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HEADER HYDROLASE 24-JUN-24 9IJK
TITLE THE CRYOEM STRUCTURE OF A C-C BOND HYDROLASE MHPC HOMOTETRAMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXY-6-OXONONADIENEDIOATE/2-HYDROXY-6-
COMPND 3 OXONONATRIENEDIOATE HYDROLASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: 2-HYDROXY-6-KETONONA-2,4-DIENE-1,9-DIOIC ACID 5,6-HYDROLASE,
COMPND 6 2-HYDROXY-6-OXONONA-2,4,7-TRIENE-1;
COMPND 7 EC: 3.7.1.14;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: MHPC, B0349, JW0340;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS C-C BOND HYDROLASE, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR W.X.JIANG,X.Q.CHENG,L.X.MA,Q.XING
REVDAT 1 02-JUL-25 9IJK 0
JRNL AUTH W.X.JIANG,X.Q.CHENG,L.X.MA,Q.XING
JRNL TITL THE CRYOEM STRUCTURE OF A C-C BOND HYDROLASE MHPC
JRNL TITL 2 HOMOTETRAMER
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 4.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.000
REMARK 3 NUMBER OF PARTICLES : 29135
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 9IJK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 27-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1300048926.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : HOMOTETRAMER OF A C-C BOND
REMARK 245 HYDROLASE MHPC
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : DIFFRACTION
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 3300.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 IN SAME ASYMMETRIC UNIT
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 SER D 85 ND2 ASN D 213 2.15
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 SER A 114 -120.63 53.99
REMARK 500 SER B 114 -124.26 52.79
REMARK 500 SER C 114 -122.45 57.97
REMARK 500 SER D 114 -122.32 55.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-60635 RELATED DB: EMDB
REMARK 900 THE CRYOEM STRUCTURE OF A C-C BOND HYDROLASE MHPC HOMOTETRAMER
DBREF 9IJK A 1 288 UNP P77044 MHPC_ECOLI 1 288
DBREF 9IJK B 1 288 UNP P77044 MHPC_ECOLI 1 288
DBREF 9IJK C 1 288 UNP P77044 MHPC_ECOLI 1 288
DBREF 9IJK D 1 288 UNP P77044 MHPC_ECOLI 1 288
SEQRES 1 A 288 MET SER TYR GLN PRO GLN THR GLU ALA ALA THR SER ARG
SEQRES 2 A 288 PHE LEU ASN VAL GLU GLU ALA GLY LYS THR LEU ARG ILE
SEQRES 3 A 288 HIS PHE ASN ASP CYS GLY GLN GLY ASP GLU THR VAL VAL
SEQRES 4 A 288 LEU LEU HIS GLY SER GLY PRO GLY ALA THR GLY TRP ALA
SEQRES 5 A 288 ASN PHE SER ARG ASN ILE ASP PRO LEU VAL GLU ALA GLY
SEQRES 6 A 288 TYR ARG VAL ILE LEU LEU ASP CYS PRO GLY TRP GLY LYS
