| content |
HEADER VIRAL PROTEIN/HYDROLASE 20-MAY-25 9V2P
TITLE COMPLEX STRUCTURE OF GX2012 SPIKE RBD BOUND TO HUMAN DPP4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SPIKE GLYCOPROTEIN;
COMPND 8 CHAIN: G;
COMPND 9 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP4, ADCP2, CD26;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: BTTP-BETACOV/GX2012;
SOURCE 10 ORGANISM_TAXID: 1503304;
SOURCE 11 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS GX2012 RBD, HUMAN DPP4, VIRAL PROTEIN, HYDROLASE, VIRAL
KEYWDS 2 PROTEIN/HYDROLASE, VIRAL PROTEIN-HYDROLASE COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR X.WANG,Z.LIN
REVDAT 1 24-DEC-25 9V2P 0
JRNL AUTH X.WANG,Z.LIN
JRNL TITL COMPLEX STRUCTURE OF GX2012 SPIKE RBD BOUND TO HUMAN DPP4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, COOT
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) : 2.400
REMARK 3 NUMBER OF PARTICLES : 447216
REMARK 3 CTF CORRECTION METHOD : NONE
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 9V2P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 23-MAY-25.
REMARK 100 THE DEPOSITION ID IS D_1300059646.
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 : COMPLEX STRUCTURE OF GX2012
REMARK 245 SPIKE RBD BOUND TO HUMAN DPP4
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : TFS KRIOS
REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00
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) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, C, D, E, F, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O
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 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 O VAL B 639 OG SER B 642 2.11
REMARK 500 O GLY B 580 OG SER B 583 2.17
REMARK 500 O GLU A 244 OH TYR B 661 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS B 339 CA - CB - SG ANGL. DEV. = 8.1 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 GLU A 73 -130.37 63.62
REMARK 500 SER A 93 166.85 179.21
REMARK 500 GLU A 97 -59.27 -120.35
REMARK 500 PHE A 98 111.24 66.12
REMARK 500 LYS A 139 -71.79 -116.35
REMARK 500 ARG A 140 -27.39 -149.08
REMARK 500 PRO A 149 160.20 -45.58
REMARK 500 ASN A 150 51.10 -91.09
REMARK 500 ASN A 151 21.67 174.66
REMARK 500 HIS A 162 43.41 -140.11
REMARK 500 ASP A 200 -168.50 -79.23
REMARK 500 VAL A 207 -64.26 -97.76
REMARK 500 SER A 242 -155.15 60.30
REMARK 500 ALA A 306 -91.40 -87.28
REMARK 500 GLN A 320 81.92 -49.21
REMARK 500 LYS A 423 12.16 59.05
REMARK 500 SER A 437 -70.17 -70.13
REMARK 500 ASN A 450 78.85 -159.29
REMARK 500 GLU A 464 -1.41 68.88
REMARK 500 ASN A 520 -129.52 62.96
REMARK 500 ALA A 548 16.70 47.85
REMARK 500 SER A 630 -115.45 62.90
REMARK 500 ASP A 678 -69.31 -95.80
REMARK 500 ASN A 679 18.37 -145.97
REMARK 500 SER A 686 45.52 -87.88
REMARK 500 ASN A 710 -61.76 -92.88
REMARK 500 MET A 733 119.90 -161.37
REMARK 500 HIS B 66 12.93 -142.37
REMARK 500 GLU B 73 -72.03 53.68
REMARK 500 PHE B 98 62.00 27.78
REMARK 500 TRP B 124 -169.02 -109.16
REMARK 500 LYS B 139 -70.36 -120.54
REMARK 500 ARG B 140 -17.88 -148.87
REMARK 500 GLU B 146 90.53 52.22
REMARK 500 ASN B 151 50.23 -109.53
REMARK 500 ASP B 192 -2.42 66.76
REMARK 500 ASP B 200 -169.70 -78.49
REMARK 500 VAL B 207 -61.26 -97.71
REMARK 500 SER B 242 -158.72 61.71
REMARK 500 ALA B 306 68.12 -101.56
REMARK 500 THR B 307 168.82 82.54
REMARK 500 GLU B 309 -32.98 78.85
REMARK 500 GLN B 320 35.11 -80.43
REMARK 500 ASN B 450 72.36 -159.82
REMARK 500 GLU B 464 -2.75 66.71
REMARK 500 ASN B 520 -130.25 62.89
REMARK 500 TYR B 547 -53.14 -122.08
REMARK 500 CYS B 551 -15.43 69.22
REMARK 500 TYR B 585 69.50 -100.39
REMARK 500 SER B 630 -114.85 63.82
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-64736 RELATED DB: EMDB
REMARK 900 COMPLEX STRUCTURE OF GX2012 SPIKE RBD BOUND TO HUMAN DPP4
DBREF 9V2P A 40 766 UNP P27487 DPP4_HUMAN 40 766
DBREF 9V2P B 40 766 UNP P27487 DPP4_HUMAN 40 766
DBREF1 9V2P G 386 594 UNP A0A0U1WJZ6_BCHK4
DBREF2 9V2P G A0A0U1WJZ6 386 594
