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HEADER HYDROLASE 01-NOV-18 6I2T
TITLE CRYOEM RECONSTRUCTION OF FULL-LENGTH, FULLY-GLYCOSYLATED HUMAN
TITLE 2 BUTYRYLCHOLINESTERASE TETRAMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: B, A, C, D;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE
COMPND 5 ESTERASE II,PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LAMELLIPODIN-DERIVED POLYPROLINE PEPTIDE;
COMPND 9 CHAIN: J
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_TAXID: 9606
KEYWDS CHOLINESTERASE, TETRAMER, HYDROLASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR M.R.LEUNG,L.S.VAN BEZOUWEN,L.M.SCHOPFER,J.L.SUSSMAN,I.SILMAN,
AUTHOR 2 O.LOCKRIDGE,T.ZEEV-BEN-MORDEHAI
REVDAT 1 19-DEC-18 6I2T 0
JRNL AUTH M.R.LEUNG,L.S.VAN BEZOUWEN,L.M.SCHOPFER,J.L.SUSSMAN,
JRNL AUTH 2 I.SILMAN,O.LOCKRIDGE,T.ZEEV-BEN-MORDEHAI
JRNL TITL CRYO-EM STRUCTURE OF THE NATIVE BUTYRYLCHOLINESTERASE
JRNL TITL 2 TETRAMER REVEALS A DIMER OF DIMERS STABILIZED BY A
JRNL TITL 3 SUPERHELICAL ASSEMBLY
JRNL REF PROC.NATL.ACAD.SCI.USA 2018
JRNL REFN ESSN 1091-6490
JRNL DOI 10.1073/PNAS.1817009115
REMARK 2
REMARK 2 RESOLUTION. 5.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION, EPU, GCTF, UCSF CHIMERA,
REMARK 3 RELION, RELION, RELION, PHENIX
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 4AQD
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
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) : 5.700
REMARK 3 NUMBER OF PARTICLES : 111986
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 6I2T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200012712.
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 : HETEROPENTAMERIC COMPLEX
REMARK 245 CONSISTING OF FOUR COPIES OF
REMARK 245 BUTYRYLCHOLINESTERASE AND ONE
REMARK 245 COPY OF A LAMELLIPODIN-DERIVED
REMARK 245 POLYPROLINE PEPTIDE
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 3.30
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOT FOR EITHER 2S OR 3S AT
REMARK 245 BLOT FORCE -2 OR 0, RESPECTIVELY
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 : 4518
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TALOS ARCTICA
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00
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) : 49.50
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 130000
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 94730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, C, D, J
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 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 465 SER B 566
REMARK 465 LYS B 567
REMARK 465 LYS B 568
REMARK 465 GLU B 569
REMARK 465 SER B 570
REMARK 465 CYS B 571
REMARK 465 VAL B 572
REMARK 465 GLY B 573
REMARK 465 LEU B 574
REMARK 465 GLU A 1
REMARK 465 ASP A 2
REMARK 465 ASP A 3
REMARK 465 ASN A 562
REMARK 465 ASP A 563
REMARK 465 TYR A 564
REMARK 465 THR A 565
REMARK 465 SER A 566
REMARK 465 LYS A 567
REMARK 465 LYS A 568
REMARK 465 GLU A 569
REMARK 465 SER A 570
REMARK 465 CYS A 571
REMARK 465 VAL A 572
REMARK 465 GLY A 573
REMARK 465 LEU A 574
REMARK 465 GLU C 1
REMARK 465 ASP C 2
REMARK 465 ASP C 3
REMARK 465 ASN C 562
REMARK 465 ASP C 563
REMARK 465 TYR C 564
REMARK 465 THR C 565
REMARK 465 SER C 566
REMARK 465 LYS C 567
REMARK 465 LYS C 568
REMARK 465 GLU C 569
REMARK 465 SER C 570
REMARK 465 CYS C 571
REMARK 465 VAL C 572
REMARK 465 GLY C 573
REMARK 465 LEU C 574
REMARK 465 GLU D 1
REMARK 465 ASP D 2
REMARK 465 ASP D 3
REMARK 465 SER D 566
REMARK 465 LYS D 567
REMARK 465 LYS D 568
REMARK 465 GLU D 569
REMARK 465 SER D 570
REMARK 465 CYS D 571
REMARK 465 VAL D 572
REMARK 465 GLY D 573
REMARK 465 LEU D 574
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 CYS B 263 CA - CB - SG ANGL. DEV. = 13.2 DEGREES
