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HEADER PLANT PROTEIN 15-JAN-26 10ET
TITLE CHLOROPLAST GLUTAMYL PEPTIDASE D855N IN OPEN-CLOSED 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: CATALYTICALLY DEAD ATCGEP D855N RECOMBINANTLY
COMPND 9 EXPRESSED IN E. COLI AND PURIFIED WITH AN N-TERMINAL 6X HIS TAG
COMPND 10 FOLLOWED BY A GG LINKER
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: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693
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 10ET 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. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, CTFFIND, COOT, PHENIX,
REMARK 3 CRYOSPARC, 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) : 3.000
REMARK 3 NUMBER OF PARTICLES : 70609
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 10ET 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_1000304254.
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) : 1.00
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 : 4206
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : TFS KRIOS
REMARK 245 DETECTOR TYPE : FEI FALCON I (4K X 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) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 96000
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 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 HIS B 54
REMARK 465 HIS B 55
REMARK 465 HIS B 56
REMARK 465 HIS B 57
REMARK 465 HIS B 58
REMARK 465 HIS B 59
REMARK 465 GLY B 60
REMARK 465 GLY B 61
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 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 HIS A 55
REMARK 465 HIS A 56
REMARK 465 HIS A 57
REMARK 465 HIS A 58
REMARK 465 HIS A 59
REMARK 465 HIS A 60
REMARK 465 GLY A 61
REMARK 465 GLY A 62
REMARK 465 ALA A 63
REMARK 465 SER A 64
REMARK 465 ARG A 65
REMARK 465 SER A 66
REMARK 465 ALA A 67
REMARK 465 SER A 68
REMARK 465 ARG A 69
REMARK 465 LEU A 70
REMARK 465 ARG A 71
REMARK 465 SER A 72
REMARK 465 LEU A 73
REMARK 465 ALA A 74
REMARK 465 SER A 75
REMARK 465 ALA A 76
REMARK 465 CYS A 77
REMARK 465 SER A 78
REMARK 465 GLY A 79
REMARK 465 GLY A 80
REMARK 465 ALA A 81
REMARK 465 GLU A 82
REMARK 465 ASP A 83
REMARK 465 GLY A 84
REMARK 465 GLY A 85
REMARK 465 GLY A 86
REMARK 465 THR A 87
REMARK 465 SER A 88
REMARK 465 ASN A 89
REMARK 465 GLY A 90
REMARK 465 SER A 91
REMARK 465 LEU A 92
REMARK 465 SER A 93
REMARK 465 ALA A 94
REMARK 465 SER A 95
REMARK 465 ALA A 96
REMARK 465 THR A 97
REMARK 465 ALA A 98
REMARK 465 THR A 99
REMARK 465 GLU A 100
REMARK 465 ASP A 101
