Header list of 1ah2.pdb file
Complete list - b 16 2 Bytes
HEADER SERINE PROTEASE 11-APR-97 1AH2 TITLE SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: SERINE PROTEASE PB92; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: INHIBITED BY DFP SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ALCALOPHILUS; SOURCE 3 ORGANISM_TAXID: 1445; SOURCE 4 STRAIN: PB92; SOURCE 5 EXPRESSION_SYSTEM: BACILLUS SUBTILIS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1423 KEYWDS SERINE PROTEASE, SUBTILASE, INDUSTRIAL ENZYME, MAXACAL(TM), KEYWDS 2 APPLICATION IN WASHING POWDERS EXPDTA SOLUTION NMR NUMMDL 18 AUTHOR R.BOELENS,D.SCHIPPER,J.R.MARTIN,Y.KARIMI-NEJAD,F.MULDER,J.V.D.ZWAN, AUTHOR 2 M.MARIANI REVDAT 4 16-FEB-22 1AH2 1 REMARK REVDAT 3 24-FEB-09 1AH2 1 VERSN REVDAT 2 01-APR-03 1AH2 1 JRNL REVDAT 1 15-APR-98 1AH2 0 JRNL AUTH J.R.MARTIN,F.A.MULDER,Y.KARIMI-NEJAD,J.VAN DER ZWAN, JRNL AUTH 2 M.MARIANI,D.SCHIPPER,R.BOELENS JRNL TITL THE SOLUTION STRUCTURE OF SERINE PROTEASE PB92 FROM BACILLUS JRNL TITL 2 ALCALOPHILUS PRESENTS A RIGID FOLD WITH A FLEXIBLE JRNL TITL 3 SUBSTRATE-BINDING SITE. JRNL REF STRUCTURE V. 5 521 1997 JRNL REFN ISSN 0969-2126 JRNL PMID 9115441 JRNL DOI 10.1016/S0969-2126(97)00208-6 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.H.FOGH,D.SCHIPPER,R.BOELENS,R.KAPTEIN REMARK 1 TITL COMPLETE 1H, 13C AND 15N NMR ASSIGNMENTS AND SECONDARY REMARK 1 TITL 2 STRUCTURE OF THE 269-RESIDUE SERINE PROTEASE PB92 FROM REMARK 1 TITL 3 BACILLUS ALCALOPHILUS REMARK 1 REF J.BIOMOL.NMR V. 5 259 1995 REMARK 1 REFN ISSN 0925-2738 REMARK 1 REFERENCE 2 REMARK 1 AUTH R.FOGH,D.SCHIPPER,R.BOELENS,R.KAPTEIN REMARK 1 TITL 1H, 13C AND 15N ASSIGNMENTS OF SERINE PROTEASE PB92 FROM REMARK 1 TITL 2 BACILLUS ALCALOPHILUS REMARK 1 REF J.BIOMOL.NMR V. 4 123 1994 REMARK 1 REFN ISSN 0925-2738 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL REFERENCE. REMARK 4 REMARK 4 1AH2 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_1000170806. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 315 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N NOESY-HSQC; 3D 13C NOESY REMARK 210 -HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS 750 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.1 REMARK 210 METHOD USED : DGSA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18 REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE AND H-BOND VIOLATIONS > REMARK 210 0.5 A 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: 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 PRO A 162 N ARG A 164 2.19 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 GLN A 12 45.81 39.91 REMARK 500 1 LEU A 31 95.74 -65.27 REMARK 500 1 ASP A 32 -144.72 -144.93 REMARK 500 1 THR A 33 27.78 -145.04 REMARK 500 1 SER A 36 126.36 51.84 REMARK 500 1 PRO A 51 -168.27 -66.63 REMARK 500 1 SER A 55 137.59 -175.11 REMARK 500 1 ASP A 58 157.47 83.31 REMARK 500 1 ASN A 60 -83.83 -145.22 REMARK 500 1 ALA A 71 41.09 -170.13 REMARK 500 1 LEU A 73 151.91 -43.74 REMARK 500 1 ASN A 74 64.57 -105.69 REMARK 500 1 SER A 76 -34.47 91.18 REMARK 500 1 ASN A 85 -87.64 -113.92 REMARK 500 1 ALA A 86 170.77 59.80 