HEADER HYDROLASE INHIBITOR 04-JUN-15 5A42
TITLE CRYO-EM SINGLE PARTICLE 3D RECONSTRUCTION OF THE NATIVE CONFORMATION
TITLE 2 OF E. COLI ALPHA-2-MACROGLOBULIN (ECAM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED LIPOPROTEIN YFHM;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 40-1653;
COMPND 5 SYNONYM: ALPHA-2-MACROGLOBULIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: THE EXPRESSED AND PURIFIED SAMPLE CONTAINED THE
COMPND 8 SEQUENCE GPM-A40 TO P1653.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCRI8B
KEYWDS HYDROLASE INHIBITOR, PEPTIDASE INHIBITOR
EXPDTA ELECTRON MICROSCOPY
AUTHOR I.GARCIA-FERRER,P.AREDE,J.GOMEZ-BLANCO,D.LUQUE,S.DUQUERROY,
AUTHOR 2 J.R.CASTON,T.GOULAS,F.X.GOMIS-RUTH
REVDAT 3 23-AUG-17 5A42 1 REMARK
REVDAT 2 19-AUG-15 5A42 1 JRNL
REVDAT 1 29-JUL-15 5A42 0
JRNL AUTH I.GARCIA-FERRER,P.AREDE,J.GOMEZ-BLANCO,D.LUQUE,S.DUQUERROY,
JRNL AUTH 2 J.R.CASTON,T.GOULAS,F.X.GOMIS-RUTH
JRNL TITL STRUCTURAL AND FUNCTIONAL INSIGHTS INTO ESCHERICHIA COLI
JRNL TITL 2 ALPHA2- MACROGLOBULIN ENDOPEPTIDASE SNAP-TRAP INHIBITION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 112 8290 2015
JRNL REFN ISSN 0027-8424
JRNL PMID 26100869
JRNL DOI 10.1073/PNAS.1506538112
REMARK 2
REMARK 2 RESOLUTION. 16.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : UCSF CHIMERA, EMAN, XMIPP
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : CROSS-CORRELATION COEFFICIENT
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : METHOD--RIGID BODY
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) : 16.00
REMARK 3 NUMBER OF PARTICLES : 46842
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: THE FITTED MODEL IS AN HOMOLOGY MODEL BASED ON A
REMARK 3 ECAM HOMOLOG FROM SALMONELLA ENTERICA (PDB CODE 4U48) AND THE
REMARK 3 CRYSTAL STRUCTURES ECAM DOMAINS (PDB CODES 4ZIU,4ZJH,4ZJG,4ZIQ).
REMARK 3 SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-3016.
REMARK 3 (DEPOSITION ID: 13326).
REMARK 4
REMARK 4 5A42 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.
REMARK 100 THE DEPOSITION ID IS D_1290063970.
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 : NATIVE CONFORMATION OF THE E.
REMARK 245 COLI ALPHA-2- MACROGLOBULIN
REMARK 245 (ECAM).
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.01
REMARK 245 SAMPLE SUPPORT DETAILS : CARBON
REMARK 245 SAMPLE VITRIFICATION DETAILS : VITRIFICATION 1 -- CRYOGEN-
REMARK 245 ETHANE, INSTRUMENT- LEICA EM
REMARK 245 CPC, METHOD- BLOTTED FOR 1MIN
REMARK 245 BEFORE PLUNGING WITH 5UL
REMARK 245 PURIFIED SAMPLE.,
REMARK 245 SAMPLE BUFFER : 10MM TRIS-HCL, 75MM NACL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 10-JUN-14
