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HEADER PLANT PROTEIN 15-JAN-26 10ER
TITLE CHLOROPLAST GLUTAMYL PEPTIDASE S781R IN OPEN-OPEN CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOFORM 2 OF PROBABLE GLUTAMYL ENDOPEPTIDASE,
COMPND 3 CHLOROPLASTIC;
COMPND 4 CHAIN: B, A;
COMPND 5 EC: 3.4.21.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: ATCGEP PRODUCED IN PLANT TISSUES WITH S781R MUTATION
COMPND 9 AND C-TERMINAL STREPII TAG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: GEP, AT2G47390, T8I13.23;
SOURCE 6 EXPRESSION_SYSTEM: ARABIDOPSIS THALIANA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 3702
KEYWDS S9 PROTEASE, ENZYME, SERINE PROTEASE, ALPHA-BETA-ALPHA SANDWICH FOLD,
KEYWDS 2 BETA-PROPELLER, PLANT PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR J.J.EHRLICH,P.ROUTRAY,K.J.VAN WIJK,T.KAWATE
REVDAT 1 27-MAY-26 10ER 0
JRNL AUTH J.J.EHRLICH,P.ROUTRAY,L.ENNS,K.J.VAN WIJK,T.KAWATE
JRNL TITL STRUCTURAL BASIS FOR DIMERIZATION, CATALYTIC REGULATION, AND
JRNL TITL 2 SUBSTRATE SELECTIVITY OF THE CHLOROPLAST S9D CGEP PROTEASE
JRNL TITL 3 IN ARABIDOPSIS THALIANA.
JRNL REF PROTEIN SCI. V. 35 70624 2026
JRNL REFN ESSN 1469-896X
JRNL PMID 42144868
JRNL DOI 10.1002/PRO.70624
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CTFFIND, COOT,
REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC, PHENIX
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) : 3.200
REMARK 3 NUMBER OF PARTICLES : 135102
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 10ER COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JAN-26.
REMARK 100 THE DEPOSITION ID IS D_1000304251.
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 : CHLOROPLAST GLUTAMYL
REMARK 245 ENDOPEPTIDASE DIMERIC PROTEIN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 4.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : 7 FORCE, 4 SECONDS, NO WAIT
REMARK 245 TIME OR DRAIN TIME
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 : 1853
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : TFS TALOS
REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X
REMARK 245 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 800.00
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 : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 4000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 63000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 ALA B 62
REMARK 465 SER B 63
REMARK 465 ARG B 64
REMARK 465 SER B 65
REMARK 465 ALA B 66
REMARK 465 SER B 67
REMARK 465 ARG B 68
REMARK 465 LEU B 69
REMARK 465 ARG B 70
REMARK 465 SER B 71
REMARK 465 LEU B 72
REMARK 465 ALA B 73
REMARK 465 SER B 74
REMARK 465 ALA B 75
REMARK 465 CYS B 76
REMARK 465 SER B 77
REMARK 465 GLY B 78
REMARK 465 GLY B 79
REMARK 465 ALA B 80
REMARK 465 GLU B 81
REMARK 465 ASP B 82
REMARK 465 GLY B 83
REMARK 465 GLY B 84
REMARK 465 GLY B 85
REMARK 465 THR B 86
REMARK 465 SER B 87
REMARK 465 ASN B 88
REMARK 465 GLY B 89
REMARK 465 SER B 90
REMARK 465 LEU B 91
REMARK 465 SER B 92
REMARK 465 ALA B 93
REMARK 465 SER B 94
REMARK 465 ALA B 95
REMARK 465 THR B 96
REMARK 465 ALA B 97