SEQRES 7 A 288 SER ASP SER VAL VAL ASN SER GLY SER ARG SER ASP LEU
SEQRES 8 A 288 ASN ALA ARG ILE LEU LYS SER VAL VAL ASP GLN LEU ASP
SEQRES 9 A 288 ILE ALA LYS ILE HIS LEU LEU GLY ASN SER MET GLY GLY
SEQRES 10 A 288 HIS SER SER VAL ALA PHE THR LEU LYS TRP PRO GLU ARG
SEQRES 11 A 288 VAL GLY LYS LEU VAL LEU MET GLY GLY GLY THR GLY GLY
SEQRES 12 A 288 MET SER LEU PHE THR PRO MET PRO THR GLU GLY ILE LYS
SEQRES 13 A 288 ARG LEU ASN GLN LEU TYR ARG GLN PRO THR ILE GLU ASN
SEQRES 14 A 288 LEU LYS LEU MET MET ASP ILE PHE VAL PHE ASP THR SER
SEQRES 15 A 288 ASP LEU THR ASP ALA LEU PHE GLU ALA ARG LEU ASN ASN
SEQRES 16 A 288 MET LEU SER ARG ARG ASP HIS LEU GLU ASN PHE VAL LYS
SEQRES 17 A 288 SER LEU GLU ALA ASN PRO LYS GLN PHE PRO ASP PHE GLY
SEQRES 18 A 288 PRO ARG LEU ALA GLU ILE LYS ALA GLN THR LEU ILE VAL
SEQRES 19 A 288 TRP GLY ARG ASN ASP ARG PHE VAL PRO MET ASP ALA GLY
SEQRES 20 A 288 LEU ARG LEU LEU SER GLY ILE ALA GLY SER GLU LEU HIS
SEQRES 21 A 288 ILE PHE ARG ASP CYS GLY HIS TRP ALA GLN TRP GLU HIS
SEQRES 22 A 288 ALA ASP ALA PHE ASN GLN LEU VAL LEU ASN PHE LEU ALA
SEQRES 23 A 288 ARG PRO
SEQRES 1 B 288 MET SER TYR GLN PRO GLN THR GLU ALA ALA THR SER ARG
SEQRES 2 B 288 PHE LEU ASN VAL GLU GLU ALA GLY LYS THR LEU ARG ILE
SEQRES 3 B 288 HIS PHE ASN ASP CYS GLY GLN GLY ASP GLU THR VAL VAL
SEQRES 4 B 288 LEU LEU HIS GLY SER GLY PRO GLY ALA THR GLY TRP ALA
SEQRES 5 B 288 ASN PHE SER ARG ASN ILE ASP PRO LEU VAL GLU ALA GLY
SEQRES 6 B 288 TYR ARG VAL ILE LEU LEU ASP CYS PRO GLY TRP GLY LYS
SEQRES 7 B 288 SER ASP SER VAL VAL ASN SER GLY SER ARG SER ASP LEU
SEQRES 8 B 288 ASN ALA ARG ILE LEU LYS SER VAL VAL ASP GLN LEU ASP
SEQRES 9 B 288 ILE ALA LYS ILE HIS LEU LEU GLY ASN SER MET GLY GLY
SEQRES 10 B 288 HIS SER SER VAL ALA PHE THR LEU LYS TRP PRO GLU ARG
SEQRES 11 B 288 VAL GLY LYS LEU VAL LEU MET GLY GLY GLY THR GLY GLY
SEQRES 12 B 288 MET SER LEU PHE THR PRO MET PRO THR GLU GLY ILE LYS
SEQRES 13 B 288 ARG LEU ASN GLN LEU TYR ARG GLN PRO THR ILE GLU ASN
SEQRES 14 B 288 LEU LYS LEU MET MET ASP ILE PHE VAL PHE ASP THR SER
SEQRES 15 B 288 ASP LEU THR ASP ALA LEU PHE GLU ALA ARG LEU ASN ASN
SEQRES 16 B 288 MET LEU SER ARG ARG ASP HIS LEU GLU ASN PHE VAL LYS
SEQRES 17 B 288 SER LEU GLU ALA ASN PRO LYS GLN PHE PRO ASP PHE GLY
SEQRES 18 B 288 PRO ARG LEU ALA GLU ILE LYS ALA GLN THR LEU ILE VAL
SEQRES 19 B 288 TRP GLY ARG ASN ASP ARG PHE VAL PRO MET ASP ALA GLY
SEQRES 20 B 288 LEU ARG LEU LEU SER GLY ILE ALA GLY SER GLU LEU HIS