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TECNAI 20
REMARK 245 DETECTOR TYPE : FEI EAGLE (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3500.00
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) : NULL
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : 84269
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: 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 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 A 40
REMARK 465 SER A 41
REMARK 465 SER A 42
REMARK 465 GLU A 43
REMARK 465 ASN A 44
REMARK 465 ALA A 45
REMARK 465 SER A 46
REMARK 465 SER A 47
REMARK 465 ALA A 48
REMARK 465 LYS A 49
REMARK 465 LEU A 50
REMARK 465 SER A 51
REMARK 465 VAL A 52
REMARK 465 PRO A 53
REMARK 465 GLU A 54
REMARK 465 ARG A 55
REMARK 465 GLN A 56
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 66 CG1 CG2
REMARK 470 VAL A 969 CG1 CG2
REMARK 470 GLN A1190 NE2
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 SG CYS A 1187 CD GLN A 1190 1.59
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 78 -138.10 49.34
REMARK 500 ASP A 291 -101.39 -100.14
REMARK 500 HIS A 300 -98.68 55.00
REMARK 500 ASP A 347 -121.06 -100.83
REMARK 500 ALA A 351 -54.78 -133.46
REMARK 500 SER A 385 -141.53 -84.50
REMARK 500 LEU A 532 64.42 -107.93
REMARK 500 GLU A 534 49.38 -107.01
REMARK 500 LEU A 556 -82.05 -91.46
REMARK 500 GLN A 560 104.40 -164.33
REMARK 500 TRP A 577 48.92 -140.32
REMARK 500 GLU A 717 -92.39 -89.63
REMARK 500 ASN A 729 35.06 -83.95
REMARK 500 GLU A 730 14.32 59.13
REMARK 500 ASP A 756 -158.21 43.37
REMARK 500 ARG A 757 -162.07 52.97
REMARK 500 ALA A 778 65.40 -150.13
REMARK 500 TRP A 798 -110.12 -100.49
REMARK 500 GLU A 800 84.73 -163.26
REMARK 500 ASN A 819 52.71 -92.78
REMARK 500 PRO A 832 43.79 -91.47
REMARK 500 ALA A 839 -96.71 55.69
REMARK 500 THR A 840 122.38 65.85
REMARK 500 LEU A 852 -26.92 -152.03
REMARK 500 LYS A 880 81.27 -154.57
REMARK 500 ASN A 885 -55.09 63.65
REMARK 500 ILE A 936 -78.76 -51.39
REMARK 500 GLU A 937 -51.30 -166.70
REMARK 500 GLN A 939 -6.85 61.05
REMARK 500 ARG A 946 -88.38 -129.90
REMARK 500 PHE A 947 24.00 -152.59
REMARK 500 VAL A 962 88.32 54.22
REMARK 500 ASN A 978 -167.68 -78.41
REMARK 500 THR A1004 -101.60 -134.99
REMARK 500 ALA A1071 -141.77 -77.82
REMARK 500 LEU A1105 -68.26 59.46
REMARK 500 GLU A1110 96.43 -162.85
REMARK 500 TRP A1243 -40.61 -132.11
REMARK 500 HIS A1333 42.51 -107.50
REMARK 500 LEU A1402 70.99 46.97
REMARK 500 VAL A1504 -65.01 60.95
REMARK 500 VAL A1619 -79.00 -131.59