REMARK 500 PHE B 298 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 LEU B 428 CB - CG - CD2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 LEU A 318 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 LEU A 330 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 LEU C 318 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 LEU C 330 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 CYS D 263 CA - CB - SG ANGL. DEV. = 13.2 DEGREES
REMARK 500 PHE D 298 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 LEU D 428 CB - CG - CD2 ANGL. DEV. = -10.7 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 PHE B 43 -12.07 75.83
REMARK 500 THR B 50 -82.54 -74.99
REMARK 500 ASP B 54 -150.09 12.05
REMARK 500 ASN B 106 52.97 -158.25
REMARK 500 ALA B 162 68.08 -160.55
REMARK 500 SER B 198 -31.03 60.55
REMARK 500 ALA B 199 -26.00 -140.77
REMARK 500 SER B 215 16.89 -142.05
REMARK 500 GLU B 255 -73.99 -47.48
REMARK 500 ASP B 297 -71.67 -105.55
REMARK 500 ARG B 381 90.29 25.84
REMARK 500 PHE B 398 -60.83 -126.14
REMARK 500 GLU B 482 -72.43 -109.92
REMARK 500 ASN B 485 128.55 79.31
REMARK 500 THR B 533 13.25 49.18
REMARK 500 GLU B 538 -6.65 72.90
REMARK 500 PHE A 43 -11.71 76.71
REMARK 500 THR A 50 -81.80 -75.52
REMARK 500 ASP A 54 -150.48 13.30
REMARK 500 ASN A 106 54.05 -158.05
REMARK 500 ALA A 162 68.96 -160.09
REMARK 500 SER A 198 -29.72 61.09
REMARK 500 ALA A 199 -25.75 -144.21
REMARK 500 GLU A 255 -73.91 -46.83
REMARK 500 ASP A 297 -71.41 -105.27
REMARK 500 ARG A 381 89.93 24.98
REMARK 500 PHE A 398 -61.30 -126.12
REMARK 500 GLU A 482 -72.08 -109.36
REMARK 500 ASN A 485 128.82 80.01
REMARK 500 ASP A 537 2.18 -64.39
REMARK 500 LYS A 558 40.99 -98.28
REMARK 500 PHE C 43 -11.77 76.71
REMARK 500 THR C 50 -81.88 -75.52
REMARK 500 ASP C 54 -150.54 13.26
REMARK 500 ASN C 106 54.14 -158.09
REMARK 500 ALA C 162 69.07 -159.94
REMARK 500 SER C 198 -29.63 61.09
REMARK 500 ALA C 199 -25.73 -144.31
REMARK 500 GLU C 255 -73.95 -46.77
REMARK 500 ASP C 297 -71.39 -105.41
REMARK 500 ARG C 381 89.95 24.92
REMARK 500 PHE C 398 -61.32 -126.02
REMARK 500 GLU C 482 -72.05 -109.45
REMARK 500 ASN C 485 128.87 80.00
REMARK 500 ASP C 537 2.31 -64.39
REMARK 500 LYS C 558 41.11 -98.32
REMARK 500 PHE D 43 -12.02 75.81
REMARK 500 THR D 50 -82.40 -75.11
REMARK 500 ASP D 54 -150.08 11.82
REMARK 500 ASN D 106 52.93 -158.19
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound
REMARK 800 to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound
REMARK 800 to ASN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 601 bound
REMARK 800 to ASN C 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 602 bound
REMARK 800 to ASN C 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 603 bound
REMARK 800 to ASN C 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 601 bound
REMARK 800 to ASN D 341
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-4400 RELATED DB: EMDB
REMARK 900 MODEL OF FULL-LENGTH, FULLY-GLYCOSYLATED HUMAN
REMARK 900 BUTYRYLCHOLINESTERASE TETRAMER
DBREF 6I2T B 1 574 UNP P06276 CHLE_HUMAN 29 602
DBREF 6I2T A 1 574 UNP P06276 CHLE_HUMAN 29 602
DBREF 6I2T C 1 574 UNP P06276 CHLE_HUMAN 29 602
DBREF 6I2T D 1 574 UNP P06276 CHLE_HUMAN 29 602
DBREF 6I2T J 4 15 PDB 6I2T 6I2T 4 15
SEQRES 1 B 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 B 574 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 B 574 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 B 574 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 B 574 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 B 574 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 B 574 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 B 574 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 B 574 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 B 574 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 B 574 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 B 574 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 B 574 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 B 574 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 