SEQRES 21 B 288 ILE PHE ARG ASP CYS GLY HIS TRP ALA GLN TRP GLU HIS
SEQRES 22 B 288 ALA ASP ALA PHE ASN GLN LEU VAL LEU ASN PHE LEU ALA
SEQRES 23 B 288 ARG PRO
SEQRES 1 C 288 MET SER TYR GLN PRO GLN THR GLU ALA ALA THR SER ARG
SEQRES 2 C 288 PHE LEU ASN VAL GLU GLU ALA GLY LYS THR LEU ARG ILE
SEQRES 3 C 288 HIS PHE ASN ASP CYS GLY GLN GLY ASP GLU THR VAL VAL
SEQRES 4 C 288 LEU LEU HIS GLY SER GLY PRO GLY ALA THR GLY TRP ALA
SEQRES 5 C 288 ASN PHE SER ARG ASN ILE ASP PRO LEU VAL GLU ALA GLY
SEQRES 6 C 288 TYR ARG VAL ILE LEU LEU ASP CYS PRO GLY TRP GLY LYS
SEQRES 7 C 288 SER ASP SER VAL VAL ASN SER GLY SER ARG SER ASP LEU
SEQRES 8 C 288 ASN ALA ARG ILE LEU LYS SER VAL VAL ASP GLN LEU ASP
SEQRES 9 C 288 ILE ALA LYS ILE HIS LEU LEU GLY ASN SER MET GLY GLY
SEQRES 10 C 288 HIS SER SER VAL ALA PHE THR LEU LYS TRP PRO GLU ARG
SEQRES 11 C 288 VAL GLY LYS LEU VAL LEU MET GLY GLY GLY THR GLY GLY
SEQRES 12 C 288 MET SER LEU PHE THR PRO MET PRO THR GLU GLY ILE LYS
SEQRES 13 C 288 ARG LEU ASN GLN LEU TYR ARG GLN PRO THR ILE GLU ASN
SEQRES 14 C 288 LEU LYS LEU MET MET ASP ILE PHE VAL PHE ASP THR SER
SEQRES 15 C 288 ASP LEU THR ASP ALA LEU PHE GLU ALA ARG LEU ASN ASN
SEQRES 16 C 288 MET LEU SER ARG ARG ASP HIS LEU GLU ASN PHE VAL LYS
SEQRES 17 C 288 SER LEU GLU ALA ASN PRO LYS GLN PHE PRO ASP PHE GLY
SEQRES 18 C 288 PRO ARG LEU ALA GLU ILE LYS ALA GLN THR LEU ILE VAL
SEQRES 19 C 288 TRP GLY ARG ASN ASP ARG PHE VAL PRO MET ASP ALA GLY
SEQRES 20 C 288 LEU ARG LEU LEU SER GLY ILE ALA GLY SER GLU LEU HIS
SEQRES 21 C 288 ILE PHE ARG ASP CYS GLY HIS TRP ALA GLN TRP GLU HIS
SEQRES 22 C 288 ALA ASP ALA PHE ASN GLN LEU VAL LEU ASN PHE LEU ALA
SEQRES 23 C 288 ARG PRO
SEQRES 1 D 288 MET SER TYR GLN PRO GLN THR GLU ALA ALA THR SER ARG
SEQRES 2 D 288 PHE LEU ASN VAL GLU GLU ALA GLY LYS THR LEU ARG ILE
SEQRES 3 D 288 HIS PHE ASN ASP CYS GLY GLN GLY ASP GLU THR VAL VAL
SEQRES 4 D 288 LEU LEU HIS GLY SER GLY PRO GLY ALA THR GLY TRP ALA
SEQRES 5 D 288 ASN PHE SER ARG ASN ILE ASP PRO LEU VAL GLU ALA GLY
SEQRES 6 D 288 TYR ARG VAL ILE LEU LEU ASP CYS PRO GLY TRP GLY LYS
SEQRES 7 D 288 SER ASP SER VAL VAL ASN SER GLY SER ARG SER ASP LEU
SEQRES 8 D 288 ASN ALA ARG ILE LEU LYS SER VAL VAL ASP GLN LEU ASP
SEQRES 9 D 288 ILE ALA LYS ILE HIS LEU LEU GLY ASN SER MET GLY GLY
SEQRES 10 D 288 HIS SER SER VAL ALA PHE THR LEU LYS TRP PRO GLU ARG
SEQRES 11 D 288 VAL GLY LYS LEU VAL LEU MET GLY GLY GLY THR GLY GLY
SEQRES 12 D 288 MET SER LEU PHE THR PRO MET PRO THR GLU GLY ILE LYS