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 ARG A 804 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-3016 RELATED DB: EMDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PURIFIED SAMPLE CONTAINED FROM A40 TO P1653
DBREF 5A42 A 40 1653 UNP P76578 YFHM_ECOLI 40 1653
SEQRES 1 A 1614 ALA SER SER GLU ASN ALA SER SER ALA LYS LEU SER VAL
SEQRES 2 A 1614 PRO GLU ARG GLN LYS LEU ALA GLN GLN SER ALA GLY LYS
SEQRES 3 A 1614 VAL LEU THR LEU LEU ASP LEU SER GLU VAL GLN LEU ASP
SEQRES 4 A 1614 GLY ALA ALA THR LEU VAL LEU THR PHE SER ILE PRO LEU
SEQRES 5 A 1614 ASP PRO ASP GLN ASP PHE SER ARG VAL ILE HIS VAL VAL
SEQRES 6 A 1614 ASP LYS LYS SER GLY LYS VAL ASP GLY ALA TRP GLU LEU
SEQRES 7 A 1614 SER ASP ASN LEU LYS GLU LEU ARG LEU ARG HIS LEU GLU
SEQRES 8 A 1614 PRO LYS ARG ASP LEU ILE VAL THR ILE GLY LYS GLU VAL
SEQRES 9 A 1614 LYS ALA LEU ASN ASN ALA THR PHE SER LYS ASP TYR GLU
SEQRES 10 A 1614 LYS THR ILE THR THR ARG ASP ILE GLN PRO SER VAL GLY
SEQRES 11 A 1614 PHE ALA SER ARG GLY SER LEU LEU PRO GLY LYS VAL VAL
SEQRES 12 A 1614 GLU GLY LEU PRO VAL MET ALA LEU ASN VAL ASN ASN VAL
SEQRES 13 A 1614 ASP VAL ASN PHE PHE ARG VAL LYS PRO GLU SER LEU PRO
SEQRES 14 A 1614 ALA PHE ILE SER GLN TRP GLU TYR ARG ASN SER LEU ALA
SEQRES 15 A 1614 ASN TRP GLN SER ASP LYS LEU LEU GLN MET ALA ASP LEU
SEQRES 16 A 1614 VAL TYR THR GLY ARG PHE ASP LEU ASN PRO ALA ARG ASN
SEQRES 17 A 1614 THR ARG GLU LYS LEU LEU LEU PRO LEU GLY ASP ILE LYS
SEQRES 18 A 1614 PRO LEU GLN GLN ALA GLY VAL TYR LEU ALA VAL MET ASN
SEQRES 19 A 1614 GLN ALA GLY ARG TYR ASP TYR SER ASN PRO ALA THR LEU
SEQRES 20 A 1614 PHE THR LEU SER ASP ILE GLY VAL SER ALA HIS ARG TYR
SEQRES 21 A 1614 HIS ASN ARG LEU ASP ILE PHE THR GLN SER LEU GLU ASN
SEQRES 22 A 1614 GLY ALA ALA GLN GLN GLY ILE GLU VAL SER LEU LEU ASN
SEQRES 23 A 1614 GLU LYS GLY GLN THR LEU THR GLN ALA THR SER ASP ALA
SEQRES 24 A 1614 GLN GLY HIS VAL GLN LEU GLU ASN ASP LYS ASN ALA ALA
SEQRES 25 A 1614 LEU LEU LEU ALA ARG LYS ASP GLY GLN THR THR LEU LEU
SEQRES 26 A 1614 ASP LEU LYS LEU PRO ALA LEU ASP LEU ALA GLU PHE ASN
SEQRES 27 A 1614 ILE ALA GLY ALA PRO GLY TYR SER LYS GLN PHE PHE MET
SEQRES 28 A 1614 PHE GLY PRO ARG ASP LEU TYR ARG PRO GLY GLU THR VAL
SEQRES 29 A 1614 ILE LEU ASN GLY LEU LEU ARG ASP ALA ASP GLY LYS ALA
SEQRES 30 A 1614 LEU PRO ASN GLN PRO ILE LYS LEU ASP VAL ILE LYS PRO
SEQRES 31 A 1614 ASP GLY GLN VAL LEU ARG SER VAL VAL SER GLN PRO GLU
SEQRES 32 A 1614 ASN GLY LEU TYR HIS PHE THR TRP PRO LEU ASP SER ASN
SEQRES 33 A 1614 ALA ALA THR GLY MET TRP HIS ILE ARG ALA ASN THR GLY
SEQRES 34 A 1614 ASP ASN GLN TYR ARG MET TRP ASP PHE HIS VAL GLU ASP
SEQRES 35 A 1614 PHE MET PRO GLU ARG MET ALA LEU ASN LEU THR GLY GLU