REMARK 465 THR B 98
REMARK 465 GLU B 99
REMARK 465 ASP B 100
REMARK 465 ASP B 101
REMARK 465 GLU B 102
REMARK 465 LEU B 103
REMARK 465 ALA B 104
REMARK 465 ILE B 105
REMARK 465 GLY B 106
REMARK 465 THR B 107
REMARK 465 LYS B 696
REMARK 465 SER B 697
REMARK 465 LYS B 698
REMARK 465 ASP B 699
REMARK 465 ALA B 700
REMARK 465 ALA B 701
REMARK 465 GLY B 702
REMARK 465 GLN B 703
REMARK 465 VAL B 704
REMARK 465 ARG B 705
REMARK 465 THR B 916
REMARK 465 SER B 917
REMARK 465 ASP B 918
REMARK 465 ALA B 919
REMARK 465 ASP B 920
REMARK 465 THR B 921
REMARK 465 SER B 922
REMARK 465 PRO B 923
REMARK 465 ASP B 924
REMARK 465 GLN B 925
REMARK 465 SER B 926
REMARK 465 LYS B 927
REMARK 465 GLU B 928
REMARK 465 GLY B 929
REMARK 465 SER B 930
REMARK 465 ASP B 931
REMARK 465 SER B 932
REMARK 465 ALA B 933
REMARK 465 ASP B 934
REMARK 465 LYS B 935
REMARK 465 VAL B 936
REMARK 465 SER B 937
REMARK 465 THR B 938
REMARK 465 GLY B 939
REMARK 465 THR B 940
REMARK 465 GLY B 941
REMARK 465 GLY B 942
REMARK 465 GLY B 943
REMARK 465 ASN B 944
REMARK 465 PRO B 945
REMARK 465 GLU B 946
REMARK 465 PHE B 947
REMARK 465 GLY B 948
REMARK 465 GLU B 949
REMARK 465 HIS B 950
REMARK 465 GLU B 951
REMARK 465 VAL B 952
REMARK 465 HIS B 953
REMARK 465 SER B 954
REMARK 465 LYS B 955
REMARK 465 LEU B 956
REMARK 465 ARG B 957
REMARK 465 ARG B 958
REMARK 465 SER B 959
REMARK 465 LEU B 960
REMARK 465 LEU B 961
REMARK 465 TRP B 962
REMARK 465 SER B 963
REMARK 465 HIS B 964
REMARK 465 PRO B 965
REMARK 465 GLN B 966
REMARK 465 PHE B 967
REMARK 465 GLU B 968
REMARK 465 LYS B 969
REMARK 465 ALA A 62
REMARK 465 SER A 63
REMARK 465 ARG A 64
REMARK 465 SER A 65
REMARK 465 ALA A 66
REMARK 465 SER A 67
REMARK 465 ARG A 68
REMARK 465 LEU A 69
REMARK 465 ARG A 70
REMARK 465 SER A 71
REMARK 465 LEU A 72
REMARK 465 ALA A 73
REMARK 465 SER A 74
REMARK 465 ALA A 75
REMARK 465 CYS A 76
REMARK 465 SER A 77
REMARK 465 GLY A 78
REMARK 465 GLY A 79
REMARK 465 ALA A 80
REMARK 465 GLU A 81
REMARK 465 ASP A 82
REMARK 465 GLY A 83
REMARK 465 GLY A 84
REMARK 465 GLY A 85
REMARK 465 THR A 86
REMARK 465 SER A 87
REMARK 465 ASN A 88
REMARK 465 GLY A 89
REMARK 465 SER A 90
REMARK 465 LEU A 91
REMARK 465 SER A 92
REMARK 465 ALA A 93
REMARK 465 SER A 94
REMARK 465 ALA A 95
REMARK 465 THR A 96
REMARK 465 ALA A 97
REMARK 465 THR A 98
REMARK 465 GLU A 99
REMARK 465 ASP A 100
REMARK 465 ASP A 101
REMARK 465 GLU A 102
REMARK 465 LEU A 103
REMARK 465 ALA A 104
REMARK 465 ILE A 105
REMARK 465 GLY A 106
REMARK 465 THR A 107
REMARK 465 LYS A 696
REMARK 465 SER A 697
REMARK 465 LYS A 698
REMARK 465 ASP A 699
REMARK 465 ALA A 700
REMARK 465 ALA A 701
REMARK 465 GLY A 702
REMARK 465 GLN A 703
REMARK 465 VAL A 704
REMARK 465 ARG A 705
REMARK 465 THR A 916
REMARK 465 SER A 917
REMARK 465 ASP A 918
REMARK 465 ALA A 919
REMARK 465 ASP A 920
REMARK 465 THR A 921
REMARK 465 SER A 922
REMARK 465 PRO A 923
REMARK 465 ASP A 924
REMARK 465 GLN A 925
REMARK 465 SER A 926
REMARK 465 LYS A 927
REMARK 465 GLU A 928
REMARK 465 GLY A 929
REMARK 465 SER A 930
REMARK 465 ASP A 931
REMARK 465 SER A 932
REMARK 465 ALA A 933
REMARK 465 ASP A 934