SEQRES 13 D 288 ARG LEU ASN GLN LEU TYR ARG GLN PRO THR ILE GLU ASN
SEQRES 14 D 288 LEU LYS LEU MET MET ASP ILE PHE VAL PHE ASP THR SER
SEQRES 15 D 288 ASP LEU THR ASP ALA LEU PHE GLU ALA ARG LEU ASN ASN
SEQRES 16 D 288 MET LEU SER ARG ARG ASP HIS LEU GLU ASN PHE VAL LYS
SEQRES 17 D 288 SER LEU GLU ALA ASN PRO LYS GLN PHE PRO ASP PHE GLY
SEQRES 18 D 288 PRO ARG LEU ALA GLU ILE LYS ALA GLN THR LEU ILE VAL
SEQRES 19 D 288 TRP GLY ARG ASN ASP ARG PHE VAL PRO MET ASP ALA GLY
SEQRES 20 D 288 LEU ARG LEU LEU SER GLY ILE ALA GLY SER GLU LEU HIS
SEQRES 21 D 288 ILE PHE ARG ASP CYS GLY HIS TRP ALA GLN TRP GLU HIS
SEQRES 22 D 288 ALA ASP ALA PHE ASN GLN LEU VAL LEU ASN PHE LEU ALA
SEQRES 23 D 288 ARG PRO
HELIX 1 AA1 THR A 7 THR A 11 1 5
HELIX 2 AA2 THR A 49 PHE A 54 1 6
HELIX 3 AA3 ASN A 57 GLY A 65 1 9
HELIX 4 AA4 SER A 87 ASP A 104 1 18
HELIX 5 AA5 SER A 114 TRP A 127 1 14
HELIX 6 AA6 THR A 152 GLN A 164 1 13
HELIX 7 AA7 ILE A 167 VAL A 178 1 12
HELIX 8 AA8 THR A 185 ARG A 199 1 15
HELIX 9 AA9 ARG A 199 ASN A 213 1 15
HELIX 10 AB1 ARG A 223 ILE A 227 5 5
HELIX 11 AB2 MET A 244 ILE A 254 1 11
HELIX 12 AB3 TRP A 268 HIS A 273 1 6
HELIX 13 AB4 HIS A 273 ARG A 287 1 15
HELIX 14 AB5 THR B 7 THR B 11 1 5
HELIX 15 AB6 THR B 49 PHE B 54 1 6
HELIX 16 AB7 ASN B 57 ALA B 64 1 8
HELIX 17 AB8 SER B 87 ASP B 104 1 18
HELIX 18 AB9 SER B 114 TRP B 127 1 14
HELIX 19 AC1 THR B 152 GLN B 164 1 13
HELIX 20 AC2 THR B 166 VAL B 178 1 13
HELIX 21 AC3 THR B 185 ARG B 199 1 15
HELIX 22 AC4 ARG B 200 ASN B 213 1 14
HELIX 23 AC5 ARG B 223 ILE B 227 5 5
HELIX 24 AC6 PRO B 243 ILE B 254 1 12
HELIX 25 AC7 TRP B 268 HIS B 273 1 6
HELIX 26 AC8 HIS B 273 ARG B 287 1 15
HELIX 27 AC9 THR C 49 PHE C 54 1 6
HELIX 28 AD1 ASN C 57 ALA C 64 1 8
HELIX 29 AD2 SER C 87 ASP C 104 1 18
HELIX 30 AD3 SER C 114 TRP C 127 1 14
HELIX 31 AD4 THR C 152 GLN C 164 1 13
HELIX 32 AD5 THR C 166 VAL C 178 1 13
HELIX 33 AD6 ASP C 180 LEU C 184 5 5
HELIX 34 AD7 THR C 185 ARG C 199 1 15
HELIX 35 AD8 ARG C 199 ASN C 213 1 15
HELIX 36 AD9 PHE C 220 ILE C 227 5 8
HELIX 37 AE1 MET C 244 ILE C 254 1 11
HELIX 38 AE2 TRP C 268 HIS C 273 1 6
HELIX 39 AE3 HIS C 273 ARG C 287 1 15
HELIX 40 AE4 THR D 7 THR D 11 1 5
HELIX 41 AE5 THR D 49 PHE D 54 1 6
HELIX 42 AE6 ASN D 57 GLY D 65 1 9
HELIX 43 AE7 SER D 87 ASP D 104 1 18
HELIX 44 AE8 SER D 114 TRP D 127 1 14
HELIX 45 AE9 THR D 152 GLN D 164 1 13
HELIX 46 AF1 THR D 166 VAL D 178 1 13
HELIX 47 AF2 ASP D 180 LEU D 184 5 5