REMARK 465 ASP A 102
REMARK 465 GLU A 103
REMARK 465 LEU A 104
REMARK 465 ALA A 105
REMARK 465 ILE A 106
REMARK 465 GLY A 107
REMARK 465 THR A 108
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 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 OG SER B 251 OD1 ASP B 253 2.18
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 ALA B 258 62.18 -102.42
REMARK 500 SER B 262 -168.67 -125.19
REMARK 500 ARG B 307 -168.71 -79.12
REMARK 500 VAL B 392 -55.45 -123.77
REMARK 500 ASN B 419 -169.73 -127.18
REMARK 500 GLU B 609 32.77 -98.67
REMARK 500 SER B 650 52.67 -93.61
REMARK 500 GLU B 744 -5.72 71.69
REMARK 500 HIS B 780 -66.37 -95.75
REMARK 500 SER B 805 45.28 72.34
REMARK 500 SER B 888 -166.84 -117.70
REMARK 500 CYS A 168 -6.36 75.35
REMARK 500 ASP A 225 53.63 -94.02
REMARK 500 ALA A 258 73.31 -100.84
REMARK 500 VAL A 464 -61.97 -96.73
REMARK 500 ASP A 479 -131.62 57.67
REMARK 500 LYS A 588 20.17 -142.99
REMARK 500 MET A 597 57.41 -99.73
REMARK 500 LEU A 648 79.95 -101.69
REMARK 500 GLU A 763 -60.33 -92.88
REMARK 500 SER A 805 52.50 36.97
REMARK 500 GLU A 854 30.45 -92.30
REMARK 500 HIS A 889 -53.92 -123.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-75118 RELATED DB: EMDB
REMARK 900 CHLOROPLAST GLUTAMYL PEPTIDASE D855N IN OPEN-CLOSED CONFORMATION
DBREF 10ET B 62 961 UNP Q8VZF3 CGEP_ARATH 63 961
DBREF 10ET A 63 961 UNP Q8VZF3 CGEP_ARATH 63 961
SEQADV 10ET HIS B 54 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET HIS B 55 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET HIS B 56 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET HIS B 57 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET HIS B 58 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET HIS B 59 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET GLY B 60 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET GLY B 61 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET ASN B 855 UNP Q8VZF3 ASP 855 ENGINEERED MUTATION
SEQADV 10ET HIS A 55 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET HIS A 56 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET HIS A 57 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET HIS A 58 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET HIS A 59 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET HIS A 60 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET GLY A 61 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET GLY A 62 UNP Q8VZF3 EXPRESSION TAG
SEQADV 10ET ASN A 855 UNP Q8VZF3 ASP 855 ENGINEERED MUTATION
SEQRES 1 B 907 HIS HIS HIS HIS HIS HIS GLY GLY ALA SER ARG SER ALA
