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HEADER HYDROLASE 05-APR-23 8OOH
TITLE CRYO-EM MAP OF THE FOCUSED REFINEMENT OF THE SUBFAMILY III HALOALKANE
TITLE 2 DEHALOGENASE FROM HALOFERAX MEDITERRANEI DIMER FORMING HEXAMERIC
TITLE 3 ASSEMBLY.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA FOLD HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOFERAX MEDITERRANEI;
SOURCE 3 ORGANISM_TAXID: 2252;
SOURCE 4 GENE: MHPC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR M.POLAK,J.NOVACEK,K.CHMELOVA,M.MAREK
REVDAT 1 11-OCT-23 8OOH 0
JRNL AUTH K.CHMELOVA,T.GAO,M.POLAK,A.SCHENKMAYEROVA,T.I.CROLL,
JRNL AUTH 2 T.R.SHAIKH,J.SKARUPOVA,R.CHALOUPKOVA,K.DIEDERICHS,R.J.READ,
JRNL AUTH 3 J.DAMBORSKY,J.NOVACEK,M.MAREK
JRNL TITL MULTIMERIC STRUCTURE OF A SUBFAMILY III HALOALKANE
JRNL TITL 2 DEHALOGENASE-LIKE ENZYME SOLVED BY COMBINATION OF CRYO-EM
JRNL TITL 3 AND X-RAY CRYSTALLOGRAPHY.
JRNL REF PROTEIN SCI. V. 32 E4751 2023
JRNL REFN ESSN 1469-896X
JRNL PMID 37574754
JRNL DOI 10.1002/PRO.4751
REMARK 2
REMARK 2 RESOLUTION. 7.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, CRYOSPARC
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) : 7.000
REMARK 3 NUMBER OF PARTICLES : 55074
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: 1)C1 NON-UNIFORM REFINEMENT 2)C3 VOLUME ALIGNMENT
REMARK 3 3)C3 SYMMETRY EXPANSION (55074 PARTICLES EXPANDED TO 165 222
REMARK 3 PARTICLES) 4)C1 LOCAL REFINEMENT
REMARK 4
REMARK 4 8OOH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1292129727.
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 : THE SUBFAMILY III HALOALKANE
REMARK 245 DEHALOGENASE DHMEA FROM
REMARK 245 HALOFERAX MEDITERRANEI
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.04
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
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 K2 QUANTUM (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2200.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 7300.00
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 ASN A 7
REMARK 465 ALA A 8
REMARK 465 ARG A 9
REMARK 465 ASP A 10
REMARK 465 GLU A 11
REMARK 465 VAL A 12
REMARK 465 ILE A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 ILE A 16
REMARK 465 HIS A 17
REMARK 465 GLU A 18
REMARK 465 GLU A 19
REMARK 465 ALA A 20
REMARK 465 ASP A 21
REMARK 465 TRP A 22
REMARK 465 VAL A 23
REMARK 465 ASP A 24
REMARK 465 ARG A 25
REMARK 465 VAL A 307
REMARK 465 LEU A 308
REMARK 465 GLU A 309
REMARK 465 VAL A 310
REMARK 465 LEU A 311
REMARK 465 PHE A 312
REMARK 465 GLN A 313
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 ASN B 7
REMARK 465 ALA B 8
REMARK 465 ARG B 9
REMARK 465 ASP B 10
REMARK 465 GLU B 11
REMARK 465 VAL B 12
REMARK 465 ILE B 13
REMARK 465 ALA B 14
REMARK 465 ALA B 15
REMARK 465 ILE B 16
REMARK 465 HIS B 17
REMARK 465 GLU B 18
REMARK 465 GLU B 19
REMARK 465 ALA B 20
REMARK 465 ASP B 21
REMARK 465 TRP B 22
REMARK 465 VAL B 23
REMARK 465 ASP B 24
REMARK 465 ARG B 25
REMARK 465 LEU B 308
REMARK 465 GLU B 309
REMARK 465 VAL B 310
REMARK 465 LEU B 311
REMARK 465 PHE B 312
REMARK 465 GLN B 313
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 HG LEU A 272 HG LEU B 272 0.00