SEQRES 36 A 1614 LYS THR PRO LEU THR PRO LYS ASP GLU VAL LYS PHE SER
SEQRES 37 A 1614 VAL VAL GLY TYR TYR LEU TYR GLY ALA PRO ALA ASN GLY
SEQRES 38 A 1614 ASN THR LEU GLN GLY GLN LEU PHE LEU ARG PRO LEU ARG
SEQRES 39 A 1614 GLU ALA VAL SER ALA LEU PRO GLY PHE GLU PHE GLY ASP
SEQRES 40 A 1614 ILE ALA ALA GLU ASN LEU SER ARG THR LEU ASP GLU VAL
SEQRES 41 A 1614 GLN LEU THR LEU ASP ASP LYS GLY ARG GLY GLU VAL SER
SEQRES 42 A 1614 THR GLU SER GLN TRP LYS GLU THR HIS SER PRO LEU GLN
SEQRES 43 A 1614 VAL ILE PHE GLN GLY SER LEU LEU GLU SER GLY GLY ARG
SEQRES 44 A 1614 PRO VAL THR ARG ARG ALA GLU GLN ALA ILE TRP PRO ALA
SEQRES 45 A 1614 ASP ALA LEU PRO GLY ILE ARG PRO GLN PHE ALA SER LYS
SEQRES 46 A 1614 SER VAL TYR ASP TYR ARG THR ASP SER THR VAL LYS GLN
SEQRES 47 A 1614 PRO ILE VAL ASP GLU GLY SER ASN ALA ALA PHE ASP ILE
SEQRES 48 A 1614 VAL TYR SER ASP ALA GLN GLY VAL LYS LYS ALA VAL SER
SEQRES 49 A 1614 GLY LEU GLN VAL ARG LEU ILE ARG GLU ARG ARG ASP TYR
SEQRES 50 A 1614 TYR TRP ASN TRP SER GLU ASP GLU GLY TRP GLN SER GLN
SEQRES 51 A 1614 PHE ASP GLN LYS ASP LEU ILE GLU ASN GLU GLN THR LEU
SEQRES 52 A 1614 ASP LEU LYS ALA ASP GLU THR GLY LYS VAL SER PHE PRO
SEQRES 53 A 1614 VAL GLU TRP GLY ALA TYR ARG LEU GLU VAL LYS ALA PRO
SEQRES 54 A 1614 ASN GLU ALA VAL SER SER VAL ARG PHE TRP ALA GLY TYR
SEQRES 55 A 1614 SER TRP GLN ASP ASN SER ASP GLY SER GLY ALA VAL ARG
SEQRES 56 A 1614 PRO ASP ARG VAL THR LEU LYS LEU ASP LYS ALA SER TYR
SEQRES 57 A 1614 ARG PRO GLY ASP THR ILE LYS LEU HIS ILE ALA ALA PRO
SEQRES 58 A 1614 THR ALA GLY LYS GLY TYR ALA MET VAL GLU SER SER GLU
SEQRES 59 A 1614 GLY PRO LEU TRP TRP GLN GLU ILE ASP VAL ARG ALA GLN
SEQRES 60 A 1614 GLY LEU ASP LEU THR ILE PRO VAL ASP LYS THR TRP ASN
SEQRES 61 A 1614 ARG HIS ASP LEU TYR LEU SER THR LEU VAL VAL ARG PRO
SEQRES 62 A 1614 GLY ASP LYS SER ARG SER ALA THR PRO LYS ARG ALA VAL
SEQRES 63 A 1614 GLY VAL LEU HIS LEU PRO LEU GLY ASP GLU ASN ARG ARG
SEQRES 64 A 1614 LEU ASP LEU ALA LEU GLU THR PRO ALA LYS MET ARG PRO
SEQRES 65 A 1614 ASN GLN PRO LEU THR VAL LYS ILE LYS ALA SER THR LYS
SEQRES 66 A 1614 ASN GLY GLU LYS PRO LYS GLN VAL ASN VAL LEU VAL SER
SEQRES 67 A 1614 ALA VAL ASP SER GLY VAL LEU ASN ILE THR ASP TYR VAL
SEQRES 68 A 1614 THR PRO ASP PRO TRP GLN ALA PHE PHE GLY GLN LYS ARG
SEQRES 69 A 1614 TYR GLY ALA ASP ILE TYR ASP ILE TYR GLY GLN VAL ILE
SEQRES 70 A 1614 GLU GLY GLN GLY ARG LEU ALA ALA LEU ARG PHE GLY GLY
SEQRES 71 A 1614 ASP GLY ASP GLU LEU LYS ARG GLY GLY LYS PRO PRO VAL
SEQRES 72 A 1614 ASN HIS VAL ASN ILE VAL VAL GLN GLN ALA LEU PRO VAL
SEQRES 73 A 1614 THR LEU ASN GLU GLN GLY GLU GLY SER VAL THR LEU PRO