REMARK 465 LYS A 935
REMARK 465 VAL A 936
REMARK 465 SER A 937
REMARK 465 THR A 938
REMARK 465 GLY A 939
REMARK 465 THR A 940
REMARK 465 GLY A 941
REMARK 465 GLY A 942
REMARK 465 GLY A 943
REMARK 465 ASN A 944
REMARK 465 PRO A 945
REMARK 465 GLU A 946
REMARK 465 PHE A 947
REMARK 465 GLY A 948
REMARK 465 GLU A 949
REMARK 465 HIS A 950
REMARK 465 GLU A 951
REMARK 465 VAL A 952
REMARK 465 HIS A 953
REMARK 465 SER A 954
REMARK 465 LYS A 955
REMARK 465 LEU A 956
REMARK 465 ARG A 957
REMARK 465 ARG A 958
REMARK 465 SER A 959
REMARK 465 LEU A 960
REMARK 465 LEU A 961
REMARK 465 TRP A 962
REMARK 465 SER A 963
REMARK 465 HIS A 964
REMARK 465 PRO A 965
REMARK 465 GLN A 966
REMARK 465 PHE A 967
REMARK 465 GLU A 968
REMARK 465 LYS A 969
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 B 122 55.78 -90.53
REMARK 500 LEU B 395 -60.32 -93.19
REMARK 500 ASP B 435 -169.32 -125.43
REMARK 500 VAL B 464 -60.44 -107.00
REMARK 500 ASP B 479 -168.75 -162.16
REMARK 500 SER B 504 -157.43 59.13
REMARK 500 ASN B 546 48.82 39.57
REMARK 500 ASP B 599 30.56 -141.00
REMARK 500 TYR B 691 79.33 -150.98
REMARK 500 SER B 888 -169.26 -126.46
REMARK 500 ASP A 122 55.78 -90.56
REMARK 500 LEU A 395 -60.38 -93.16
REMARK 500 ASP A 435 -169.28 -125.46
REMARK 500 VAL A 464 -60.37 -107.03
REMARK 500 ASP A 479 -168.75 -162.18
REMARK 500 SER A 504 -157.46 59.08
REMARK 500 ASN A 546 48.80 39.52
REMARK 500 ASP A 599 30.58 -141.00
REMARK 500 TYR A 691 79.25 -151.00
REMARK 500 SER A 888 -169.30 -126.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-75116 RELATED DB: EMDB
REMARK 900 CHLOROPLAST GLUTAMYL PEPTIDASE S781R IN OPEN-OPEN CONFORMATION
DBREF 10ER B 62 961 UNP Q8VZF3 CGEP_ARATH 63 961
DBREF 10ER A 62 961 UNP Q8VZF3 CGEP_ARATH 63 961
SEQADV 10ER ARG B 781 UNP Q8VZF3 SER 781 ENGINEERED MUTATION
SEQADV 10ER TRP B 962 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER SER B 963 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER HIS B 964 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER PRO B 965 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER GLN B 966 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER PHE B 967 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER GLU B 968 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER LYS B 969 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER ARG A 781 UNP Q8VZF3 SER 781 ENGINEERED MUTATION
SEQADV 10ER TRP A 962 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER SER A 963 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER HIS A 964 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER PRO A 965 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER GLN A 966 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER PHE A 967 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER GLU A 968 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ER LYS A 969 UNP Q8VZF3 EXPRESSION TAG
SEQRES 1 B 907 ALA SER ARG SER ALA SER ARG LEU ARG SER LEU ALA SER
SEQRES 2 B 907 ALA CYS SER GLY GLY ALA GLU ASP GLY GLY GLY THR SER
SEQRES 3 B 907 ASN GLY SER LEU SER ALA SER ALA THR ALA THR GLU ASP