REMARK 500 CA LEU A 272 HD23 LEU B 272 0.22
REMARK 500 HD23 LEU A 272 CA LEU B 272 0.22
REMARK 500 N LEU A 272 CD2 LEU B 272 0.23
REMARK 500 CZ2 TRP A 239 C ARG B 267 0.23
REMARK 500 CD2 LEU A 272 N LEU B 272 0.23
REMARK 500 C ARG A 267 CZ2 TRP B 239 0.23
REMARK 500 HZ3 TRP A 157 OG1 THR B 268 0.36
REMARK 500 OG1 THR A 268 HZ3 TRP B 157 0.36
REMARK 500 CZ3 TRP A 239 CB ARG B 267 0.44
REMARK 500 CB ARG A 267 CZ3 TRP B 239 0.44
REMARK 500 HB2 SER A 160 CG PRO B 263 0.48
REMARK 500 CG PRO A 263 HB2 SER B 160 0.48
REMARK 500 CG ASP A 161 HA ARG B 262 0.49
REMARK 500 HA ARG A 262 CG ASP B 161 0.49
REMARK 500 HG3 PRO A 263 CB SER B 160 0.51
REMARK 500 CB SER A 160 HG3 PRO B 263 0.51
REMARK 500 HB3 ARG A 267 CE3 TRP B 239 0.54
REMARK 500 CE3 TRP A 239 HB3 ARG B 267 0.54
REMARK 500 CD ARG A 262 HB3 ASP B 161 0.55
REMARK 500 HB3 ASP A 161 CD ARG B 262 0.55
REMARK 500 HD22 LEU A 272 C ALA B 271 0.59
REMARK 500 C ALA A 271 HD22 LEU B 272 0.59
REMARK 500 O PRO A 158 HH22 ARG B 267 0.66
REMARK 500 OD2 ASP A 161 CA ARG B 262 0.66
REMARK 500 HH22 ARG A 267 O PRO B 158 0.66
REMARK 500 CA ARG A 262 OD2 ASP B 161 0.66
REMARK 500 HG22 THR A 268 HG22 THR B 268 0.68
REMARK 500 HD21 LEU A 272 H LEU B 272 0.71
REMARK 500 H LEU A 272 HD21 LEU B 272 0.71
REMARK 500 CZ3 TRP A 239 HB2 ARG B 267 0.73
REMARK 500 HB2 ARG A 267 CZ3 TRP B 239 0.73
REMARK 500 HB2 PRO A 158 HH12 ARG B 267 0.74
REMARK 500 CB ALA A 271 HD13 LEU B 272 0.74
REMARK 500 HD13 LEU A 272 CB ALA B 271 0.74
REMARK 500 HH12 ARG A 267 HB2 PRO B 158 0.74
REMARK 500 HG23 THR A 268 HH2 TRP B 157 0.78
REMARK 500 HH2 TRP A 157 HG23 THR B 268 0.78
REMARK 500 HB3 ALA A 271 HD13 LEU B 272 0.78
REMARK 500 HD13 LEU A 272 HB3 ALA B 271 0.78
REMARK 500 HD2 ARG A 262 CA ASP B 161 0.80
REMARK 500 CA ASP A 161 HD2 ARG B 262 0.80
REMARK 500 HB3 ALA A 271 CD1 LEU B 272 0.81
REMARK 500 CD1 LEU A 272 HB3 ALA B 271 0.81
REMARK 500 HD2 ARG A 267 HE3 TRP B 239 0.83
REMARK 500 HE3 TRP A 239 HD2 ARG B 267 0.83
REMARK 500 OG1 THR A 268 CZ3 TRP B 157 0.84
REMARK 500 CZ3 TRP A 157 OG1 THR B 268 0.84
REMARK 500 HB2 ASP A 161 HB3 ARG B 262 0.86
REMARK 500 HB3 ARG A 262 HB2 ASP B 161 0.86
REMARK 500
REMARK 500 THIS ENTRY HAS 278 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 103 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 129 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG B 103 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP B 129 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
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 ASP A 129 -121.90 55.07
REMARK 500 TRP A 157 141.02 76.92
REMARK 500 PHE A 224 -64.33 -26.99
REMARK 500 ASP B 129 -121.92 55.12
REMARK 500 TRP B 157 141.06 76.91
REMARK 500 PHE B 224 -64.25 -27.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-17015 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HEXAMERIC FORM OF A SUBFAMILY III HALOALKANE
REMARK 900 DEHALOGENASE FROM HALOFERAX MEDITERRANEI
DBREF 8OOH A 1 307 UNP I3R766 I3R766_HALMT 1 307
DBREF 8OOH B 1 307 UNP I3R766 I3R766_HALMT 1 307