SEQRES 2 B 907 SER ARG LEU ARG SER LEU ALA SER ALA CYS SER GLY GLY
SEQRES 3 B 907 ALA GLU ASP GLY GLY GLY THR SER ASN GLY SER LEU SER
SEQRES 4 B 907 ALA SER ALA THR ALA THR GLU ASP ASP GLU LEU ALA ILE
SEQRES 5 B 907 GLY THR GLY TYR ARG LEU PRO PRO PRO GLU ILE ARG ASP
SEQRES 6 B 907 ILE VAL ASP ALA PRO PRO VAL PRO ALA LEU SER PHE SER
SEQRES 7 B 907 PRO HIS ARG ASP LYS ILE LEU PHE LEU LYS ARG ARG ALA
SEQRES 8 B 907 LEU PRO PRO LEU ALA ASP LEU ALA ARG PRO GLU GLU LYS
SEQRES 9 B 907 LEU ALA GLY VAL ARG ILE ASP GLY TYR CYS ASN THR ARG
SEQRES 10 B 907 SER ARG MET SER PHE TYR THR GLY LEU GLY ILE HIS GLN
SEQRES 11 B 907 LEU LEU PRO ASP GLY THR LEU SER PRO GLU LYS GLU ILE
SEQRES 12 B 907 THR GLY ILE PRO ASP GLY GLY LYS ILE ASN PHE VAL THR
SEQRES 13 B 907 TRP SER ASN ASP GLY LYS HIS LEU ALA PHE SER ILE ARG
SEQRES 14 B 907 VAL ASP GLU ASN GLY ASN SER SER LYS PRO VAL VAL TRP
SEQRES 15 B 907 VAL ALA ASP VAL GLU THR GLY VAL ALA ARG PRO LEU PHE
SEQRES 16 B 907 ASN SER GLN ASP ILE PHE LEU ASN ALA ILE PHE GLU SER
SEQRES 17 B 907 PHE VAL TRP ILE ASP ASN SER THR LEU LEU VAL SER THR
SEQRES 18 B 907 ILE PRO SER SER ARG GLY GLU PRO PRO LYS LYS PRO LEU
SEQRES 19 B 907 VAL PRO SER GLY PRO LYS THR LEU SER ASN GLU THR LYS
SEQRES 20 B 907 THR VAL VAL GLN VAL ARG THR PHE GLN ASP LEU LEU LYS
SEQRES 21 B 907 ASP GLU TYR ASP ALA ASP LEU PHE ASP TYR TYR ALA SER
SEQRES 22 B 907 SER GLN LEU VAL LEU ALA SER LEU ASP GLY THR VAL LYS
SEQRES 23 B 907 GLU VAL GLY VAL PRO ALA VAL TYR THR SER LEU ASP PRO
SEQRES 24 B 907 SER THR ASP HIS LYS TYR LEU LEU VAL SER SER LEU HIS
SEQRES 25 B 907 ARG PRO TYR SER PHE ILE VAL PRO CYS GLY ARG PHE PRO
SEQRES 26 B 907 LYS LYS VAL GLU VAL TRP THR THR ASP GLY ARG PHE VAL
SEQRES 27 B 907 ARG GLN LEU CYS ASP LEU PRO LEU ALA GLU ASP ILE PRO
SEQRES 28 B 907 ILE ALA SER ASN SER VAL ARG LYS GLY MET ARG SER ILE
SEQRES 29 B 907 ASN TRP ARG ALA ASP LYS PRO SER THR LEU TYR TRP ALA
SEQRES 30 B 907 GLU THR GLN ASP GLY GLY ASP ALA LYS MET GLU VAL SER
SEQRES 31 B 907 PRO ARG ASP ILE VAL TYR MET GLN SER ALA GLU PRO LEU
SEQRES 32 B 907 ALA GLY GLU GLU PRO GLU VAL LEU HIS LYS LEU ASP LEU
SEQRES 33 B 907 ARG TYR GLY GLY ILE SER TRP CYS ASP ASP THR LEU ALA
SEQRES 34 B 907 LEU VAL TYR GLU SER TRP TYR LYS THR ARG ARG THR ARG
SEQRES 35 B 907 THR TRP VAL ILE SER PRO GLY SER ASN ASP VAL SER PRO
SEQRES 36 B 907 ARG ILE LEU PHE ASP ARG SER SER GLU ASP VAL TYR SER
SEQRES 37 B 907 ASP PRO GLY SER THR MET LEU ARG ARG THR ASP ALA GLY
SEQRES 38 B 907 THR TYR VAL ILE ALA LYS ILE LYS LYS GLU ASN ASP GLU