SEQRES 4 B 907 ASP GLU LEU ALA ILE GLY THR GLY TYR ARG LEU PRO PRO
SEQRES 5 B 907 PRO GLU ILE ARG ASP ILE VAL ASP ALA PRO PRO VAL PRO
SEQRES 6 B 907 ALA LEU SER PHE SER PRO HIS ARG ASP LYS ILE LEU PHE
SEQRES 7 B 907 LEU LYS ARG ARG ALA LEU PRO PRO LEU ALA ASP LEU ALA
SEQRES 8 B 907 ARG PRO GLU GLU LYS LEU ALA GLY VAL ARG ILE ASP GLY
SEQRES 9 B 907 TYR CYS ASN THR ARG SER ARG MET SER PHE TYR THR GLY
SEQRES 10 B 907 LEU GLY ILE HIS GLN LEU LEU PRO ASP GLY THR LEU SER
SEQRES 11 B 907 PRO GLU LYS GLU ILE THR GLY ILE PRO ASP GLY GLY LYS
SEQRES 12 B 907 ILE ASN PHE VAL THR TRP SER ASN ASP GLY LYS HIS LEU
SEQRES 13 B 907 ALA PHE SER ILE ARG VAL ASP GLU ASN GLY ASN SER SER
SEQRES 14 B 907 LYS PRO VAL VAL TRP VAL ALA ASP VAL GLU THR GLY VAL
SEQRES 15 B 907 ALA ARG PRO LEU PHE ASN SER GLN ASP ILE PHE LEU ASN
SEQRES 16 B 907 ALA ILE PHE GLU SER PHE VAL TRP ILE ASP ASN SER THR
SEQRES 17 B 907 LEU LEU VAL SER THR ILE PRO SER SER ARG GLY GLU PRO
SEQRES 18 B 907 PRO LYS LYS PRO LEU VAL PRO SER GLY PRO LYS THR LEU
SEQRES 19 B 907 SER ASN GLU THR LYS THR VAL VAL GLN VAL ARG THR PHE
SEQRES 20 B 907 GLN ASP LEU LEU LYS ASP GLU TYR ASP ALA ASP LEU PHE
SEQRES 21 B 907 ASP TYR TYR ALA SER SER GLN LEU VAL LEU ALA SER LEU
SEQRES 22 B 907 ASP GLY THR VAL LYS GLU VAL GLY VAL PRO ALA VAL TYR
SEQRES 23 B 907 THR SER LEU ASP PRO SER THR ASP HIS LYS TYR LEU LEU
SEQRES 24 B 907 VAL SER SER LEU HIS ARG PRO TYR SER PHE ILE VAL PRO
SEQRES 25 B 907 CYS GLY ARG PHE PRO LYS LYS VAL GLU VAL TRP THR THR
SEQRES 26 B 907 ASP GLY ARG PHE VAL ARG GLN LEU CYS ASP LEU PRO LEU
SEQRES 27 B 907 ALA GLU ASP ILE PRO ILE ALA SER ASN SER VAL ARG LYS
SEQRES 28 B 907 GLY MET ARG SER ILE ASN TRP ARG ALA ASP LYS PRO SER
SEQRES 29 B 907 THR LEU TYR TRP ALA GLU THR GLN ASP GLY GLY ASP ALA
SEQRES 30 B 907 LYS MET GLU VAL SER PRO ARG ASP ILE VAL TYR MET GLN
SEQRES 31 B 907 SER ALA GLU PRO LEU ALA GLY GLU GLU PRO GLU VAL LEU
SEQRES 32 B 907 HIS LYS LEU ASP LEU ARG TYR GLY GLY ILE SER TRP CYS
SEQRES 33 B 907 ASP ASP THR LEU ALA LEU VAL TYR GLU SER TRP TYR LYS
SEQRES 34 B 907 THR ARG ARG THR ARG THR TRP VAL ILE SER PRO GLY SER
SEQRES 35 B 907 ASN ASP VAL SER PRO ARG ILE LEU PHE ASP ARG SER SER
SEQRES 36 B 907 GLU ASP VAL TYR SER ASP PRO GLY SER THR MET LEU ARG
SEQRES 37 B 907 ARG THR ASP ALA GLY THR TYR VAL ILE ALA LYS ILE LYS
SEQRES 38 B 907 LYS GLU ASN ASP GLU GLY THR TYR VAL LEU LEU ASN GLY
SEQRES 39 B 907 SER GLY ALA THR PRO GLN GLY ASN VAL PRO PHE LEU ASP
SEQRES 40 B 907 LEU PHE ASP ILE ASN THR GLY ASN LYS GLU ARG ILE TRP
SEQRES 41 B 907 GLU SER ASP LYS GLU LYS TYR PHE GLU THR VAL VAL ALA
SEQRES 42 B 907 LEU MET SER ASP GLN LYS GLU GLY ASP LEU LYS MET GLU
SEQRES 43 B 907 GLU LEU LYS ILE LEU THR SER LYS GLU SER LYS THR GLU
SEQRES 44 B 907 ASN THR GLN TYR SER LEU GLN LEU TRP PRO ASP ARG LYS
SEQRES 45 B 907 VAL GLN GLN ILE THR ASN PHE PRO HIS PRO TYR PRO GLN
SEQRES 46 B 907 LEU ALA SER LEU GLN LYS GLU MET ILE ARG TYR GLN ARG
SEQRES 47 B 907 LYS ASP GLY VAL GLN LEU THR ALA THR LEU TYR LEU PRO
SEQRES 48 B 907 PRO GLY TYR ASP PRO SER LYS ASP GLY PRO LEU PRO CYS
SEQRES 49 B 907 LEU PHE TRP SER TYR PRO GLY GLU PHE LYS SER LYS ASP