B 574 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 B 574 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 B 574 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 B 574 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 B 574 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 B 574 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 B 574 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 B 574 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 B 574 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 B 574 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 B 574 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 B 574 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 B 574 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 B 574 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 B 574 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 B 574 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 B 574 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 B 574 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 B 574 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 B 574 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 B 574 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 B 574 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 B 574 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 B 574 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 B 574 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 B 574 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 B 574 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 B 574 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY
SEQRES 43 B 574 PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN
SEQRES 44 B 574 GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL
SEQRES 45 B 574 GLY LEU
SEQRES 1 A 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 574 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 574 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 574 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 574 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 574 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 574 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 574 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 574 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 574 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 574 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 574 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 574 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 574 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 574 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 574 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 574 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 574 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 574 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 574 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 574 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 574 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 574 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 574 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 574 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 574 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 574 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 574 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 574 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 574 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 574 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 574 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 574 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 574 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 574 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 A 574 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 574 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 A 574 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 574 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 574 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 574 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 A 574 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY
SEQRES 43 A 574 PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN
SEQRES 44 A 574 GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL
SEQRES 45 A 574 GLY LEU
SEQRES 1 C 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 C 574 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 C 574 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 C 574 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 C 574 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 C 574 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 C 574 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 C 574 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 C 574 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 C 574 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 C 574 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 C 574 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 C 574 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 C 574 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 C 574 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 C 574 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 C 574 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 C 574 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 C 574 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 C 574 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 C 574 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 C 574 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 C 574 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 C 574 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 C 574 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 C 574 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 C 574 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 C 574 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 C 574 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 C 574 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 C 574 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 C 574 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 C 574 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 C 574 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 C 574 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 C 574 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 C 574 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 C 574 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 C 574 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 C 574 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 C 574 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 C 574 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY
SEQRES 43 C 574 PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN
SEQRES 44 C 574 GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL
SEQRES 45 C 574 GLY LEU
SEQRES 1 D 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 D 574 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 D 574 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 D 574 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 D 574 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 D 574 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 D 574 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 D 574 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 D 574 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 D 574 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 D 574 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 