SEQRES 74 A 1614 ILE GLY ASP PHE ASN GLY GLU LEU ARG VAL MET ALA GLN
SEQRES 75 A 1614 ALA TRP THR ALA ASP ASP PHE GLY SER ASN GLU SER LYS
SEQRES 76 A 1614 VAL ILE VAL ALA ALA PRO VAL ILE ALA GLU LEU ASN MET
SEQRES 77 A 1614 PRO ARG PHE MET ALA SER GLY ASP THR SER ARG LEU THR
SEQRES 78 A 1614 LEU ASP ILE THR ASN LEU THR ASP LYS PRO GLN LYS LEU
SEQRES 79 A 1614 ASN VAL ALA LEU THR ALA SER GLY LEU LEU GLU LEU VAL
SEQRES 80 A 1614 SER ASP SER PRO ALA ALA VAL GLU LEU ALA PRO GLY VAL
SEQRES 81 A 1614 ARG THR THR LEU PHE ILE PRO VAL ARG ALA LEU PRO GLY
SEQRES 82 A 1614 TYR GLY ASP GLY GLU ILE GLN ALA THR ILE SER GLY LEU
SEQRES 83 A 1614 ALA LEU PRO GLY GLU THR VAL ALA ASP GLN HIS LYS GLN
SEQRES 84 A 1614 TRP LYS ILE GLY VAL ARG PRO ALA PHE PRO ALA GLN THR
SEQRES 85 A 1614 VAL ASN TYR GLY THR ALA LEU GLN PRO GLY GLU THR TRP
SEQRES 86 A 1614 ALA ILE PRO ALA ASP GLY LEU GLN ASN PHE SER PRO VAL
SEQRES 87 A 1614 THR LEU GLU GLY GLN LEU LEU LEU SER GLY LYS PRO PRO
SEQRES 88 A 1614 LEU ASN ILE ALA ARG TYR ILE LYS GLU LEU LYS ALA TYR
SEQRES 89 A 1614 PRO TYR GLY CYS LEU GLU GLN THR ALA SER GLY LEU PHE
SEQRES 90 A 1614 PRO SER LEU TYR THR ASN ALA ALA GLN LEU GLN ALA LEU
SEQRES 91 A 1614 GLY ILE LYS GLY ASP SER ASP GLU LYS ARG ARG ALA SER
SEQRES 92 A 1614 VAL ASP ILE GLY ILE SER ARG LEU LEU GLN MET GLN ARG
SEQRES 93 A 1614 ASP ASN GLY GLY PHE ALA LEU TRP ASP LYS ASN GLY ASP
SEQRES 94 A 1614 GLU GLU TYR TRP LEU THR ALA TYR VAL MET ASP PHE LEU
SEQRES 95 A 1614 VAL ARG ALA GLY GLU GLN GLY TYR SER VAL PRO THR ASP
SEQRES 96 A 1614 ALA ILE ASN ARG GLY ASN GLU ARG LEU LEU ARG TYR LEU
SEQRES 97 A 1614 GLN ASP PRO GLY MET MET SER ILE PRO TYR ALA ASP ASN
SEQRES 98 A 1614 LEU LYS ALA SER LYS PHE ALA VAL GLN SER TYR ALA ALA
SEQRES 99 A 1614 LEU VAL LEU ALA ARG GLN GLN LYS ALA PRO LEU GLY ALA
SEQRES 100 A 1614 LEU ARG GLU ILE TRP GLU HIS ARG ALA ASP ALA ALA SER
SEQRES 101 A 1614 GLY LEU PRO LEU LEU GLN LEU GLY VAL ALA LEU LYS THR
SEQRES 102 A 1614 MET GLY ASP ALA THR ARG GLY GLU GLU ALA ILE ALA LEU
SEQRES 103 A 1614 ALA LEU LYS THR PRO ARG ASN SER ASP GLU ARG ILE TRP
SEQRES 104 A 1614 LEU GLY ASP TYR GLY SER SER LEU ARG ASP ASN ALA LEU
SEQRES 105 A 1614 MET LEU SER LEU LEU GLU GLU ASN LYS LEU LEU PRO ASP
SEQRES 106 A 1614 GLU GLN TYR THR LEU LEU ASN THR LEU SER GLN GLN ALA
SEQRES 107 A 1614 PHE GLY GLU ARG TRP LEU SER THR GLN GLU SER ASN ALA
SEQRES 108 A 1614 LEU PHE LEU ALA ALA ARG THR ILE GLN ASP LEU PRO GLY
SEQRES 109 A 1614 LYS TRP GLN ALA GLN THR SER PHE SER ALA GLU GLN LEU
SEQRES 110 A 1614 THR GLY GLU LYS ALA GLN ASN SER ASN LEU ASN SER ASP
SEQRES 111 A 1614 GLN LEU VAL THR LEU GLN VAL SER ASN SER GLY ASP GLN
