27 REMARK 500 1 ALA A 94 26.32 -175.03 REMARK 500 1 SER A 103 76.40 -60.41 REMARK 500 1 SER A 104 87.97 45.97 REMARK 500 1 PRO A 105 -156.31 -66.25 REMARK 500 1 CYS A 125 -6.34 -48.41 REMARK 500 1 PHE A 135 119.11 -177.27 REMARK 500 1 THR A 136 -143.51 -79.52 REMARK 500 2 SER A 11 26.84 178.20 REMARK 500 2 PRO A 34 82.59 -46.69 REMARK 500 2 ASN A 37 141.58 164.88 REMARK 500 2 LEU A 38 136.19 -20.88 REMARK 500 2 VAL A 39 152.75 -39.70 REMARK 500 2 VAL A 41 89.34 -164.69 REMARK 500 2 SER A 60 10.84 -66.27 REMARK 500 2 GLN A 73 12.61 47.69 REMARK 500 2 THR A 75 20.82 -149.24 REMARK 500 2 PRO A 77 38.28 -63.77 REMARK 500 2 ASN A 78 -53.79 -144.24 REMARK 500 2 GLU A 80 27.72 -150.84 REMARK 500 2 TRP A 82 92.83 40.26 REMARK 500 2 SER A 87 -53.45 -121.65 REMARK 500 2 ASP A 88 -103.32 150.45 REMARK 500 2 MET A 90 85.24 -62.75 REMARK 500 2 ALA A 94 22.59 -168.70 REMARK 500 2 SER A 104 87.36 45.73 REMARK 500 2 CYS A 125 -5.18 -49.38 REMARK 500 2 PHE A 135 125.59 -179.60 REMARK 500 3 TYR A 9 131.54 -171.33 REMARK 500 3 SER A 11 35.76 -175.99 REMARK 500 3 PRO A 34 82.80 -47.06 REMARK 500 REMARK 500 THIS ENTRY HAS 449 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 1 0.20 SIDE CHAIN REMARK 500 1 ARG A 33 0.31 SIDE CHAIN REMARK 500 1 ARG A 97 0.23 SIDE CHAIN REMARK 500 1 ARG A 113 0.19 SIDE CHAIN REMARK 500 1 ARG A 119 0.30 SIDE CHAIN REMARK 500 1 ARG A 128 0.24 SIDE CHAIN REMARK 500 2 ARG A 1 0.26 SIDE CHAIN REMARK 500 2 ARG A 33 0.30 SIDE CHAIN REMARK 500 2 ARG A 113 0.31 SIDE CHAIN REMARK 500 2 ARG A 119 0.28 SIDE CHAIN REMARK 500 2 ARG A 128 0.31 SIDE CHAIN REMARK 500 3 ARG A 1 0.19 SIDE CHAIN REMARK 500 3 ARG A 33 0.31 SIDE CHAIN REMARK 500 3 ARG A 97 0.08 SIDE CHAIN REMARK 500 3 ARG A 113 0.29 SIDE CHAIN REMARK 500 3 ARG A 119 0.30 SIDE CHAIN REMARK 500 3 ARG A 128 0.09 SIDE CHAIN REMARK 500 4 ARG A 1 0.29 SIDE CHAIN REMARK 500 4 ARG A 33 0.26 SIDE CHAIN REMARK 500 4 ARG A 97 0.27 SIDE CHAIN REMARK 500 4 ARG A 113 0.32 SIDE CHAIN REMARK 500 4 ARG A 119 0.15 SIDE CHAIN REMARK 500 4 ARG A 128 0.13 SIDE CHAIN REMARK 500 5 ARG A 1 0.31 SIDE CHAIN REMARK 500 5 ARG A 33 0.26 SIDE CHAIN REMARK 500 5 ARG A 119 0.23 SIDE CHAIN REMARK 500 5 ARG A 128 0.21 SIDE CHAIN REMARK 500 6 ARG A 1 0.15 SIDE CHAIN REMARK 500 6 ARG A 33 0.27 SIDE CHAIN REMARK 500 6 ARG A 113 0.32 SIDE CHAIN REMARK 500 6 ARG A 119 0.08 SIDE CHAIN REMARK 500 6 ARG A 