SEQADV 8OOH LEU A 308 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH GLU A 309 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH VAL A 310 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH LEU A 311 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH PHE A 312 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH GLN A 313 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH LEU B 308 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH GLU B 309 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH VAL B 310 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH LEU B 311 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH PHE B 312 UNP I3R766 EXPRESSION TAG
SEQADV 8OOH GLN B 313 UNP I3R766 EXPRESSION TAG
SEQRES 1 A 313 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 A 313 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 A 313 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 A 313 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 A 313 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 A 313 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 A 313 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 A 313 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 A 313 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 A 313 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 A 313 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 A 313 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 A 313 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 A 313 LYS LEU LEU GLY GLY ARG ILE GLY ARG GLU LEU CYS GLU
SEQRES 15 A 313 ARG TYR ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY
SEQRES 16 A 313 PHE ALA ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU
SEQRES 17 A 313 GLN TYR ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR
SEQRES 18 A 313 GLY ILE PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP
SEQRES 19 A 313 LEU SER SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP
SEQRES 20 A 313 ILE PRO ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA
SEQRES 21 A 313 PHE ARG PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE
SEQRES 22 A 313 GLU ASP SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS
SEQRES 23 A 313 TYR VAL PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU
SEQRES 24 A 313 VAL ARG GLU PHE LEU GLU GLU VAL LEU GLU VAL LEU PHE
SEQRES 25 A 313 GLN
SEQRES 1 B 313 MET SER SER ALA SER SER ASN ALA ARG ASP GLU VAL ILE
SEQRES 2 B 313 ALA ALA ILE HIS GLU GLU ALA ASP TRP VAL ASP ARG THR
SEQRES 3 B 313 VAL TYR PRO PHE GLU SER ARG CYS ILE GLY LEU SER SER
SEQRES 4 B 313 GLY ALA VAL HIS TYR ILE ASP GLU GLY PRO ASP ASP GLY
SEQRES 5 B 313 GLY ARG GLU THR LEU LEU MET LEU HIS GLY ASN PRO THR
SEQRES 6 B 313 TRP SER PHE LEU TYR ARG HIS LEU VAL ARG ASP LEU ARG
SEQRES 7 B 313 ASP GLU TYR ARG CYS VAL ALA LEU ASP TYR LEU GLY PHE
SEQRES 8 B 313 GLY LEU SER GLU ARG PRO THR ASP PHE SER TYR ARG PRO
SEQRES 9 B 313 GLU ASP HIS ALA ASP VAL VAL GLU GLU PHE ILE ASP GLU
SEQRES 10 B 313 LEU GLY LEU GLU ASP VAL VAL LEU VAL GLY HIS ASP TRP
SEQRES 11 B 313 GLY GLY PRO ILE GLY PHE SER TYR ALA ILE ASP HIS PRO
SEQRES 12 B 313 GLU ASN VAL GLY GLY LEU VAL VAL MET ASN THR TRP MET