SEQRES 39 B 907 GLY THR TYR VAL LEU LEU ASN GLY SER GLY ALA THR PRO
SEQRES 40 B 907 GLN GLY ASN VAL PRO PHE LEU ASP LEU PHE ASP ILE ASN
SEQRES 41 B 907 THR GLY ASN LYS GLU ARG ILE TRP GLU SER ASP LYS GLU
SEQRES 42 B 907 LYS TYR PHE GLU THR VAL VAL ALA LEU MET SER ASP GLN
SEQRES 43 B 907 LYS GLU GLY ASP LEU LYS MET GLU GLU LEU LYS ILE LEU
SEQRES 44 B 907 THR SER LYS GLU SER LYS THR GLU ASN THR GLN TYR SER
SEQRES 45 B 907 LEU GLN LEU TRP PRO ASP ARG LYS VAL GLN GLN ILE THR
SEQRES 46 B 907 ASN PHE PRO HIS PRO TYR PRO GLN LEU ALA SER LEU GLN
SEQRES 47 B 907 LYS GLU MET ILE ARG TYR GLN ARG LYS ASP GLY VAL GLN
SEQRES 48 B 907 LEU THR ALA THR LEU TYR LEU PRO PRO GLY TYR ASP PRO
SEQRES 49 B 907 SER LYS ASP GLY PRO LEU PRO CYS LEU PHE TRP SER TYR
SEQRES 50 B 907 PRO GLY GLU PHE LYS SER LYS ASP ALA ALA GLY GLN VAL
SEQRES 51 B 907 ARG GLY SER PRO ASN GLU PHE ALA GLY ILE GLY SER THR
SEQRES 52 B 907 SER ALA LEU LEU TRP LEU ALA ARG ARG PHE ALA ILE LEU
SEQRES 53 B 907 SER GLY PRO THR ILE PRO ILE ILE GLY GLU GLY ASP GLU
SEQRES 54 B 907 GLU ALA ASN ASP ARG TYR VAL GLU GLN LEU VAL ALA SER
SEQRES 55 B 907 ALA GLU ALA ALA VAL GLU GLU VAL VAL ARG ARG GLY VAL
SEQRES 56 B 907 ALA ASP ARG SER LYS ILE ALA VAL GLY GLY HIS SER TYR
SEQRES 57 B 907 GLY ALA PHE MET THR ALA ASN LEU LEU ALA HIS ALA PRO
SEQRES 58 B 907 HIS LEU PHE ALA CYS GLY ILE ALA ARG SER GLY ALA TYR
SEQRES 59 B 907 ASN ARG THR LEU THR PRO PHE GLY PHE GLN ASN GLU ASP
SEQRES 60 B 907 ARG THR LEU TRP GLU ALA THR ASN VAL TYR VAL GLU MET
SEQRES 61 B 907 SER PRO PHE MET SER ALA ASN LYS ILE LYS LYS PRO ILE
SEQRES 62 B 907 LEU LEU ILE HIS GLY GLU GLU ASN ASN ASN PRO GLY THR
SEQRES 63 B 907 LEU THR MET GLN SER ASP ARG PHE PHE ASN ALA LEU LYS
SEQRES 64 B 907 GLY HIS GLY ALA LEU CYS ARG LEU VAL VAL LEU PRO HIS
SEQRES 65 B 907 GLU SER HIS GLY TYR SER ALA ARG GLU SER ILE MET HIS
SEQRES 66 B 907 VAL LEU TRP GLU THR ASP ARG TRP LEU GLN LYS TYR CYS
SEQRES 67 B 907 VAL PRO ASN THR SER ASP ALA ASP THR SER PRO ASP GLN
SEQRES 68 B 907 SER LYS GLU GLY SER ASP SER ALA ASP LYS VAL SER THR
SEQRES 69 B 907 GLY THR GLY GLY GLY ASN PRO GLU PHE GLY GLU HIS GLU
SEQRES 70 B 907 VAL HIS SER LYS LEU ARG ARG SER LEU LEU
SEQRES 1 A 907 HIS HIS HIS HIS HIS HIS GLY GLY ALA SER ARG SER ALA
SEQRES 2 A 907 SER ARG LEU ARG SER LEU ALA SER ALA CYS SER GLY GLY
SEQRES 3 A 907 ALA GLU ASP GLY GLY GLY THR SER ASN GLY SER LEU SER
SEQRES 4 A 907 ALA SER ALA THR ALA THR GLU ASP ASP GLU LEU ALA ILE
SEQRES 5 A 907 GLY THR GLY TYR ARG LEU PRO PRO PRO GLU ILE ARG ASP
SEQRES 6 A 907 ILE VAL ASP ALA PRO PRO VAL PRO ALA LEU SER PHE SER