128 0.31 SIDE CHAIN REMARK 500 7 ARG A 1 0.27 SIDE CHAIN REMARK 500 7 ARG A 33 0.23 SIDE CHAIN REMARK 500 7 ARG A 113 0.31 SIDE CHAIN REMARK 500 7 ARG A 119 0.31 SIDE CHAIN REMARK 500 7 ARG A 128 0.18 SIDE CHAIN REMARK 500 8 ARG A 1 0.21 SIDE CHAIN REMARK 500 8 ARG A 33 0.29 SIDE CHAIN REMARK 500 8 ARG A 97 0.25 SIDE CHAIN REMARK 500 8 ARG A 113 0.17 SIDE CHAIN REMARK 500 8 ARG A 119 0.27 SIDE CHAIN REMARK 500 9 ARG A 1 0.31 SIDE CHAIN REMARK 500 9 ARG A 33 0.17 SIDE CHAIN REMARK 500 9 ARG A 97 0.31 SIDE CHAIN REMARK 500 9 ARG A 113 0.18 SIDE CHAIN REMARK 500 9 ARG A 119 0.23 SIDE CHAIN REMARK 500 9 ARG A 128 0.18 SIDE CHAIN REMARK 500 10 ARG A 1 0.25 SIDE CHAIN REMARK 500 10 ARG A 33 0.29 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 105 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6231 RELATED DB: BMRB REMARK 900 NMR RESONANCE ASSIGNMENT OF HUMAN PANCREATITIS-ASSOCIATED PROTEIN. DBREF 2GO0 A 1 137 UNP Q06141 REG3A_HUMAN 39 175 SEQRES 1 A 137 ARG CYS PRO LYS GLY SER LYS ALA TYR GLY SER HIS CYS SEQRES 2 A 137 TYR ALA LEU PHE LEU SER PRO LYS SER TRP THR ASP ALA SEQRES 3 A 137 ASP LEU ALA CYS GLN LYS ARG PRO SER GLY ASN LEU VAL SEQRES 4 A 137 SER VAL LEU SER GLY ALA GLU GLY SER PHE VAL SER SER SEQRES 5 A 137 LEU VAL LYS SER ILE GLY ASN SER TYR SER TYR VAL TRP SEQRES 6 A 137 ILE GLY LEU HIS ASP PRO THR GLN GLY THR GLU PRO ASN SEQRES 7 A 137 GLY GLU GLY TRP GLU TRP SER SER SER ASP VAL MET ASN SEQRES 8 A 137 TYR PHE ALA TRP GLU ARG ASN PRO SER THR ILE SER SER SEQRES 9 A 137 PRO GLY HIS CYS ALA SER LEU SER ARG SER THR ALA PHE SEQRES 10 A 137 LEU ARG TRP LYS ASP TYR ASN CYS ASN VAL ARG LEU PRO SEQRES 11 A 137 TYR VAL CYS LYS PHE THR ASP HELIX 1 1 TRP A 23 LYS A 32 1 10 HELIX 2 2 SER A 43 VAL A 54 1 12 HELIX 3 3 SER A 114 ALA A 116 5 3 SHEET 1 A 4 LYS A 7 TYR A 9 0 SHEET 2 A 4 HIS A 12 SER A 22 -1 O TYR A 14 N LYS A 7 SHEET 3 A 4 ARG A 128 PHE A 135 -1 O TYR A 131 N PHE A 17 SHEET 4 A 4 ASN A 37 LEU A 38 -1 N ASN A 37 O LYS A 134 SHEET 1 B 4 GLU A 83 TRP A 84 0 SHEET 2 B 4 TYR A 63 HIS A 69 -1 N HIS A 69 O GLU A 83 SHEET 3 B 4 CYS A 108 SER A 112 -1 O LEU A 111 N VAL A 64 SHEET 4 B 4 TRP A 120 ASP A 122 -1 O LYS A 121 N SER A 110 SSBOND 1 CYS A 2 CYS A 13 1555 1555 2.02 SSBOND 2 CYS A 30 CYS A 133 1555 1555 2.02 SSBOND 3 CYS A 108 CYS A 125 1555 1555 2.02 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 26 2 Bytes