SEQRES 50 B 907 ALA ALA GLY GLN VAL ARG GLY SER PRO ASN GLU PHE ALA
SEQRES 51 B 907 GLY ILE GLY SER THR SER ALA LEU LEU TRP LEU ALA ARG
SEQRES 52 B 907 ARG PHE ALA ILE LEU SER GLY PRO THR ILE PRO ILE ILE
SEQRES 53 B 907 GLY GLU GLY ASP GLU GLU ALA ASN ASP ARG TYR VAL GLU
SEQRES 54 B 907 GLN LEU VAL ALA SER ALA GLU ALA ALA VAL GLU GLU VAL
SEQRES 55 B 907 VAL ARG ARG GLY VAL ALA ASP ARG SER LYS ILE ALA VAL
SEQRES 56 B 907 GLY GLY HIS ARG TYR GLY ALA PHE MET THR ALA ASN LEU
SEQRES 57 B 907 LEU ALA HIS ALA PRO HIS LEU PHE ALA CYS GLY ILE ALA
SEQRES 58 B 907 ARG SER GLY ALA TYR ASN ARG THR LEU THR PRO PHE GLY
SEQRES 59 B 907 PHE GLN ASN GLU ASP ARG THR LEU TRP GLU ALA THR ASN
SEQRES 60 B 907 VAL TYR VAL GLU MET SER PRO PHE MET SER ALA ASN LYS
SEQRES 61 B 907 ILE LYS LYS PRO ILE LEU LEU ILE HIS GLY GLU GLU ASP
SEQRES 62 B 907 ASN ASN PRO GLY THR LEU THR MET GLN SER ASP ARG PHE
SEQRES 63 B 907 PHE ASN ALA LEU LYS GLY HIS GLY ALA LEU CYS ARG LEU
SEQRES 64 B 907 VAL VAL LEU PRO HIS GLU SER HIS GLY TYR SER ALA ARG
SEQRES 65 B 907 GLU SER ILE MET HIS VAL LEU TRP GLU THR ASP ARG TRP
SEQRES 66 B 907 LEU GLN LYS TYR CYS VAL PRO ASN THR SER ASP ALA ASP
SEQRES 67 B 907 THR SER PRO ASP GLN SER LYS GLU GLY SER ASP SER ALA
SEQRES 68 B 907 ASP LYS VAL SER THR GLY THR GLY GLY GLY ASN PRO GLU
SEQRES 69 B 907 PHE GLY GLU HIS GLU VAL HIS SER LYS LEU ARG ARG SER
SEQRES 70 B 907 LEU LEU TRP SER HIS PRO GLN PHE GLU LYS
SEQRES 1 A 907 ALA SER ARG SER ALA SER ARG LEU ARG SER LEU ALA SER
SEQRES 2 A 907 ALA CYS SER GLY GLY ALA GLU ASP GLY GLY GLY THR SER
SEQRES 3 A 907 ASN GLY SER LEU SER ALA SER ALA THR ALA THR GLU ASP
SEQRES 4 A 907 ASP GLU LEU ALA ILE GLY THR GLY TYR ARG LEU PRO PRO
SEQRES 5 A 907 PRO GLU ILE ARG ASP ILE VAL ASP ALA PRO PRO VAL PRO
SEQRES 6 A 907 ALA LEU SER PHE SER PRO HIS ARG ASP LYS ILE LEU PHE
SEQRES 7 A 907 LEU LYS ARG ARG ALA LEU PRO PRO LEU ALA ASP LEU ALA
SEQRES 8 A 907 ARG PRO GLU GLU LYS LEU ALA GLY VAL ARG ILE ASP GLY
SEQRES 9 A 907 TYR CYS ASN THR ARG SER ARG MET SER PHE TYR THR GLY
SEQRES 10 A 907 LEU GLY ILE HIS GLN LEU LEU PRO ASP GLY THR LEU SER
SEQRES 11 A 907 PRO GLU LYS GLU ILE THR GLY ILE PRO ASP GLY GLY LYS
SEQRES 12 A 907 ILE ASN PHE VAL THR TRP SER ASN ASP GLY LYS HIS LEU
SEQRES 13 A 907 ALA PHE SER ILE ARG VAL ASP GLU ASN GLY ASN SER SER
SEQRES 14 A 907 LYS PRO VAL VAL TRP VAL ALA ASP VAL GLU THR GLY VAL
SEQRES 15 A 907 ALA ARG PRO LEU PHE ASN SER GLN ASP ILE PHE LEU ASN
SEQRES 16 A 907 ALA ILE PHE GLU SER PHE VAL TRP ILE ASP ASN SER THR
SEQRES 17 A 907 LEU LEU VAL SER THR ILE PRO SER SER ARG GLY GLU PRO
SEQRES 18 A 907 PRO LYS LYS PRO LEU VAL PRO SER GLY PRO LYS THR LEU
SEQRES 19 A 907 SER ASN GLU THR LYS THR VAL VAL GLN VAL ARG THR PHE
SEQRES 20 A 907 GLN ASP LEU LEU LYS ASP GLU TYR ASP ALA ASP LEU PHE
SEQRES 21 A 907 ASP TYR TYR ALA SER SER GLN LEU VAL LEU ALA SER LEU
SEQRES 22 A 907 ASP GLY THR VAL LYS GLU VAL GLY VAL PRO ALA VAL TYR
SEQRES 23 A 907 THR SER LEU ASP PRO SER THR ASP HIS LYS TYR LEU LEU
SEQRES 24 A 907 VAL SER SER LEU HIS ARG PRO TYR SER PHE ILE VAL PRO
SEQRES 25 A 907 CYS GLY ARG PHE PRO LYS LYS VAL GLU VAL TRP THR THR