SEQRES 1 A 727 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 2 A 727 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 3 A 727 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 4 A 727 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 5 A 727 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 6 A 727 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 7 A 727 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 A 727 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 A 727 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 10 A 727 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 11 A 727 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 12 A 727 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 13 A 727 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 14 A 727 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 A 727 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 16 A 727 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 A 727 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 18 A 727 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 19 A 727 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 20 A 727 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 21 A 727 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 22 A 727 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 A 727 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 24 A 727 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 25 A 727 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 26 A 727 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 27 A 727 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 28 A 727 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 29 A 727 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 30 A 727 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 31 A 727 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 32 A 727 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 33 A 727 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 34 A 727 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 35 A 727 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 36 A 727 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 37 A 727 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 38 A 727 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 39 A 727 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 40 A 727 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 41 A 727 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 42 A 727 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 43 A 727 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 44 A 727 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 45 A 727 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 46 A 727 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 47 A 727 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 48 A 727 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 49 A 727 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 50 A 727 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 51 A 727 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 52 A 727 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 53 A 727 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 54 A 727 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 55 A 727 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 56 A 727 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 B 727 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 2 B 727 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 3 B 727 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 4 B 727 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 5 B 727 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 6 B 727 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 7 B 727 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 B 727 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 B 727 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 10 B 727 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 11 B 727 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 12 B 727 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 13 B 727 