REMARK 500 1 LYS A 92 89.80 -51.88 REMARK 500 1 SER A 99 101.15 -179.80 REMARK 500 1 ASN A 114 -61.70 -101.95 REMARK 500 1 ASN A 115 40.77 -104.16 REMARK 500 1 MET A 117 -166.04 41.14 REMARK 500 1 SER A 130 132.78 -170.69 REMARK 500 1 SER A 151 -85.09 -91.95 REMARK 500 1 ASN A 153 34.51 177.72 REMARK 500 1 SER A 154 102.12 87.06 REMARK 500 1 ALA A 156 171.42 66.07 REMARK 500 1 ALA A 163 -76.95 27.29 REMARK 500 1 TYR A 165 -164.66 -120.02 REMARK 500 1 ALA A 166 26.16 85.98 REMARK 500 1 ASP A 175 -142.46 -108.41 REMARK 500 1 ASN A 177 -60.93 -122.16 REMARK 500 1 ASN A 179 164.83 -47.17 REMARK 500 1 ALA A 181 -154.25 -55.72 REMARK 500 1 ASN A 198 124.79 127.36 REMARK 500 1 VAL A 199 105.37 -160.33 REMARK 500 1 SER A 201 -157.09 -149.05 REMARK 500 1 THR A 249 169.05 -45.93 REMARK 500 1 SER A 253 -179.20 58.17 REMARK 500 1 ASN A 255 -28.13 -175.48 REMARK 500 1 TYR A 257 -77.43 -88.78 REMARK 500 1 SER A 259 103.53 61.37 REMARK 500 2 ILE A 8 -50.97 -151.55 REMARK 500 2 VAL A 30 78.65 -115.14 REMARK 500 2 ASP A 32 -72.54 -175.75 REMARK 500 2 THR A 33 -73.59 -141.97 REMARK 500 2 ILE A 35 98.82 -170.82 REMARK 500 2 ARG A 44 -39.47 -152.69 REMARK 500 2 PRO A 51 -159.64 -86.23 REMARK 500 2 GLU A 53 62.52 174.44 REMARK 500 2 PRO A 54 -90.20 -81.85 REMARK 500 2 ASP A 58 148.26 65.47 REMARK 500 REMARK 500 THIS ENTRY HAS 807 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 10 0.30 SIDE CHAIN REMARK 500 1 ARG A 19 0.13 SIDE CHAIN REMARK 500 1 ARG A 44 0.27 SIDE CHAIN REMARK 500 1 ARG A 143 0.14 SIDE CHAIN REMARK 500 1 ARG A 164 0.27 SIDE CHAIN REMARK 500 1 ARG A 180 0.31 SIDE CHAIN REMARK 500 1 ARG A 241 0.19 SIDE CHAIN REMARK 500 1 ARG A 269 0.20 SIDE CHAIN REMARK 500 2 ARG A 10 0.15 SIDE CHAIN REMARK 500 2 ARG A 44 0.22 SIDE CHAIN REMARK 500 2 ARG A 143 0.29 SIDE CHAIN REMARK 500 2 ARG A 164 0.16 SIDE CHAIN REMARK 500 2 ARG A 180 0.15 SIDE CHAIN REMARK 500 2 ARG A 241 0.31 SIDE CHAIN REMARK 500 3 ARG A 10 0.16 SIDE CHAIN REMARK 500 3 ARG A 19 0.32 SIDE CHAIN REMARK 500 3 ARG A 44 0.32 SIDE CHAIN REMARK 500 3 ARG A 143 0.30 SIDE CHAIN REMARK 500 3 ARG A 164 0.15 SIDE CHAIN REMARK 500 3 ARG A 180 0.19 SIDE CHAIN REMARK 500 3 ARG A 269 0.12 SIDE CHAIN REMARK 500 4 ARG A 19 0.24 SIDE CHAIN REMARK 500 4 ARG A 143 0.30 SIDE CHAIN REMARK 500 4 ARG A 164 0.19 SIDE CHAIN REMARK 500 4 ARG A 180 0.12 SIDE CHAIN REMARK 500 4 ARG A 241 0.31 SIDE CHAIN REMARK 500 4 ARG A 269 0.28 SIDE CHAIN REMARK 500 5 ARG A 10 0.32 SIDE CHAIN REMARK 500 5 ARG A 19 0.31 SIDE CHAIN REMARK 500 5 ARG A 44 0.32 SIDE CHAIN REMARK 500 5 ARG A 143 0.32 SIDE CHAIN REMARK 500 5 ARG A 164 0.09 SIDE CHAIN REMARK 500 5 ARG A 180 0.18 SIDE CHAIN REMARK 500 5 ARG A 241 0.14 SIDE CHAIN REMARK 500 5 ARG A 269 0.22 SIDE CHAIN REMARK 500 6 ARG A 10 0.25 SIDE CHAIN REMARK 500 6 ARG A 19 0.28 SIDE CHAIN REMARK 500 6 ARG A 44 0.30 SIDE CHAIN REMARK 500 6 ARG A 164 0.14 SIDE CHAIN REMARK 500 6 ARG A 180 0.28 SIDE CHAIN REMARK 500 6 ARG A 241 0.31 SIDE CHAIN REMARK 500 6 ARG A 269 0.30 SIDE CHAIN REMARK 500 7 ARG A 10 0.18 SIDE CHAIN REMARK 500 7 ARG A 19 0.32 SIDE CHAIN REMARK 500 7 ARG A 143 0.30 SIDE CHAIN REMARK 500 7 ARG A 241 