SEQRES 26 A 907 ASP GLY ARG PHE VAL ARG GLN LEU CYS ASP LEU PRO LEU
SEQRES 27 A 907 ALA GLU ASP ILE PRO ILE ALA SER ASN SER VAL ARG LYS
SEQRES 28 A 907 GLY MET ARG SER ILE ASN TRP ARG ALA ASP LYS PRO SER
SEQRES 29 A 907 THR LEU TYR TRP ALA GLU THR GLN ASP GLY GLY ASP ALA
SEQRES 30 A 907 LYS MET GLU VAL SER PRO ARG ASP ILE VAL TYR MET GLN
SEQRES 31 A 907 SER ALA GLU PRO LEU ALA GLY GLU GLU PRO GLU VAL LEU
SEQRES 32 A 907 HIS LYS LEU ASP LEU ARG TYR GLY GLY ILE SER TRP CYS
SEQRES 33 A 907 ASP ASP THR LEU ALA LEU VAL TYR GLU SER TRP TYR LYS
SEQRES 34 A 907 THR ARG ARG THR ARG THR TRP VAL ILE SER PRO GLY SER
SEQRES 35 A 907 ASN ASP VAL SER PRO ARG ILE LEU PHE ASP ARG SER SER
SEQRES 36 A 907 GLU ASP VAL TYR SER ASP PRO GLY SER THR MET LEU ARG
SEQRES 37 A 907 ARG THR ASP ALA GLY THR TYR VAL ILE ALA LYS ILE LYS
SEQRES 38 A 907 LYS GLU ASN ASP GLU GLY THR TYR VAL LEU LEU ASN GLY
SEQRES 39 A 907 SER GLY ALA THR PRO GLN GLY ASN VAL PRO PHE LEU ASP
SEQRES 40 A 907 LEU PHE ASP ILE ASN THR GLY ASN LYS GLU ARG ILE TRP
SEQRES 41 A 907 GLU SER ASP LYS GLU LYS TYR PHE GLU THR VAL VAL ALA
SEQRES 42 A 907 LEU MET SER ASP GLN LYS GLU GLY ASP LEU LYS MET GLU
SEQRES 43 A 907 GLU LEU LYS ILE LEU THR SER LYS GLU SER LYS THR GLU
SEQRES 44 A 907 ASN THR GLN TYR SER LEU GLN LEU TRP PRO ASP ARG LYS
SEQRES 45 A 907 VAL GLN GLN ILE THR ASN PHE PRO HIS PRO TYR PRO GLN
SEQRES 46 A 907 LEU ALA SER LEU GLN LYS GLU MET ILE ARG TYR GLN ARG
SEQRES 47 A 907 LYS ASP GLY VAL GLN LEU THR ALA THR LEU TYR LEU PRO
SEQRES 48 A 907 PRO GLY TYR ASP PRO SER LYS ASP GLY PRO LEU PRO CYS
SEQRES 49 A 907 LEU PHE TRP SER TYR PRO GLY GLU PHE LYS SER LYS ASP
SEQRES 50 A 907 ALA ALA GLY GLN VAL ARG GLY SER PRO ASN GLU PHE ALA
SEQRES 51 A 907 GLY ILE GLY SER THR SER ALA LEU LEU TRP LEU ALA ARG
SEQRES 52 A 907 ARG PHE ALA ILE LEU SER GLY PRO THR ILE PRO ILE ILE
SEQRES 53 A 907 GLY GLU GLY ASP GLU GLU ALA ASN ASP ARG TYR VAL GLU
SEQRES 54 A 907 GLN LEU VAL ALA SER ALA GLU ALA ALA VAL GLU GLU VAL
SEQRES 55 A 907 VAL ARG ARG GLY VAL ALA ASP ARG SER LYS ILE ALA VAL
SEQRES 56 A 907 GLY GLY HIS ARG TYR GLY ALA PHE MET THR ALA ASN LEU
SEQRES 57 A 907 LEU ALA HIS ALA PRO HIS LEU PHE ALA CYS GLY ILE ALA
SEQRES 58 A 907 ARG SER GLY ALA TYR ASN ARG THR LEU THR PRO PHE GLY
SEQRES 59 A 907 PHE GLN ASN GLU ASP ARG THR LEU TRP GLU ALA THR ASN
SEQRES 60 A 907 VAL TYR VAL GLU MET SER PRO PHE MET SER ALA ASN LYS
SEQRES 61 A 907 ILE LYS LYS PRO ILE LEU LEU ILE HIS GLY GLU GLU ASP
SEQRES 62 A 907 ASN ASN PRO GLY THR LEU THR MET GLN SER ASP ARG PHE
SEQRES 63 A 907 PHE ASN ALA LEU LYS GLY HIS GLY ALA LEU CYS ARG LEU
SEQRES 64 A 907 VAL VAL LEU PRO HIS GLU SER HIS GLY TYR SER ALA ARG
SEQRES 65 A 907 GLU SER ILE MET HIS VAL LEU TRP GLU THR ASP ARG TRP
SEQRES 66 A 907 LEU GLN LYS TYR CYS VAL PRO ASN THR SER ASP ALA ASP
SEQRES 67 A 907 THR SER PRO ASP GLN SER LYS GLU GLY SER ASP SER ALA
SEQRES 68 A 907 ASP LYS VAL SER THR GLY THR GLY GLY GLY ASN PRO GLU
SEQRES 69 A 907 PHE GLY GLU HIS GLU VAL HIS SER LYS LEU ARG ARG SER
SEQRES 70 A 907 LEU LEU TRP SER HIS PRO GLN PHE GLU LYS
HELIX 1 AA1 PRO B 114 ASP B 122 1 9