D 574 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 D 574 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 D 574 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 D 574 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 D 574 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 D 574 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 D 574 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 D 574 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 D 574 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 D 574 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 D 574 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 D 574 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 D 574 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 D 574 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 D 574 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 D 574 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 D 574 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 D 574 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 D 574 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 D 574 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 D 574 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 D 574 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 D 574 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 D 574 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 D 574 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 D 574 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 D 574 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 D 574 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 D 574 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 D 574 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 D 574 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY
SEQRES 43 D 574 PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN
SEQRES 44 D 574 GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL
SEQRES 45 D 574 GLY LEU
SEQRES 1 J 12 PRO PRO PRO PRO PRO PRO PRO PRO PRO PRO PRO PRO
HET NAG B 601 14
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG C 601 14
HET NAG C 602 14
HET NAG C 603 14
HET NAG D 601 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 6 NAG 8(C8 H15 N O6)
HELIX 1 AA1 LEU B 38 ARG B 42 5 5
HELIX 2 AA2 PHE B 76 MET B 81 1 6
HELIX 3 AA3 LEU B 125 ASP B 129 5 5
HELIX 4 AA4 GLY B 130 ARG B 138 1 9
HELIX 5 AA5 VAL B 148 LEU B 154 1 7
HELIX 6 AA6 ASN B 165 ILE B 182 1 18
HELIX 7 AA7 ALA B 183 PHE B 185 5 3
HELIX 8 AA8 ALA B 199 SER B 210 1 12
HELIX 9 AA9 PRO B 211 HIS B 214 5 4
HELIX 10 AB1 SER B 235 THR B 250 1 16
HELIX 11 AB2 ASN B 256 ARG B 265 1 10
HELIX 12 AB3 ASP B 268 GLU B 276 1 9
HELIX 13 AB4 ALA B 277 VAL B 279 5 3
HELIX 14 AB5 MET B 302 LEU B 309 1 8
HELIX 15 AB6 GLY B 326 GLY B 333 5 8
HELIX 16 AB7 THR B 346 PHE B 358 1 13
HELIX 17 AB8 SER B 362 TYR B 373 1 12
HELIX 18 AB9 GLU B 383 PHE B 398 1 16
HELIX 19 AC1 PHE B 398 GLU B 411 1 14
HELIX 20 AC2 PRO B 431 GLY B 435 5 5
HELIX 21 AC3 GLU B 441 PHE B 446 1 6
HELIX 22 AC4 GLY B 447 ASN B 455 5 9
HELIX 23 AC5 THR B 457 GLY B 478 1 22
HELIX 24 AC6 ARG B 515 PHE B 525 1 11
HELIX 25 AC7 PHE B 526 LEU B 530 5 5
HELIX 26 AC8 GLU B 538 ASP B 556 1 19
HELIX 27 AC9 TRP B 557 ASN B 562 1 6
HELIX 28 AD1 LEU A 38 ARG A 42 5 5
HELIX 29 AD2 PHE A 76 MET A 81 1 6
HELIX 30 AD3 LEU A 125 ASP A 129 5 5
HELIX 31 AD4 GLY A 130 ARG A 138 1 9
HELIX 32 AD5 GLY A 149 LEU A 154 1 6
HELIX 33 AD6 ASN A 165 ILE A 182 1 18
HELIX 34 AD7 ALA A 183 PHE A 185 5 3
HELIX 35 AD8 ALA A 199 SER A 210 1 12
HELIX 36 AD9 PRO A 211 HIS A 214 5 4
HELIX 37 AE1 SER A 235 THR A 250 1 16
HELIX 38 AE2 ASN A 256 ARG A 265 1 10
HELIX 39 AE3 ASP A 268 GLU A 276 1 9
HELIX 40 AE4 ALA A 277 VAL A 279 5 3
HELIX 41 AE5 MET A 302 LEU A 309 1 8
HELIX 42 AE6 GLY A 326 GLY A 333 5 8
HELIX 43 AE7 THR A 346 PHE A 358 1 13