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 14 B 727 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 B 727 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 16 B 727 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 B 727 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 18 B 727 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 19 B 727 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 20 B 727 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 21 B 727 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 22 B 727 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 B 727 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 24 B 727 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 25 B 727 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 26 B 727 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 27 B 727 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 28 B 727 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 29 B 727 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 30 B 727 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 31 B 727 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 32 B 727 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 33 B 727 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 34 B 727 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 35 B 727 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 36 B 727 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 37 B 727 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 38 B 727 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 39 B 727 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 40 B 727 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 41 B 727 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 42 B 727 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 43 B 727 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 44 B 727 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 45 B 727 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 46 B 727 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 47 B 727 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 48 B 727 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 49 B 727 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 50 B 727 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 51 B 727 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 52 B 727 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 53 B 727 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 54 B 727 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 55 B 727 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 56 B 727 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 1 G 209 THR GLU CYS ASP PHE SER PRO MET PHE LYS GLY VAL ALA
SEQRES 2 G 209 PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE SER ASN
SEQRES 3 G 209 CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE ALA
SEQRES 4 G 209 VAL ASP GLU PHE SER CYS ASN GLY ILE SER PRO ASP ALA
SEQRES 5 G 209 ILE ALA ARG GLY CYS TYR SER THR LEU THR VAL ASP TYR
SEQRES 6 G 209 PHE ALA TYR PRO LEU SER MET LYS SER TYR ILE ARG PRO
SEQRES 7 G 209 GLY SER ALA GLY ASN ILE PRO LEU TYR ASN TYR LYS GLN
SEQRES 8 G 209 SER PHE ALA HIS PRO THR CYS ARG VAL LEU ALA SER VAL
SEQRES 9 G 209 PRO PRO ASN VAL THR ILE THR LYS PRO GLU ALA TYR GLY
SEQRES 10 G 209 TYR ILE SER LYS CYS SER ARG LEU THR GLY ASP TYR GLN
SEQRES 11 G 209 HIS ILE GLU THR PRO LEU TYR ILE ASN PRO GLY GLU TYR
SEQRES 12 G 209 SER ILE CYS ARG ASP PHE ALA PRO LEU GLY PHE SER GLU
SEQRES 13 G 209 ASP GLY GLN VAL PHE LYS ARG THR LEU THR GLN PHE GLU
SEQRES 14 G 209 GLY GLY GLY LEU LEU ILE GLY VAL GLY THR ARG VAL PRO
SEQRES 15 G 209 MET THR ALA ASN LEU GLU MET GLY PHE VAL ILE SER VAL
SEQRES 16 G 209 GLN TYR GLY ALA GLY THR ASP SER VAL CYS PRO MET LEU
SEQRES 17 G 209 ASP
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET NAG K 1 14
HET NAG K 2 14
HET NAG L 1 14
HET NAG L 2 14
HET NAG M 1 14
HET NAG M 2 14
HET NAG N 1 14
HET NAG N 2 14
HET NAG O 1 14
HET NAG O 2 14
HET BMA O 3 11