0.26 SIDE CHAIN REMARK 500 7 ARG A 269 0.32 SIDE CHAIN REMARK 500 8 ARG A 10 0.21 SIDE CHAIN REMARK 500 8 ARG A 19 0.28 SIDE CHAIN REMARK 500 8 ARG A 44 0.30 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 133 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CIC REMARK 800 EVIDENCE_CODE: UNKNOWN REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD. DBREF 1AH2 A 1 269 UNP P27693 ELYA_BACAO 112 380 SEQRES 1 A 269 ALA GLN SER VAL PRO TRP GLY ILE SER ARG VAL GLN ALA SEQRES 2 A 269 PRO ALA ALA HIS ASN ARG GLY LEU THR GLY SER GLY VAL SEQRES 3 A 269 LYS VAL ALA VAL LEU ASP THR GLY ILE SER THR HIS PRO SEQRES 4 A 269 ASP LEU ASN ILE ARG GLY GLY ALA SER PHE VAL PRO GLY SEQRES 5 A 269 GLU PRO SER THR GLN ASP GLY ASN GLY HIS GLY THR HIS SEQRES 6 A 269 VAL ALA GLY THR ILE ALA ALA LEU ASN ASN SER ILE GLY SEQRES 7 A 269 VAL LEU GLY VAL ALA PRO ASN ALA GLU LEU TYR ALA VAL SEQRES 8 A 269 LYS VAL LEU GLY ALA SER GLY SER GLY SER VAL SER SER SEQRES 9 A 269 ILE ALA GLN GLY LEU GLU TRP ALA GLY ASN ASN GLY MET SEQRES 10 A 269 HIS VAL ALA ASN LEU SER LEU GLY SER PRO SER PRO SER SEQRES 11 A 269 ALA THR LEU GLU GLN ALA VAL ASN SER ALA THR SER ARG SEQRES 12 A 269 GLY VAL LEU VAL VAL ALA ALA SER GLY ASN SER GLY ALA SEQRES 13 A 269 GLY SER ILE SER TYR PRO ALA ARG TYR ALA ASN ALA MET SEQRES 14 A 269 ALA VAL GLY ALA THR ASP GLN ASN ASN ASN ARG ALA SER SEQRES 15 A 269 PHE SER GLN TYR GLY ALA GLY LEU ASP ILE VAL ALA PRO SEQRES 16 A 269 GLY VAL ASN VAL GLN SER THR TYR PRO GLY SER THR TYR SEQRES 17 A 269 ALA SER LEU ASN GLY THR SER MET ALA THR PRO HIS VAL SEQRES 18 A 269 ALA GLY ALA ALA ALA LEU VAL LYS GLN LYS ASN PRO SER SEQRES 19 A 269 TRP SER ASN VAL GLN ILE ARG ASN HIS LEU LYS ASN THR SEQRES 20 A 269 ALA THR SER LEU GLY SER THR ASN LEU TYR GLY SER GLY SEQRES 21 A 269 LEU VAL ASN ALA GLU ALA ALA THR ARG HELIX 1 1 ALA A 13 ASN A 18 1 6 HELIX 2 2 HIS A 62 ALA A 71 1 10 HELIX 3 3 VAL A 102 ASN A 114 1 13 HELIX 4 4 ALA A 131 THR A 141 1 11 HELIX 5 5 THR A 214 LYS A 231 1 18 HELIX 6 6 ASN A 237 THR A 247 1 11 HELIX 7 7 GLU A 265 THR A 268 1 4 SHEET 1 A 7 ILE A 43 SER A 48 0 SHEET 2 A 7 GLU A 87 LYS A 92 1 SHEET 3 A 7 LYS A 27 LEU A 31 1 SHEET 4 A 7 VAL A 119 LEU A 122 1 SHEET 5 A 7 LEU A 146 ALA A 149 1 SHEET 6 A 7 ALA A 168 THR A 174 1 SHEET 7 A 7 ILE A 192 PRO A 195 1 SHEET 1 B 2 VAL A 199 TYR A 203 0 SHEET 2 B 2 THR A 207 LEU A 211 -1 CISPEP 1 TYR A 161 PRO A 162 1 3.97 CISPEP 2 TYR A 161 PRO A 162 2 4.29 CISPEP 3 TYR A 161 PRO A 162 3 2.99 CISPEP 4 TYR A 161 PRO A 162 4 3.93 CISPEP 5 TYR A 161 PRO A 162 5 3.81 CISPEP 6 TYR A 161 PRO A 162 6 3.58 CISPEP 7 TYR A 161 PRO A 162 7 3.66 CISPEP 8 TYR A 161 PRO A 162 8 3.18 CISPEP 9 TYR A 161 PRO A 162 9 4.08 CISPEP 10 TYR A 161 PRO A 162 10 4.01 CISPEP 11 TYR A 161 PRO A 162 11 4.24 CISPEP 12 TYR A 161 PRO A 162 12 3.78 CISPEP 13 TYR A 161 PRO A 162 13 3.06 CISPEP 14 TYR A 161 PRO A 162 14 3.71 CISPEP 15 TYR A 161 PRO A 162 15 3.68 CISPEP 16 TYR A 161 PRO A 162 16 3.42 CISPEP 17 TYR A 161 PRO A 162 17 3.48 CISPEP 18 TYR A 161 PRO A 162 18 4.78 SITE 1 CIC 3 ASP A 32 HIS A 62 SER A 215 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 16 2 Bytes