HELIX 48 AF3 THR D 185 ARG D 199 1 15
HELIX 49 AF4 ARG D 199 ASN D 213 1 15
HELIX 50 AF5 GLY D 221 ILE D 227 5 7
HELIX 51 AF6 PRO D 243 ILE D 254 1 12
HELIX 52 AF7 TRP D 268 HIS D 273 1 6
HELIX 53 AF8 ALA D 274 ARG D 287 1 14
SHEET 1 AA116 SER A 12 GLU A 19 0
SHEET 2 AA116 LYS A 22 CYS A 31 -1 O ILE A 26 N LEU A 15
SHEET 3 AA116 ARG A 67 LEU A 71 -1 O VAL A 68 N CYS A 31
SHEET 4 AA116 THR A 37 LEU A 41 1 N LEU A 40 O ILE A 69
SHEET 5 AA116 ILE A 108 ASN A 113 1 O HIS A 109 N VAL A 39
SHEET 6 AA116 VAL A 131 MET A 137 1 O GLY A 132 N ILE A 108
SHEET 7 AA116 THR A 231 GLY A 236 1 O LEU A 232 N LEU A 136
SHEET 8 AA116 GLU A 258 PHE A 262 1 O GLU A 258 N ILE A 233
SHEET 9 AA116 GLU B 258 PHE B 262 -1 O LEU B 259 N ILE A 261
SHEET 10 AA116 THR B 231 GLY B 236 1 N ILE B 233 O GLU B 258
SHEET 11 AA116 VAL B 131 MET B 137 1 N LEU B 136 O VAL B 234
SHEET 12 AA116 ILE B 108 ASN B 113 1 N ILE B 108 O GLY B 132
SHEET 13 AA116 THR B 37 LEU B 40 1 N VAL B 39 O HIS B 109
SHEET 14 AA116 ARG B 67 LEU B 71 1 O LEU B 71 N LEU B 40
SHEET 15 AA116 LYS B 22 CYS B 31 -1 N CYS B 31 O VAL B 68
SHEET 16 AA116 SER B 12 GLU B 19 -1 N LEU B 15 O ILE B 26
SHEET 1 AA216 SER C 12 GLU C 19 0
SHEET 2 AA216 LYS C 22 CYS C 31 -1 O ILE C 26 N LEU C 15
SHEET 3 AA216 ARG C 67 LEU C 71 -1 O LEU C 70 N ASN C 29
SHEET 4 AA216 THR C 37 LEU C 41 1 N VAL C 38 O ILE C 69
SHEET 5 AA216 ILE C 108 ASN C 113 1 O HIS C 109 N VAL C 39
SHEET 6 AA216 VAL C 131 MET C 137 1 O GLY C 132 N ILE C 108
SHEET 7 AA216 THR C 231 GLY C 236 1 O VAL C 234 N LEU C 136
SHEET 8 AA216 GLU C 258 PHE C 262 1 O GLU C 258 N ILE C 233
SHEET 9 AA216 GLU D 258 PHE D 262 -1 O LEU D 259 N ILE C 261
SHEET 10 AA216 GLN D 230 GLY D 236 1 N ILE D 233 O GLU D 258
SHEET 11 AA216 VAL D 131 MET D 137 1 N LEU D 136 O LEU D 232
SHEET 12 AA216 ILE D 108 ASN D 113 1 N LEU D 110 O VAL D 135
SHEET 13 AA216 THR D 37 LEU D 41 1 N VAL D 39 O LEU D 111
SHEET 14 AA216 ARG D 67 LEU D 71 1 O ILE D 69 N VAL D 38
SHEET 15 AA216 LYS D 22 CYS D 31 -1 N ASN D 29 O LEU D 70
SHEET 16 AA216 SER D 12 GLU D 19 -1 N VAL D 17 O LEU D 24
CISPEP 1 MET A 150 PRO A 151 0 -0.88
CISPEP 2 MET B 150 PRO B 151 0 -1.49
CISPEP 3 MET C 150 PRO C 151 0 4.05
CISPEP 4 MET D 150 PRO D 151 0 4.64
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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
TER 2249 PRO A 288
TER 4498 PRO B 288
TER 6747 PRO C 288
TER 8996 PRO D 288
MASTER 130 0 0 53 32 0 0 6 8992 4 0 92
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