SEQRES 112 A 1614 PRO LEU TRP LEU ARG MET ASP ALA SER GLY TYR PRO GLN
SEQRES 113 A 1614 SER ALA PRO LEU PRO ALA ASN ASN VAL LEU GLN ILE GLU
SEQRES 114 A 1614 ARG HIS ILE LEU GLY THR ASP GLY LYS SER LYS SER LEU
SEQRES 115 A 1614 ASP SER LEU ARG SER GLY ASP LEU VAL LEU VAL TRP LEU
SEQRES 116 A 1614 GLN VAL LYS ALA SER ASN SER VAL PRO ASP ALA LEU VAL
SEQRES 117 A 1614 VAL ASP LEU LEU PRO ALA GLY LEU GLU LEU GLU ASN GLN
SEQRES 118 A 1614 ASN LEU ALA ASN GLY SER ALA SER LEU GLU GLN SER GLY
SEQRES 119 A 1614 GLY GLU VAL GLN ASN LEU LEU ASN GLN MET GLN GLN ALA
SEQRES 120 A 1614 SER ILE LYS HIS ILE GLU PHE ARG ASP ASP ARG PHE VAL
SEQRES 121 A 1614 ALA ALA VAL ALA VAL ASP GLU TYR GLN PRO VAL THR LEU
SEQRES 122 A 1614 VAL TYR LEU ALA ARG ALA VAL THR PRO GLY THR TYR GLN
SEQRES 123 A 1614 VAL PRO GLN PRO MET VAL GLU SER MET TYR VAL PRO GLN
SEQRES 124 A 1614 TRP ARG ALA THR GLY ALA ALA GLU ASP LEU LEU ILE VAL
SEQRES 125 A 1614 ARG PRO
HELIX 1 1 LEU A 58 ALA A 63 1 6
HELIX 2 2 ASP A 96 VAL A 100 1 5
HELIX 3 3 LYS A 180 GLY A 184 5 5
HELIX 4 4 SER A 206 ASN A 218 1 13
HELIX 5 5 SER A 225 GLN A 230 1 6
HELIX 6 6 ILE A 259 GLN A 264 5 6
HELIX 7 7 ASP A 854 ARG A 857 5 4
HELIX 8 8 SER A 901 ASP A 908 1 8
HELIX 9 9 ASP A 913 GLY A 920 1 8
HELIX 10 10 ASP A 952 GLY A 957 1 6
HELIX 11 11 PRO A 1147 GLN A 1152 5 6
HELIX 12 12 ASN A 1172 TYR A 1183 1 12
HELIX 13 13 CYS A 1187 THR A 1201 1 15
HELIX 14 14 ASN A 1202 LEU A 1209 1 8
HELIX 15 15 SER A 1215 MET A 1233 1 19
HELIX 16 16 GLU A 1250 GLN A 1267 1 18
HELIX 17 17 PRO A 1272 ASP A 1289 1 18
HELIX 18 18 PRO A 1290 MET A 1293 5 4
HELIX 19 19 ASN A 1300 GLN A 1319 1 20
HELIX 20 20 PRO A 1323 HIS A 1333 1 11
HELIX 21 21 ARG A 1334 ALA A 1337 5 4
HELIX 22 22 SER A 1339 MET A 1353 1 15
HELIX 23 23 ASP A 1355 LEU A 1367 1 13
HELIX 24 24 SER A 1384 ASN A 1399 1 16
HELIX 25 25 LEU A 1402 PHE A 1418 1 17
HELIX 26 26 SER A 1424 ILE A 1438 1 15
HELIX 27 27 SER A 1468 THR A 1473 1 6
HELIX 28 28 ASN A 1561 GLY A 1565 5 5
HELIX 29 29 VAL A 1576 ALA A 1586 1 11
SHEET 1 AA 4 LEU A 69 VAL A 75 0
SHEET 2 AA 4 THR A 82 PHE A 87 -1 O THR A 82 N VAL A 75
SHEET 3 AA 4 GLU A 123 ARG A 127 -1 O LEU A 124 N LEU A 85
SHEET 4 AA 4 GLU A 116 LEU A 117 -1 O GLU A 116 N ARG A 125
SHEET 1 AB 4 GLY A 109 LYS A 110 0
SHEET 2 AB 4 ILE A 101 ASP A 105 -1 O ASP A 105 N GLY A 109
SHEET 3 AB 4 ASP A 134 ILE A 139 -1 O ILE A 136 N VAL A 104
SHEET 4 AB 4 TYR A 155 THR A 160 -1 O TYR A 155 N ILE A 139
SHEET 1 AC 4 GLU A 250 LEU A 254 0
SHEET 2 AC 4 LEU A 185 LEU A 190 -1 O LEU A 185 N LEU A 254
SHEET 3 AC 4 SER A 167 PHE A 170 -1 O SER A 167 N LEU A 190