HELIX 44 AE8 SER A 362 THR A 374 1 13
HELIX 45 AE9 GLU A 383 PHE A 398 1 16
HELIX 46 AF1 PHE A 398 GLU A 411 1 14
HELIX 47 AF2 PRO A 431 GLY A 435 5 5
HELIX 48 AF3 GLU A 441 PHE A 446 1 6
HELIX 49 AF4 GLY A 447 ASN A 455 5 9
HELIX 50 AF5 THR A 457 GLY A 478 1 22
HELIX 51 AF6 ARG A 515 PHE A 525 1 11
HELIX 52 AF7 PHE A 526 GLU A 531 1 6
HELIX 53 AF8 ASP A 537 ASN A 551 1 15
HELIX 54 AF9 ASN A 552 LYS A 558 1 7
HELIX 55 AG1 LEU C 38 ARG C 42 5 5
HELIX 56 AG2 PHE C 76 MET C 81 1 6
HELIX 57 AG3 LEU C 125 ASP C 129 5 5
HELIX 58 AG4 GLY C 130 ARG C 138 1 9
HELIX 59 AG5 GLY C 149 LEU C 154 1 6
HELIX 60 AG6 ASN C 165 ILE C 182 1 18
HELIX 61 AG7 ALA C 183 PHE C 185 5 3
HELIX 62 AG8 ALA C 199 SER C 210 1 12
HELIX 63 AG9 PRO C 211 HIS C 214 5 4
HELIX 64 AH1 SER C 235 THR C 250 1 16
HELIX 65 AH2 ASN C 256 ARG C 265 1 10
HELIX 66 AH3 ASP C 268 GLU C 276 1 9
HELIX 67 AH4 ALA C 277 VAL C 279 5 3
HELIX 68 AH5 MET C 302 LEU C 309 1 8
HELIX 69 AH6 GLY C 326 GLY C 333 5 8
HELIX 70 AH7 THR C 346 PHE C 358 1 13
HELIX 71 AH8 SER C 362 THR C 374 1 13
HELIX 72 AH9 GLU C 383 PHE C 398 1 16
HELIX 73 AI1 PHE C 398 GLU C 411 1 14
HELIX 74 AI2 PRO C 431 GLY C 435 5 5
HELIX 75 AI3 GLU C 441 PHE C 446 1 6
HELIX 76 AI4 GLY C 447 ASN C 455 5 9
HELIX 77 AI5 THR C 457 GLY C 478 1 22
HELIX 78 AI6 ARG C 515 PHE C 525 1 11
HELIX 79 AI7 PHE C 526 GLU C 531 1 6
HELIX 80 AI8 ASP C 537 ASN C 551 1 15
HELIX 81 AI9 ASN C 552 LYS C 558 1 7
HELIX 82 AJ1 LEU D 38 ARG D 42 5 5
HELIX 83 AJ2 PHE D 76 MET D 81 1 6
HELIX 84 AJ3 LEU D 125 ASP D 129 5 5
HELIX 85 AJ4 GLY D 130 ARG D 138 1 9
HELIX 86 AJ5 VAL D 148 LEU D 154 1 7
HELIX 87 AJ6 ASN D 165 ILE D 182 1 18
HELIX 88 AJ7 ALA D 183 PHE D 185 5 3
HELIX 89 AJ8 ALA D 199 SER D 210 1 12
HELIX 90 AJ9 PRO D 211 HIS D 214 5 4
HELIX 91 AK1 SER D 235 THR D 250 1 16
HELIX 92 AK2 ASN D 256 ARG D 265 1 10
HELIX 93 AK3 ASP D 268 GLU D 276 1 9
HELIX 94 AK4 ALA D 277 VAL D 279 5 3
HELIX 95 AK5 MET D 302 LEU D 309 1 8
HELIX 96 AK6 GLY D 326 GLY D 333 5 8
HELIX 97 AK7 THR D 346 PHE D 358 1 13
HELIX 98 AK8 SER D 362 TYR D 373 1 12
HELIX 99 AK9 GLU D 383 PHE D 398 1 16
HELIX 100 AL1 PHE D 398 GLU D 411 1 14
HELIX 101 AL2 PRO D 431 GLY D 435 5 5
HELIX 102 AL3 GLU D 441 PHE D 446 1 6
HELIX 103 AL4 GLY D 447 ASN D 455 5 9
HELIX 104 AL5 THR D 457 GLY D 478 1 22
HELIX 105 AL6 ARG D 515 PHE D 525 1 11
HELIX 106 AL7 PHE D 526 LEU D 530 5 5
HELIX 107 AL8 GLU D 538 ASP D 556 1 19
HELIX 108 AL9 TRP D 557 ASN D 562 1 6
SHEET 1 AA1 3 ILE B 5 THR B 8 0
SHEET 2 AA1 3 GLY B 11 ARG B 14 -1 O VAL B 13 N ILE B 6
SHEET 3 AA1 3 TRP B 56 ASN B 57 1 O TRP B 56 N ARG B 14
SHEET 1 AA211 MET B 16 VAL B 20 0
SHEET 2 AA211 GLY B 23 PRO B 32 -1 O ALA B 27 N MET B 16
SHEET 3 AA211 TYR B 94 ALA B 101 -1 O LEU B 95 N ILE B 31
SHEET 4 AA211 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 5 AA211 ALA B 107 ILE B 113 1 N LEU B 110 O ILE B 140
SHEET 6 AA211 GLY B 187 GLU B 197 1 O PHE B 195 N ILE B 111
SHEET 7 AA211 ARG B 219 GLN B 223 1 O ILE B 221 N LEU B 194
SHEET 8 AA211 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 AA211 ALA B 416 PHE B 421 1 O PHE B 417 N VAL B 319
SHEET 10 AA211 LYS B 499 LEU B 503 1 O LEU B 503 N TYR B 420
SHEET 11 AA211 ILE B 510 THR B 512 -1 O MET B 511 N TYR B 500
SHEET 1 AA3 2 SER B 64 CYS B 65 0
SHEET 2 AA3 2 LEU B 88 SER B 89 1 O SER B 89 N SER B 64
SHEET 1 AA4 3 ILE A 5 THR A 8 0
SHEET 2 AA4 3 GLY A 11 ARG A 14 -1 O GLY A 11 N THR A 8
SHEET 3 AA4 3 TRP A 56 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AA511 MET A 16 VAL A 20 0
SHEET 2 AA511 GLY A 23 PRO A 32 -1 O ALA A 27 N MET A 16
SHEET 3 AA511 TYR A 94 PRO A 100 -1 O LEU A 95 N ILE A 31
SHEET 4 AA511 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 AA511 ALA A 107 ILE A 113 1 N LEU A 110 O ILE A 140
SHEET 6 AA511 GLY A 187 GLU A 197 1 O THR A 193 N ILE A 111
SHEET 7 AA511 ARG A 219 GLN A 223 1 O ILE A 221 N LEU A 194