HELIX 2 AA2 LEU B 149 ARG B 154 1 6
HELIX 3 AA3 ASP B 315 SER B 327 1 13
HELIX 4 AA4 PRO B 374 PHE B 378 5 5
HELIX 5 AA5 ALA B 719 ARG B 726 5 8
HELIX 6 AA6 GLU B 744 ARG B 748 5 5
HELIX 7 AA7 TYR B 749 GLY B 768 1 20
HELIX 8 AA8 TYR B 782 ALA B 794 1 13
HELIX 9 AA9 ASN B 809 THR B 813 5 5
HELIX 10 AB1 ALA B 827 SER B 835 1 9
HELIX 11 AB2 PRO B 836 ALA B 840 5 5
HELIX 12 AB3 THR B 862 HIS B 875 1 14
HELIX 13 AB4 ALA B 893 CYS B 912 1 20
HELIX 14 AB5 PRO A 114 ASP A 122 1 9
HELIX 15 AB6 LEU A 149 ARG A 154 1 6
HELIX 16 AB7 ASP A 315 SER A 327 1 13
HELIX 17 AB8 PRO A 374 PHE A 378 5 5
HELIX 18 AB9 ALA A 719 ARG A 726 5 8
HELIX 19 AC1 GLU A 744 ARG A 748 5 5
HELIX 20 AC2 TYR A 749 GLY A 768 1 20
HELIX 21 AC3 TYR A 782 ALA A 794 1 13
HELIX 22 AC4 ASN A 809 THR A 813 5 5
HELIX 23 AC5 ALA A 827 SER A 835 1 9
HELIX 24 AC6 PRO A 836 ALA A 840 5 5
HELIX 25 AC7 THR A 862 HIS A 875 1 14
HELIX 26 AC8 ALA A 893 CYS A 912 1 20
SHEET 1 AA1 4 ALA B 128 PHE B 131 0
SHEET 2 AA1 4 LYS B 137 LYS B 142 -1 O LEU B 139 N SER B 130
SHEET 3 AA1 4 GLY B 179 GLN B 184 -1 O HIS B 183 N ILE B 138
SHEET 4 AA1 4 LYS B 195 GLU B 196 -1 O LYS B 195 N ILE B 182
SHEET 1 AA2 3 GLU B 156 LEU B 159 0
SHEET 2 AA2 3 VAL B 162 ASP B 165 -1 O ILE B 164 N GLU B 157
SHEET 3 AA2 3 THR B 170 ARG B 171 -1 O THR B 170 N ASP B 165
SHEET 1 AA3 4 ILE B 206 TRP B 211 0
SHEET 2 AA3 4 HIS B 217 ILE B 222 -1 O SER B 221 N ASN B 207
SHEET 3 AA3 4 VAL B 234 ASP B 239 -1 O TRP B 236 N PHE B 220
SHEET 4 AA3 4 ALA B 245 PRO B 247 -1 O ARG B 246 N VAL B 237
SHEET 1 AA4 4 VAL B 264 ASP B 267 0
SHEET 2 AA4 4 THR B 270 THR B 275 -1 O LEU B 272 N VAL B 264
SHEET 3 AA4 4 GLN B 329 SER B 334 -1 O VAL B 331 N VAL B 273
SHEET 4 AA4 4 VAL B 339 GLU B 341 -1 O LYS B 340 N LEU B 332
SHEET 1 AA5 4 LYS B 294 SER B 297 0
SHEET 2 AA5 4 CYS A 879 LEU A 884 -1 O LEU A 881 N LEU B 296
SHEET 3 AA5 4 ILE A 847 GLY A 852 1 N LEU A 849 O ARG A 880
SHEET 4 AA5 4 GLY A 801 ARG A 804 1 N ALA A 803 O LEU A 848
SHEET 1 AA6 4 TYR B 348 PRO B 353 0
SHEET 2 AA6 4 TYR B 359 LEU B 365 -1 O LEU B 361 N ASP B 352
SHEET 3 AA6 4 LYS B 380 THR B 386 -1 O GLU B 383 N VAL B 362
SHEET 4 AA6 4 PHE B 391 LEU B 398 -1 O CYS B 396 N VAL B 382
SHEET 1 AA7 4 MET B 415 ASN B 419 0
SHEET 2 AA7 4 THR B 427 THR B 433 -1 O TYR B 429 N ASN B 419
SHEET 3 AA7 4 ASP B 447 SER B 453 -1 O ILE B 448 N GLU B 432
SHEET 4 AA7 4 GLU B 463 LYS B 467 -1 O LYS B 467 N ASP B 447
SHEET 1 AA8 4 SER B 476 TRP B 477 0
SHEET 2 AA8 4 ALA B 483 TRP B 489 -1 O LEU B 484 N SER B 476
SHEET 3 AA8 4 ARG B 494 VAL B 499 -1 O ARG B 496 N GLU B 487
SHEET 4 AA8 4 ARG B 510 PHE B 513 -1 O PHE B 513 N THR B 495
SHEET 1 AA9 4 SER B 526 THR B 527 0
SHEET 2 AA9 4 TYR B 551 GLY B 556 -1 O ASN B 555 N SER B 526
SHEET 3 AA9 4 PHE B 567 ASP B 572 -1 O ASP B 569 N LEU B 554
SHEET 4 AA9 4 ARG B 580 GLU B 583 -1 O TRP B 582 N LEU B 568
SHEET 1 AB1 2 LEU B 529 ARG B 531 0
SHEET 2 AB1 2 TYR B 537 ILE B 539 -1 O VAL B 538 N ARG B 530
SHEET 1 AB2 2 ILE B 542 LYS B 543 0
SHEET 2 AB2 2 LEU B 605 LYS B 606 1 O LEU B 605 N LYS B 543
SHEET 1 AB3 4 THR B 592 LEU B 596 0