SHEET 4 AC 4 ASP A 279 TYR A 280 1 O ASP A 279 N VAL A 168
SHEET 1 AD 5 SER A 175 PRO A 178 0
SHEET 2 AD 5 ALA A 284 LEU A 289 1 O LEU A 286 N SER A 175
SHEET 3 AD 5 GLY A 266 MET A 272 -1 O GLY A 266 N LEU A 289
SHEET 4 AD 5 ASN A 194 VAL A 202 -1 O ASN A 198 N VAL A 271
SHEET 5 AD 5 ALA A 232 ASP A 241 -1 O ASP A 233 N ARG A 201
SHEET 1 AE 4 HIS A 341 LEU A 344 0
SHEET 2 AE 4 ARG A 302 GLN A 308 -1 O LEU A 303 N LEU A 344
SHEET 3 AE 4 GLY A 293 TYR A 299 -1 O GLY A 293 N GLN A 308
SHEET 4 AE 4 ASP A 927 ASP A 930 -1 O ASP A 927 N ARG A 298
SHEET 1 AF 4 THR A 330 THR A 335 0
SHEET 2 AF 4 GLU A 320 LEU A 324 -1 O VAL A 321 N ALA A 334
SHEET 3 AF 4 LEU A 352 LYS A 357 -1 O LEU A 352 N LEU A 324
SHEET 4 AF 4 GLN A 360 ASP A 365 -1 O GLN A 360 N LYS A 357
SHEET 1 AG 3 GLN A 387 PHE A 391 0
SHEET 2 AG 3 THR A 402 ARG A 410 -1 O ASN A 406 N PHE A 391
SHEET 3 AG 3 TYR A 446 PRO A 451 -1 O TYR A 446 N GLY A 407
SHEET 1 AH 5 LEU A 396 TYR A 397 0
SHEET 2 AH 5 ASP A 476 VAL A 479 1 O HIS A 478 N TYR A 397
SHEET 3 AH 5 GLY A 459 ASN A 466 -1 N GLY A 459 O VAL A 479
SHEET 4 AH 5 ILE A 422 ILE A 427 -1 O LYS A 423 N ASN A 466
SHEET 5 AH 5 VAL A 433 SER A 439 -1 N LEU A 434 O VAL A 426
SHEET 1 AI 2 MET A 487 THR A 492 0
SHEET 2 AI 2 VAL A 504 TYR A 512 -1 O SER A 507 N THR A 492
SHEET 1 AJ 2 ALA A 516 PRO A 517 0
SHEET 2 AJ 2 VAL A 504 TYR A 512 1 N TYR A 512 O ALA A 516
SHEET 1 AK 2 ARG A 568 THR A 573 0
SHEET 2 AK 2 VAL A 504 TYR A 512 -1 O VAL A 504 N THR A 573
SHEET 1 AL 4 ARG A 554 THR A 562 0
SHEET 2 AL 4 THR A 522 PRO A 531 -1 O LEU A 523 N LEU A 561
SHEET 3 AL 4 LEU A 584 LEU A 593 -1 O GLN A 585 N ARG A 530
SHEET 4 AL 4 PRO A 599 ARG A 602 -1 O VAL A 600 N LEU A 592
SHEET 1 AM 4 ARG A 554 THR A 562 0
SHEET 2 AM 4 THR A 522 PRO A 531 -1 O LEU A 523 N LEU A 561
SHEET 3 AM 4 LEU A 584 LEU A 593 -1 O GLN A 585 N ARG A 530
SHEET 4 AM 4 ALA A 607 ILE A 608 -1 O ILE A 608 N LEU A 584
SHEET 1 AN 2 PRO A 599 ARG A 602 0
SHEET 2 AN 2 LEU A 584 LEU A 593 -1 O GLY A 590 N ARG A 602
SHEET 1 AO 4 GLU A 543 PHE A 544 0
SHEET 2 AO 4 GLY A 616 ARG A 618 -1 O ILE A 617 N GLU A 543
SHEET 3 AO 4 ASN A 645 VAL A 651 -1 O ASP A 649 N ARG A 618
SHEET 4 AO 4 GLY A 710 PRO A 715 -1 O GLY A 710 N ILE A 650
SHEET 1 AP 4 GLN A 687 LEU A 702 0
SHEET 2 AP 4 LEU A 665 ASN A 679 -1 N LEU A 665 O LEU A 702
SHEET 3 AP 4 ALA A 720 LYS A 726 -1 O ALA A 720 N GLU A 672
SHEET 4 AP 4 VAL A 732 TRP A 738 -1 O SER A 733 N VAL A 725
SHEET 1 AQ 2 THR A 772 LYS A 774 0
SHEET 2 AQ 2 THR A 811 PRO A 813 -1 O ILE A 812 N ILE A 773
SHEET 1 AR 3 LYS A 784 GLU A 790 0
SHEET 2 AR 3 TYR A 824 VAL A 830 -1 O TYR A 824 N GLU A 790