SEQRES 7 A 907 PRO HIS ARG ASP LYS ILE LEU PHE LEU LYS ARG ARG ALA
SEQRES 8 A 907 LEU PRO PRO LEU ALA ASP LEU ALA ARG PRO GLU GLU LYS
SEQRES 9 A 907 LEU ALA GLY VAL ARG ILE ASP GLY TYR CYS ASN THR ARG
SEQRES 10 A 907 SER ARG MET SER PHE TYR THR GLY LEU GLY ILE HIS GLN
SEQRES 11 A 907 LEU LEU PRO ASP GLY THR LEU SER PRO GLU LYS GLU ILE
SEQRES 12 A 907 THR GLY ILE PRO ASP GLY GLY LYS ILE ASN PHE VAL THR
SEQRES 13 A 907 TRP SER ASN ASP GLY LYS HIS LEU ALA PHE SER ILE ARG
SEQRES 14 A 907 VAL ASP GLU ASN GLY ASN SER SER LYS PRO VAL VAL TRP
SEQRES 15 A 907 VAL ALA ASP VAL GLU THR GLY VAL ALA ARG PRO LEU PHE
SEQRES 16 A 907 ASN SER GLN ASP ILE PHE LEU ASN ALA ILE PHE GLU SER
SEQRES 17 A 907 PHE VAL TRP ILE ASP ASN SER THR LEU LEU VAL SER THR
SEQRES 18 A 907 ILE PRO SER SER ARG GLY GLU PRO PRO LYS LYS PRO LEU
SEQRES 19 A 907 VAL PRO SER GLY PRO LYS THR LEU SER ASN GLU THR LYS
SEQRES 20 A 907 THR VAL VAL GLN VAL ARG THR PHE GLN ASP LEU LEU LYS
SEQRES 21 A 907 ASP GLU TYR ASP ALA ASP LEU PHE ASP TYR TYR ALA SER
SEQRES 22 A 907 SER GLN LEU VAL LEU ALA SER LEU ASP GLY THR VAL LYS
SEQRES 23 A 907 GLU VAL GLY VAL PRO ALA VAL TYR THR SER LEU ASP PRO
SEQRES 24 A 907 SER THR ASP HIS LYS TYR LEU LEU VAL SER SER LEU HIS
SEQRES 25 A 907 ARG PRO TYR SER PHE ILE VAL PRO CYS GLY ARG PHE PRO
SEQRES 26 A 907 LYS LYS VAL GLU VAL TRP THR THR ASP GLY ARG PHE VAL
SEQRES 27 A 907 ARG GLN LEU CYS ASP LEU PRO LEU ALA GLU ASP ILE PRO
SEQRES 28 A 907 ILE ALA SER ASN SER VAL ARG LYS GLY MET ARG SER ILE
SEQRES 29 A 907 ASN TRP ARG ALA ASP LYS PRO SER THR LEU TYR TRP ALA
SEQRES 30 A 907 GLU THR GLN ASP GLY GLY ASP ALA LYS MET GLU VAL SER
SEQRES 31 A 907 PRO ARG ASP ILE VAL TYR MET GLN SER ALA GLU PRO LEU
SEQRES 32 A 907 ALA GLY GLU GLU PRO GLU VAL LEU HIS LYS LEU ASP LEU
SEQRES 33 A 907 ARG TYR GLY GLY ILE SER TRP CYS ASP ASP THR LEU ALA
SEQRES 34 A 907 LEU VAL TYR GLU SER TRP TYR LYS THR ARG ARG THR ARG
SEQRES 35 A 907 THR TRP VAL ILE SER PRO GLY SER ASN ASP VAL SER PRO
SEQRES 36 A 907 ARG ILE LEU PHE ASP ARG SER SER GLU ASP VAL TYR SER
SEQRES 37 A 907 ASP PRO GLY SER THR MET LEU ARG ARG THR ASP ALA GLY
SEQRES 38 A 907 THR TYR VAL ILE ALA LYS ILE LYS LYS GLU ASN ASP GLU
SEQRES 39 A 907 GLY THR TYR VAL LEU LEU ASN GLY SER GLY ALA THR PRO
SEQRES 40 A 907 GLN GLY ASN VAL PRO PHE LEU ASP LEU PHE ASP ILE ASN
SEQRES 41 A 907 THR GLY ASN LYS GLU ARG ILE TRP GLU SER ASP LYS GLU
SEQRES 42 A 907 LYS TYR PHE GLU THR VAL VAL ALA LEU MET SER ASP GLN
SEQRES 43 A 907 LYS GLU GLY ASP LEU LYS MET GLU GLU LEU LYS ILE LEU
SEQRES 44 A 907 THR SER LYS GLU SER LYS THR GLU ASN THR GLN TYR SER