SHEET 8 AA511 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AA511 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AA511 LYS A 499 LEU A 503 1 O LEU A 501 N TYR A 420
SHEET 11 AA511 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AA6 2 SER A 64 CYS A 65 0
SHEET 2 AA6 2 LEU A 88 SER A 89 1 O SER A 89 N SER A 64
SHEET 1 AA7 3 ILE C 5 THR C 8 0
SHEET 2 AA7 3 GLY C 11 ARG C 14 -1 O GLY C 11 N THR C 8
SHEET 3 AA7 3 TRP C 56 ASN C 57 1 O TRP C 56 N ARG C 14
SHEET 1 AA811 MET C 16 VAL C 20 0
SHEET 2 AA811 GLY C 23 PRO C 32 -1 O ALA C 27 N MET C 16
SHEET 3 AA811 TYR C 94 PRO C 100 -1 O LEU C 95 N ILE C 31
SHEET 4 AA811 ILE C 140 MET C 144 -1 O SER C 143 N ASN C 96
SHEET 5 AA811 ALA C 107 ILE C 113 1 N LEU C 110 O ILE C 140
SHEET 6 AA811 GLY C 187 GLU C 197 1 O THR C 193 N ILE C 111
SHEET 7 AA811 ARG C 219 GLN C 223 1 O ILE C 221 N LEU C 194
SHEET 8 AA811 ILE C 317 ASN C 322 1 O LEU C 318 N LEU C 222
SHEET 9 AA811 ALA C 416 PHE C 421 1 O PHE C 417 N VAL C 319
SHEET 10 AA811 LYS C 499 LEU C 503 1 O LEU C 501 N TYR C 420
SHEET 11 AA811 ILE C 510 THR C 512 -1 O MET C 511 N TYR C 500
SHEET 1 AA9 2 SER C 64 CYS C 65 0
SHEET 2 AA9 2 LEU C 88 SER C 89 1 O SER C 89 N SER C 64
SHEET 1 AB1 3 ILE D 5 THR D 8 0
SHEET 2 AB1 3 GLY D 11 ARG D 14 -1 O VAL D 13 N ILE D 6
SHEET 3 AB1 3 TRP D 56 ASN D 57 1 O TRP D 56 N ARG D 14
SHEET 1 AB211 MET D 16 VAL D 20 0
SHEET 2 AB211 GLY D 23 PRO D 32 -1 O ALA D 27 N MET D 16
SHEET 3 AB211 TYR D 94 ALA D 101 -1 O LEU D 95 N ILE D 31
SHEET 4 AB211 ILE D 140 MET D 144 -1 O SER D 143 N ASN D 96
SHEET 5 AB211 ALA D 107 ILE D 113 1 N LEU D 110 O ILE D 140
SHEET 6 AB211 GLY D 187 GLU D 197 1 O PHE D 195 N ILE D 111
SHEET 7 AB211 ARG D 219 GLN D 223 1 O ILE D 221 N LEU D 194
SHEET 8 AB211 ILE D 317 ASN D 322 1 O LEU D 318 N LEU D 222
SHEET 9 AB211 ALA D 416 PHE D 421 1 O PHE D 417 N VAL D 319
SHEET 10 AB211 LYS D 499 LEU D 503 1 O LEU D 503 N TYR D 420
SHEET 11 AB211 ILE D 510 THR D 512 -1 O MET D 511 N TYR D 500
SHEET 1 AB3 2 SER D 64 CYS D 65 0
SHEET 2 AB3 2 LEU D 88 SER D 89 1 O SER D 89 N SER D 64
SSBOND 1 CYS B 65 CYS B 92 1555 1555 2.05
SSBOND 2 CYS B 252 CYS B 263 1555 1555 2.03
SSBOND 3 CYS B 400 CYS B 519 1555 1555 2.04
SSBOND 4 CYS A 65 CYS A 92 1555 1555 2.04
SSBOND 5 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 6 CYS A 400 CYS A 519 1555 1555 2.04
SSBOND 7 CYS C 65 CYS C 92 1555 1555 2.04
SSBOND 8 CYS C 252 CYS C 263 1555 1555 2.04
SSBOND 9 CYS C 400 CYS C 519 1555 1555 2.03
SSBOND 10 CYS D 65 CYS D 92 1555 1555 2.05
SSBOND 11 CYS D 252 CYS D 263 1555 1555 2.03
SSBOND 12 CYS D 400 CYS D 519 1555 1555 2.04
LINK ND2 ASN B 341 C1 NAG B 601 1555 1555 1.43
LINK ND2 ASN A 17 C1 NAG A 601 1555 1555 1.43
LINK ND2 ASN A 341 C1 NAG A 602 1555 1555 1.44
LINK ND2 ASN A 481 C1 NAG A 603 1555 1555 1.44
LINK ND2 ASN C 17 C1 NAG C 601 1555 1555 1.43
LINK ND2 ASN C 341 C1 NAG C 602 1555 1555 1.44
LINK ND2 ASN C 481 C1 NAG C 603 1555 1555 1.44
LINK ND2 ASN D 341 C1 NAG D 601 1555 1555 1.43
CISPEP 1 ALA B 101 PRO B 102 0 0.13
CISPEP 2 ASP B 379 GLN B 380 0 -4.63
CISPEP 3 ALA A 101 PRO A 102 0 -0.20
CISPEP 4 ASP A 379 GLN A 380 0 -3.57
CISPEP 5 ALA C 101 PRO C 102 0 -0.22
CISPEP 6 ASP C 379 GLN C 380 0 -3.48
CISPEP 7 ALA D 101 PRO D 102 0 0.11
CISPEP 8 ASP D 379 GLN D 380 0 -4.69
SITE 1 AC1 2 ILE A 4 ASN A 17
SITE 1 AC2 3 GLY A 336 ASN A 341 ASN A 342
SITE 1 AC3 5 TYR A 477 ASN A 479 ASN A 481 THR A 483
SITE 2 AC3 5 GLN A 484
SITE 1 AC4 2 ASN B 341 ASN B 342
SITE 1 AC5 2 ILE C 4 ASN C 17
SITE 1 AC6 3 GLY C 336 ASN C 341 ASN C 342
SITE 1 AC7 5 TYR C 477 ASN C 479 ASN C 481 THR C 483
SITE 2 AC7 5 GLN C 484
SITE 1 AC8 2 ASN D 341 ASN D 342
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 0.003241 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003241 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003241 0.00000
TER 4513 THR B 565
TER 8991 PHE A 561
TER 13469 PHE C 561
TER 17982 THR D 565
TER 18067 PRO J 15
MASTER 310 0 8 108 64 0 10 618174 5 144 181
END |