SHEET 3 AR 3 ARG A 843 HIS A 849 -1 O ALA A 844 N VAL A 829
SHEET 1 AS 5 LYS A 868 MET A 869 0
SHEET 2 AS 5 PHE A1008 VAL A1017 1 O ILE A1016 N MET A 869
SHEET 3 AS 5 GLY A 994 TRP A1003 -1 O GLY A 994 N VAL A1017
SHEET 4 AS 5 ASN A 893 ASP A 900 -1 O ASN A 893 N TRP A1003
SHEET 5 AS 5 VAL A 969 GLN A 971 -1 O GLN A 970 N ALA A 898
SHEET 1 AT 5 LYS A 868 MET A 869 0
SHEET 2 AT 5 PHE A1008 VAL A1017 1 O ILE A1016 N MET A 869
SHEET 3 AT 5 GLY A 994 TRP A1003 -1 O GLY A 994 N VAL A1017
SHEET 4 AT 5 ASN A 893 ASP A 900 -1 O ASN A 893 N TRP A1003
SHEET 5 AT 5 VAL A 975 THR A 976 -1 O VAL A 975 N VAL A 894
SHEET 1 AU 2 VAL A 969 GLN A 971 0
SHEET 2 AU 2 ASN A 893 ASP A 900 -1 O ALA A 898 N GLN A 970
SHEET 1 AV 2 PRO A 874 LYS A 880 0
SHEET 2 AV 2 GLU A 982 PRO A 988 -1 O GLY A 983 N ILE A 879
SHEET 1 AW 4 ILE A1022 ASN A1026 0
SHEET 2 AW 4 THR A1036 THR A1044 -1 O THR A1040 N ASN A1026
SHEET 3 AW 4 ARG A1080 ALA A1089 -1 O THR A1081 N ILE A1043
SHEET 4 AW 4 LEU A1063 LEU A1065 -1 O GLU A1064 N ARG A1088
SHEET 1 AX 4 PHE A1030 MET A1031 0
SHEET 2 AX 4 LYS A1117 VAL A1123 1 O GLY A1122 N MET A1031
SHEET 3 AX 4 GLY A1094 ALA A1100 -1 O GLY A1094 N VAL A1123
SHEET 4 AX 4 THR A1058 GLY A1061 -1 O THR A1058 N GLN A1099
SHEET 1 AY 3 ALA A1072 LEU A1075 0
SHEET 2 AY 3 GLN A1051 VAL A1055 -1 O GLN A1051 N LEU A1075
SHEET 3 AY 3 ILE A1102 SER A1103 -1 O SER A1103 N ASN A1054
SHEET 1 AZ 4 GLN A1130 LEU A1138 0
SHEET 2 AZ 4 LEU A1484 GLY A1492 -1 O LEU A1484 N LEU A1138
SHEET 3 AZ 4 GLU A1160 SER A1166 -1 O GLU A1160 N SER A1491
SHEET 4 AZ 4 GLN A1462 ASN A1467 -1 O GLN A1462 N LEU A1165
SHEET 1 A0 4 THR A1143 ALA A1145 0
SHEET 2 A0 4 GLN A1475 SER A1477 -1 O VAL A1476 N TRP A1144
SHEET 3 A0 4 TRP A1445 THR A1449 -1 O GLN A1448 N SER A1477
SHEET 4 A0 4 LEU A1456 GLY A1458 -1 O LEU A1456 N ALA A1447
SHEET 1 A1 6 ALA A1501 ASN A1503 0
SHEET 2 A1 6 ARG A1640 THR A1642 -1 O ARG A1640 N ASN A1503
SHEET 3 A1 6 MET A1630 SER A1633 -1 O VAL A1631 N ALA A1641
SHEET 4 A1 6 VAL A1542 LEU A1550 -1 O LEU A1546 N GLU A1632
SHEET 5 A1 6 ARG A1597 VAL A1604 -1 O PHE A1598 N ASP A1549
SHEET 6 A1 6 ILE A1588 PHE A1593 -1 N LYS A1589 O ALA A1601
SHEET 1 A2 4 LEU A1505 LEU A1512 0
SHEET 2 A2 4 LEU A1529 ALA A1538 -1 O LEU A1531 N LEU A1512
SHEET 3 A2 4 VAL A1610 ALA A1618 -1 O VAL A1610 N VAL A1536
SHEET 4 A2 4 LEU A1555 LEU A1557 -1 O GLU A1556 N ARG A1617
SHEET 1 A3 3 LEU A1524 ARG A1525 0
SHEET 2 A3 3 LEU A1648 ARG A1652 1 O ILE A1650 N LEU A1524
SHEET 3 A3 3 GLY A1622 GLN A1625 -1 O GLY A1622 N VAL A1651
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
(ATOM LINES ARE NOT SHOWN.)
END