SEQRES 45 A 907 LEU GLN LEU TRP PRO ASP ARG LYS VAL GLN GLN ILE THR
SEQRES 46 A 907 ASN PHE PRO HIS PRO TYR PRO GLN LEU ALA SER LEU GLN
SEQRES 47 A 907 LYS GLU MET ILE ARG TYR GLN ARG LYS ASP GLY VAL GLN
SEQRES 48 A 907 LEU THR ALA THR LEU TYR LEU PRO PRO GLY TYR ASP PRO
SEQRES 49 A 907 SER LYS ASP GLY PRO LEU PRO CYS LEU PHE TRP SER TYR
SEQRES 50 A 907 PRO GLY GLU PHE LYS SER LYS ASP ALA ALA GLY GLN VAL
SEQRES 51 A 907 ARG GLY SER PRO ASN GLU PHE ALA GLY ILE GLY SER THR
SEQRES 52 A 907 SER ALA LEU LEU TRP LEU ALA ARG ARG PHE ALA ILE LEU
SEQRES 53 A 907 SER GLY PRO THR ILE PRO ILE ILE GLY GLU GLY ASP GLU
SEQRES 54 A 907 GLU ALA ASN ASP ARG TYR VAL GLU GLN LEU VAL ALA SER
SEQRES 55 A 907 ALA GLU ALA ALA VAL GLU GLU VAL VAL ARG ARG GLY VAL
SEQRES 56 A 907 ALA ASP ARG SER LYS ILE ALA VAL GLY GLY HIS SER TYR
SEQRES 57 A 907 GLY ALA PHE MET THR ALA ASN LEU LEU ALA HIS ALA PRO
SEQRES 58 A 907 HIS LEU PHE ALA CYS GLY ILE ALA ARG SER GLY ALA TYR
SEQRES 59 A 907 ASN ARG THR LEU THR PRO PHE GLY PHE GLN ASN GLU ASP
SEQRES 60 A 907 ARG THR LEU TRP GLU ALA THR ASN VAL TYR VAL GLU MET
SEQRES 61 A 907 SER PRO PHE MET SER ALA ASN LYS ILE LYS LYS PRO ILE
SEQRES 62 A 907 LEU LEU ILE HIS GLY GLU GLU ASN ASN ASN PRO GLY THR
SEQRES 63 A 907 LEU THR MET GLN SER ASP ARG PHE PHE ASN ALA LEU LYS
SEQRES 64 A 907 GLY HIS GLY ALA LEU CYS ARG LEU VAL VAL LEU PRO HIS
SEQRES 65 A 907 GLU SER HIS GLY TYR SER ALA ARG GLU SER ILE MET HIS
SEQRES 66 A 907 VAL LEU TRP GLU THR ASP ARG TRP LEU GLN LYS TYR CYS
SEQRES 67 A 907 VAL PRO ASN THR SER ASP ALA ASP THR SER PRO ASP GLN
SEQRES 68 A 907 SER LYS GLU GLY SER ASP SER ALA ASP LYS VAL SER THR
SEQRES 69 A 907 GLY THR GLY GLY GLY ASN PRO GLU PHE GLY GLU HIS GLU
SEQRES 70 A 907 VAL HIS SER LYS LEU ARG ARG SER LEU LEU
HELIX 1 AA1 PRO B 114 ASP B 122 1 9
HELIX 2 AA2 PRO B 148 ALA B 153 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 TYR B 645 ALA B 649 5 5
HELIX 6 AA6 SER B 697 GLY B 702 1 6
HELIX 7 AA7 SER B 718 ALA B 724 5 7
HELIX 8 AA8 ARG B 748 ARG B 767 1 20
HELIX 9 AA9 SER B 781 ALA B 794 1 14
HELIX 10 AB1 ALA B 827 GLU B 833 1 7
HELIX 11 AB2 MET B 834 SER B 835 5 2
HELIX 12 AB3 PRO B 836 ALA B 840 5 5
HELIX 13 AB4 LEU B 861 HIS B 875 1 15
HELIX 14 AB5 ALA B 893 TYR B 911 1 19
HELIX 15 AB6 PRO A 114 ASP A 122 1 9
HELIX 16 AB7 PRO A 148 LEU A 152 5 5
HELIX 17 AB8 ASP A 315 SER A 327 1 13
HELIX 18 AB9 PRO A 374 PHE A 378 5 5
HELIX 19 AC1 PRO A 631 ARG A 633 5 3
HELIX 20 AC2 ALA A 719 ARG A 725 5 7
HELIX 21 AC3 ALA A 745 ASP A 747 5 3
HELIX 22 AC4 ARG A 748 GLY A 768 1 21