SEQRES 13 B 313 TRP PRO VAL SER ASP ASP LYS HIS PHE SER ARG PHE SER
SEQRES 14 B 313 LYS LEU LEU GLY GLY ARG ILE GLY ARG GLU LEU CYS GLU
SEQRES 15 B 313 ARG TYR ASP LEU PHE THR ARG VAL ILE MET PRO MET GLY
SEQRES 16 B 313 PHE ALA ASP ARG SER ARG PHE THR GLU SER ALA ARG GLU
SEQRES 17 B 313 GLN TYR ARG ALA ALA ASN ARG GLY ASP ARG THR GLY THR
SEQRES 18 B 313 GLY ILE PHE PRO GLN ALA ILE LEU GLY SER ARG ALA TRP
SEQRES 19 B 313 LEU SER SER LEU TRP GLU GLN ARG ASP ASN ILE ALA ASP
SEQRES 20 B 313 ILE PRO ALA ARG ILE ILE TRP GLY MET GLU ASP SER ALA
SEQRES 21 B 313 PHE ARG PRO ALA GLU LEU ARG THR PHE GLU ALA LEU PHE
SEQRES 22 B 313 GLU ASP SER SER THR VAL ARG LEU TYR GLY VAL GLY HIS
SEQRES 23 B 313 TYR VAL PRO GLU GLU PHE GLY SER ASP LEU VAL PRO LEU
SEQRES 24 B 313 VAL ARG GLU PHE LEU GLU GLU VAL LEU GLU VAL LEU PHE
SEQRES 25 B 313 GLN
HELIX 1 AA1 TRP A 66 LEU A 69 5 4
HELIX 2 AA2 TYR A 70 ARG A 78 1 9
HELIX 3 AA3 ARG A 103 LEU A 118 1 16
HELIX 4 AA4 TRP A 130 HIS A 142 1 13
HELIX 5 AA5 ASP A 162 GLY A 173 1 12
HELIX 6 AA6 GLY A 173 ASP A 185 1 13
HELIX 7 AA7 ASP A 185 VAL A 190 1 6
HELIX 8 AA8 VAL A 190 GLY A 195 1 6
HELIX 9 AA9 ASP A 198 PHE A 202 5 5
HELIX 10 AB1 THR A 203 ALA A 212 1 10
HELIX 11 AB2 ASN A 214 SER A 231 1 18
HELIX 12 AB3 SER A 231 GLN A 241 1 11
HELIX 13 AB4 GLN A 241 ALA A 246 1 6
HELIX 14 AB5 ARG A 262 PHE A 273 1 12
HELIX 15 AB6 TYR A 287 PHE A 292 1 6
HELIX 16 AB7 PHE A 292 GLU A 306 1 15
HELIX 17 AB8 TRP B 66 LEU B 69 5 4
HELIX 18 AB9 TYR B 70 ARG B 78 1 9
HELIX 19 AC1 ARG B 103 LEU B 118 1 16
HELIX 20 AC2 TRP B 130 HIS B 142 1 13
HELIX 21 AC3 ASP B 162 GLY B 173 1 12
HELIX 22 AC4 GLY B 173 ASP B 185 1 13
HELIX 23 AC5 ASP B 185 VAL B 190 1 6
HELIX 24 AC6 VAL B 190 GLY B 195 1 6
HELIX 25 AC7 ASP B 198 PHE B 202 5 5
HELIX 26 AC8 THR B 203 ALA B 212 1 10
HELIX 27 AC9 ASN B 214 SER B 231 1 18
HELIX 28 AD1 SER B 231 GLN B 241 1 11
HELIX 29 AD2 GLN B 241 ALA B 246 1 6
HELIX 30 AD3 ARG B 262 PHE B 273 1 12
HELIX 31 AD4 TYR B 287 PHE B 292 1 6
HELIX 32 AD5 PHE B 292 VAL B 307 1 16
SHEET 1 AA1 8 SER A 32 LEU A 37 0
SHEET 2 AA1 8 GLY A 40 GLU A 47 -1 O VAL A 42 N ILE A 35
SHEET 3 AA1 8 ARG A 82 LEU A 86 -1 O CYS A 83 N GLU A 47
SHEET 4 AA1 8 THR A 56 LEU A 60 1 N LEU A 57 O ARG A 82
SHEET 5 AA1 8 VAL A 123 HIS A 128 1 O VAL A 126 N LEU A 60
SHEET 6 AA1 8 VAL A 146 MET A 152 1 O VAL A 150 N LEU A 125
SHEET 7 AA1 8 ALA A 250 GLY A 255 1 O ILE A 253 N VAL A 151
SHEET 8 AA1 8 SER A 276 LEU A 281 1 O VAL A 279 N ILE A 252
SHEET 1 AA2 8 SER B 32 LEU B 37 0
SHEET 2 AA2 8 GLY B 40 GLU B 47 -1 O VAL B 42 N ILE B 35
SHEET 3 AA2 8 ARG B 82 LEU B 86 -1 O CYS B 83 N GLU B 47
SHEET 4 AA2 8 THR B 56 LEU B 60 1 N LEU B 57 O ARG B 82
SHEET 5 AA2 8 VAL B 123 HIS B 128 1 O VAL B 126 N LEU B 60
SHEET 6 AA2 8 VAL B 146 MET B 152 1 O VAL B 150 N LEU B 125
SHEET 7 AA2 8 ALA B 250 GLY B 255 1 O ILE B 253 N VAL B 151
SHEET 8 AA2 8 SER B 276 LEU B 281 1 O VAL B 279 N ILE B 252
CISPEP 1 ASN A 63 PRO A 64 0 -18.43
CISPEP 2 ASN B 63 PRO B 64 0 -18.47
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
TER 4413 GLU A 306
TER 8842 VAL B 307
MASTER 278 0 0 32 16 0 0 6 4543 2 0 50
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