SHEET 2 AB3 4 LYS B 611 LYS B 616 -1 O LEU B 613 N ALA B 595
SHEET 3 AB3 4 GLN B 624 LEU B 629 -1 O GLN B 628 N ILE B 612
SHEET 4 AB3 4 LYS B 634 GLN B 637 -1 O GLN B 636 N LEU B 627
SHEET 1 AB4 4 GLN B 652 GLN B 659 0
SHEET 2 AB4 4 GLN B 665 LEU B 672 -1 O LEU B 666 N TYR B 658
SHEET 3 AB4 4 ALA B 728 SER B 731 -1 O ILE B 729 N TYR B 671
SHEET 4 AB4 4 CYS B 686 TRP B 689 1 N LEU B 687 O LEU B 730
SHEET 1 AB5 4 GLY B 801 ARG B 804 0
SHEET 2 AB5 4 ILE B 847 GLY B 852 1 O LEU B 848 N ALA B 803
SHEET 3 AB5 4 CYS B 879 LEU B 884 1 O ARG B 880 N LEU B 849
SHEET 4 AB5 4 LYS A 294 SER A 297 -1 O LEU A 296 N LEU B 881
SHEET 1 AB6 4 ALA A 128 PHE A 131 0
SHEET 2 AB6 4 LYS A 137 LYS A 142 -1 O LEU A 139 N SER A 130
SHEET 3 AB6 4 GLY A 179 GLN A 184 -1 O HIS A 183 N ILE A 138
SHEET 4 AB6 4 LYS A 195 GLU A 196 -1 O LYS A 195 N ILE A 182
SHEET 1 AB7 3 GLU A 156 LEU A 159 0
SHEET 2 AB7 3 VAL A 162 ASP A 165 -1 O ILE A 164 N GLU A 157
SHEET 3 AB7 3 THR A 170 ARG A 171 -1 O THR A 170 N ASP A 165
SHEET 1 AB8 4 ILE A 206 TRP A 211 0
SHEET 2 AB8 4 HIS A 217 ILE A 222 -1 O SER A 221 N ASN A 207
SHEET 3 AB8 4 VAL A 234 ASP A 239 -1 O TRP A 236 N PHE A 220
SHEET 4 AB8 4 ALA A 245 PRO A 247 -1 O ARG A 246 N VAL A 237
SHEET 1 AB9 4 VAL A 264 ASP A 267 0
SHEET 2 AB9 4 THR A 270 THR A 275 -1 O LEU A 272 N VAL A 264
SHEET 3 AB9 4 GLN A 329 SER A 334 -1 O VAL A 331 N VAL A 273
SHEET 4 AB9 4 VAL A 339 GLU A 341 -1 O LYS A 340 N LEU A 332
SHEET 1 AC1 4 TYR A 348 PRO A 353 0
SHEET 2 AC1 4 TYR A 359 LEU A 365 -1 O LEU A 361 N ASP A 352
SHEET 3 AC1 4 LYS A 380 THR A 386 -1 O GLU A 383 N VAL A 362
SHEET 4 AC1 4 PHE A 391 LEU A 398 -1 O CYS A 396 N VAL A 382
SHEET 1 AC2 4 MET A 415 ASN A 419 0
SHEET 2 AC2 4 THR A 427 THR A 433 -1 O TYR A 429 N ASN A 419
SHEET 3 AC2 4 ASP A 447 SER A 453 -1 O ILE A 448 N GLU A 432
SHEET 4 AC2 4 GLU A 463 LYS A 467 -1 O LYS A 467 N ASP A 447
SHEET 1 AC3 4 SER A 476 TRP A 477 0
SHEET 2 AC3 4 ALA A 483 TRP A 489 -1 O LEU A 484 N SER A 476
SHEET 3 AC3 4 ARG A 494 VAL A 499 -1 O ARG A 496 N GLU A 487
SHEET 4 AC3 4 ARG A 510 PHE A 513 -1 O PHE A 513 N THR A 495
SHEET 1 AC4 4 SER A 526 THR A 527 0
SHEET 2 AC4 4 TYR A 551 GLY A 556 -1 O ASN A 555 N SER A 526
SHEET 3 AC4 4 PHE A 567 ASP A 572 -1 O ASP A 569 N LEU A 554
SHEET 4 AC4 4 ARG A 580 GLU A 583 -1 O TRP A 582 N LEU A 568
SHEET 1 AC5 2 LEU A 529 ARG A 531 0
SHEET 2 AC5 2 TYR A 537 ILE A 539 -1 O VAL A 538 N ARG A 530
SHEET 1 AC6 2 ILE A 542 LYS A 543 0
SHEET 2 AC6 2 LEU A 605 LYS A 606 1 O LEU A 605 N LYS A 543
SHEET 1 AC7 4 THR A 592 LEU A 596 0
SHEET 2 AC7 4 LYS A 611 LYS A 616 -1 O LEU A 613 N ALA A 595
SHEET 3 AC7 4 GLN A 624 LEU A 629 -1 O GLN A 628 N ILE A 612
SHEET 4 AC7 4 LYS A 634 GLN A 637 -1 O GLN A 636 N LEU A 627
SHEET 1 AC8 4 GLN A 652 GLN A 659 0
SHEET 2 AC8 4 GLN A 665 LEU A 672 -1 O LEU A 666 N TYR A 658
SHEET 3 AC8 4 ALA A 728 SER A 731 -1 O ILE A 729 N TYR A 671
SHEET 4 AC8 4 CYS A 686 TRP A 689 1 N LEU A 687 O LEU A 730
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 6299 ASN B 915
TER 12598 ASN A 915
MASTER 367 0 0 26 94 0 0 612596 2 0 140
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