HELIX 23 AC5 TYR A 782 ALA A 794 1 13
HELIX 24 AC6 THR A 823 GLU A 826 5 4
HELIX 25 AC7 ALA A 827 MET A 834 1 8
HELIX 26 AC8 PRO A 836 ALA A 840 5 5
HELIX 27 AC9 MET A 863 GLY A 874 1 12
HELIX 28 AD1 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 LEU B 141 -1 O LEU B 139 N SER B 130
SHEET 3 AA1 4 GLY B 181 GLN B 184 -1 O GLY B 181 N PHE B 140
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 157 LEU B 159 0
SHEET 2 AA2 3 VAL B 162 ASP B 165 -1 O VAL B 162 N LEU B 159
SHEET 3 AA2 3 THR B 170 ARG B 171 -1 O THR B 170 N ASP B 165
SHEET 1 AA3 4 GLY B 204 THR B 210 0
SHEET 2 AA3 4 HIS B 217 VAL B 224 -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 SER B 328 SER B 334 -1 O GLN B 329 N THR B 275
SHEET 4 AA4 4 VAL B 339 ALA B 346 -1 O LYS B 340 N LEU B 332
SHEET 1 AA5 9 LYS B 294 SER B 297 0
SHEET 2 AA5 9 CYS A 879 LEU A 884 -1 O VAL A 883 N LYS B 294
SHEET 3 AA5 9 ILE A 847 GLY A 852 1 N HIS A 851 O LEU A 884
SHEET 4 AA5 9 CYS A 800 ARG A 804 1 N ALA A 803 O LEU A 848
SHEET 5 AA5 9 ALA A 770 GLY A 779 1 N VAL A 777 O ILE A 802
SHEET 6 AA5 9 LEU A 684 SER A 690 1 N PHE A 688 O ALA A 776
SHEET 7 AA5 9 ALA A 728 SER A 731 1 O LEU A 730 N LEU A 687
SHEET 8 AA5 9 GLN A 665 LEU A 672 -1 N TYR A 671 O ILE A 729
SHEET 9 AA5 9 GLN A 652 GLN A 659 -1 N TYR A 658 O LEU A 666
SHEET 1 AA6 4 LEU B 351 PRO B 353 0
SHEET 2 AA6 4 TYR B 359 VAL B 362 -1 O LEU B 361 N ASP B 352
SHEET 3 AA6 4 VAL B 382 THR B 386 -1 O TRP B 385 N LEU B 360
SHEET 4 AA6 4 PHE B 391 CYS B 396 -1 O ARG B 393 N VAL B 384
SHEET 1 AA7 4 ARG B 416 TRP B 420 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 TYR B 450 N TRP B 430
SHEET 4 AA7 4 GLU B 463 LEU B 468 -1 O LEU B 465 N VAL B 449
SHEET 1 AA8 4 ARG B 471 ASP B 479 0
SHEET 2 AA8 4 LEU B 482 TRP B 489 -1 O TYR B 486 N GLY B 473
SHEET 3 AA8 4 ARG B 494 ILE B 500 -1 O ARG B 496 N GLU B 487
SHEET 4 AA8 4 ARG B 510 SER B 516 -1 O ARG B 515 N THR B 495
SHEET 1 AA9 4 SER B 526 THR B 527 0
SHEET 2 AA9 4 TYR B 551 ALA B 559 -1 O ASN B 555 N SER B 526
SHEET 3 AA9 4 ASN B 564 ASP B 572 -1 O PHE B 571 N VAL B 552
SHEET 4 AA9 4 LYS B 578 GLU B 583 -1 O GLU B 579 N LEU B 570
SHEET 1 AB1 4 SER B 526 THR B 527 0
SHEET 2 AB1 4 TYR B 551 ALA B 559 -1 O ASN B 555 N SER B 526
SHEET 3 AB1 4 LYS B 541 LYS B 543 -1 N ILE B 542 O TYR B 551
SHEET 4 AB1 4 LEU B 605 LYS B 606 1 O LEU B 605 N LYS B 543
SHEET 1 AB2 2 LEU B 529 ARG B 531 0
SHEET 2 AB2 2 TYR B 537 ILE B 539 -1 O VAL B 538 N ARG B 530
SHEET 1 AB3 4 PHE B 590 LEU B 596 0
SHEET 2 AB3 4 LYS B 611 GLU B 617 -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 LYS B 634 N LEU B 629
SHEET 1 AB4 9 GLN B 652 GLN B 659 0
SHEET 2 AB4 9 GLN B 665 LEU B 672 -1 O ALA B 668 N ILE B 656
SHEET 3 AB4 9 ILE B 729 SER B 731 -1 O SER B 731 N THR B 669
SHEET 4 AB4 9 PHE B 688 TRP B 689 1 N TRP B 689 O LEU B 730
SHEET 5 AB4 9 ALA B 776 GLY B 779 1 O ALA B 776 N PHE B 688
SHEET 6 AB4 9 CYS B 800 ARG B 804 1 O CYS B 800 N VAL B 777
SHEET 7 AB4 9 ILE B 847 GLY B 852 1 O LEU B 848 N ALA B 803
SHEET 8 AB4 9 CYS B 879 LEU B 884 1 O ARG B 880 N LEU B 849
SHEET 9 AB4 9 LYS A 294 SER A 297 -1 O LEU A 296 N LEU B 881
SHEET 1 AB5 3 ALA A 128 PHE A 131 0
SHEET 2 AB5 3 LYS A 137 LEU A 141 -1 O LEU A 139 N SER A 130
SHEET 3 AB5 3 LEU A 180 GLN A 184 -1 O GLY A 181 N PHE A 140
SHEET 1 AB6 3 GLU A 157 LEU A 159 0
SHEET 2 AB6 3 VAL A 162 ASP A 165 -1 O VAL A 162 N LEU A 159
SHEET 3 AB6 3 THR A 170 ARG A 171 -1 O THR A 170 N ASP A 165
SHEET 1 AB7 3 PHE A 220 ILE A 222 0
SHEET 2 AB7 3 VAL A 234 ALA A 238 -1 O TRP A 236 N PHE A 220
SHEET 3 AB7 3 ALA A 245 PRO A 247 -1 O ARG A 246 N VAL A 237
SHEET 1 AB8 3 THR A 270 THR A 275 0
SHEET 2 AB8 3 GLN A 329 SER A 334 -1 O ALA A 333 N LEU A 271
SHEET 3 AB8 3 VAL A 339 GLU A 341 -1 O LYS A 340 N LEU A 332
SHEET 1 AB9 4 TYR A 348 PRO A 353 0
SHEET 2 AB9 4 TYR A 359 SER A 364 -1 O SER A 363 N THR A 349
SHEET 3 AB9 4 LYS A 381 THR A 386 -1 O TRP A 385 N LEU A 360
SHEET 4 AB9 4 PHE A 391 ASP A 397 -1 O CYS A 396 N VAL A 382
SHEET 1 AC1 3 ALA A 431 THR A 433 0
SHEET 2 AC1 3 ASP A 447 TYR A 450 -1 O ILE A 448 N GLU A 432
SHEET 3 AC1 3 GLU A 463 LYS A 467 -1 O LYS A 467 N ASP A 447
SHEET 1 AC2 4 LEU A 470 ILE A 475 0
SHEET 2 AC2 4 ALA A 483 TRP A 489 -1 O SER A 488 N LEU A 470
SHEET 3 AC2 4 ARG A 494 ILE A 500 -1 O ARG A 496 N GLU A 487
SHEET 4 AC2 4 ARG A 510 ASP A 514 -1 O ILE A 511 N THR A 497
SHEET 1 AC3 4 SER A 526 THR A 527 0
SHEET 2 AC3 4 TYR A 551 GLY A 556 -1 O ASN A 555 N SER A 526
SHEET 3 AC3 4 PHE A 567 ASP A 572 -1 O ASP A 569 N LEU A 554
SHEET 4 AC3 4 ARG A 580 GLU A 583 -1 O TRP A 582 N LEU A 568
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 LYS A 541 LYS A 543 -1 N ILE A 542 O TYR A 551
SHEET 4 AC4 4 LEU A 605 LYS A 606 1 O LEU A 605 N LYS A 543
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 4 PHE A 590 LEU A 596 0
SHEET 2 AC6 4 LYS A 611 GLU A 617 -1 O LEU A 613 N ALA A 595
SHEET 3 AC6 4 GLN A 624 LEU A 629 -1 O GLN A 628 N ILE A 612
SHEET 4 AC6 4 LYS A 634 GLN A 637 -1 O LYS A 634 N LEU A 629
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 6367 ASN B 915
TER 12661 ASN A 915
MASTER 369 0 0 28 96 0 0 612659 2 0 140
END |