HET NAG A 801 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 4 NAG 25(C8 H15 N O6)
FORMUL 15 BMA C6 H12 O6
HELIX 1 AA1 THR A 44 ASN A 51 1 8
HELIX 2 AA2 SER A 93 GLU A 97 5 5
HELIX 3 AA3 ASP A 200 GLU A 206 1 7
HELIX 4 AA4 ASP A 274 LEU A 276 5 3
HELIX 5 AA5 LEU A 340 GLN A 344 5 5
HELIX 6 AA6 GLU A 421 MET A 425 5 5
HELIX 7 AA7 LYS A 463 ALA A 465 5 3
HELIX 8 AA8 ASN A 497 GLN A 505 1 9
HELIX 9 AA9 ASN A 562 GLU A 571 1 10
HELIX 10 AB1 ILE A 590 ASN A 595 5 6
HELIX 11 AB2 THR A 600 LYS A 615 1 16
HELIX 12 AB3 SER A 630 GLY A 641 1 12
HELIX 13 AB4 ARG A 658 TYR A 662 5 5
HELIX 14 AB5 ASP A 663 GLY A 672 1 10
HELIX 15 AB6 ASN A 679 SER A 686 1 8
HELIX 16 AB7 VAL A 688 VAL A 698 5 11
HELIX 17 AB8 HIS A 712 VAL A 726 1 15
HELIX 18 AB9 SER A 744 SER A 764 1 21
HELIX 19 AC1 THR B 44 LYS B 50 1 7
HELIX 20 AC2 SER B 93 GLU B 97 5 5
HELIX 21 AC3 ASP B 200 VAL B 207 1 8
HELIX 22 AC4 ASP B 274 LEU B 276 5 3
HELIX 23 AC5 LEU B 340 GLN B 344 5 5
HELIX 24 AC6 GLU B 421 MET B 425 5 5
HELIX 25 AC7 LYS B 463 ALA B 465 5 3
HELIX 26 AC8 ASN B 497 GLN B 505 1 9
HELIX 27 AC9 ASN B 562 ASN B 572 1 11
HELIX 28 AD1 GLY B 587 HIS B 592 1 6
HELIX 29 AD2 THR B 600 LYS B 615 1 16
HELIX 30 AD3 SER B 630 GLY B 641 1 12
HELIX 31 AD4 ARG B 658 TYR B 662 5 5
HELIX 32 AD5 ASP B 663 GLY B 672 1 10
HELIX 33 AD6 ASN B 679 ASN B 685 1 7
HELIX 34 AD7 SER B 686 THR B 687 5 2
HELIX 35 AD8 VAL B 688 VAL B 698 5 11
HELIX 36 AD9 HIS B 712 VAL B 726 1 15
HELIX 37 AE1 SER B 744 SER B 764 1 21
HELIX 38 AE2 PHE G 390 LYS G 395 5 6
HELIX 39 AE3 ASN G 415 PHE G 423 1 9
HELIX 40 AE4 SER G 434 ALA G 439 1 6
HELIX 41 AE5 GLY G 467 ASN G 473 1 7
SHEET 1 AA1 2 LYS A 41 THR A 42 0
SHEET 2 AA1 2 VAL A 507 GLN A 508 1 O GLN A 508 N LYS A 41
SHEET 1 AA2 4 ARG A 61 TRP A 62 0
SHEET 2 AA2 4 GLU A 67 TYR A 70 -1 O LEU A 69 N ARG A 61
SHEET 3 AA2 4 ILE A 76 ASN A 80 -1 O PHE A 79 N TYR A 68
SHEET 4 AA2 4 SER A 86 LEU A 90 -1 O SER A 87 N VAL A 78
SHEET 1 AA3 4 ASP A 104 ILE A 107 0
SHEET 2 AA3 4 PHE A 113 LYS A 122 -1 O LEU A 115 N SER A 106
SHEET 3 AA3 4 TYR A 128 ASP A 136 -1 O ASP A 133 N LEU A 116
SHEET 4 AA3 4 LEU A 142 ILE A 143 -1 O ILE A 143 N ILE A 134
SHEET 1 AA4 4 TRP A 154 TRP A 157 0
SHEET 2 AA4 4 LEU A 164 TRP A 168 -1 O ALA A 165 N THR A 156
SHEET 3 AA4 4 ASP A 171 LYS A 175 -1 O TYR A 173 N TYR A 166
SHEET 4 AA4 4 TYR A 183 ARG A 184 -1 O TYR A 183 N VAL A 174
SHEET 1 AA5 3 ILE A 194 ASN A 196 0
SHEET 2 AA5 3 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA5 3 LEU A 214 TRP A 216 -1 N TRP A 215 O ALA A 224
SHEET 1 AA6 4 ILE A 194 ASN A 196 0
SHEET 2 AA6 4 PHE A 222 ASN A 229 -1 O PHE A 228 N TYR A 195
SHEET 3 AA6 4 THR A 265 ASN A 272 -1 O THR A 265 N ASN A 229
SHEET 4 AA6 4 SER A 284 GLN A 286 -1 O ILE A 285 N VAL A 270
SHEET 1 AA7 2 LEU A 235 PHE A 240 0
SHEET 2 AA7 2 LYS A 250 PRO A 255 -1 O LYS A 250 N PHE A 240
SHEET 1 AA8 4 HIS A 298 TRP A 305 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O GLN A 314 N CYS A 301
SHEET 3 AA8 4 SER A 323 TYR A 330 -1 O VAL A 324 N TRP A 315
SHEET 4 AA8 4 TRP A 337 ASN A 338 -1 O ASN A 338 N ASP A 329
SHEET 1 AA9 4 HIS A 298 TRP A 305 0
SHEET 2 AA9 4 ARG A 310 ARG A 317 -1 O GLN A 314 N CYS A 301
SHEET 3 AA9 4 SER A 323 TYR A 330 -1 O VAL A 324 N TRP A 315
SHEET 4 AA9 4 HIS A 345 GLU A 347 -1 O HIS A 345 N MET A 325
SHEET 1 AB1 4 HIS A 363 PHE A 364 0
SHEET 2 AB1 4 SER A 370 SER A 376 -1 O TYR A 372 N HIS A 363
SHEET 3 AB1 4 ARG A 382 GLN A 388 -1 O CYS A 385 N LYS A 373
SHEET 4 AB1 4 THR A 395 PHE A 396 -1 O THR A 395 N TYR A 386
SHEET 1 AB2 4 VAL A 404 LEU A 410 0
SHEET 2 AB2 4 TYR A 414 SER A 419 -1 O ILE A 418 N GLY A 406
SHEET 3 AB2 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB2 4 VAL A 442 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 AB3 4 TYR A 457 PHE A 461 0
SHEET 2 AB3 4 TYR A 467 CYS A 472 -1 O ARG A 471 N SER A 458
SHEET 3 AB3 4 LEU A 479 SER A 484 -1 O LEU A 479 N CYS A 472
SHEET 4 AB3 4 LYS A 489 GLU A 495 -1 O GLU A 495 N TYR A 480
SHEET 1 AB4 8 SER A 511 LEU A 519 0
SHEET 2 AB4 8 THR A 522 LEU A 530 -1 O THR A 522 N LEU A 519
SHEET 3 AB4 8 ILE A 574 PHE A 578 -1 O VAL A 575 N ILE A 529
SHEET 4 AB4 8 TYR A 540 VAL A 546 1 N LEU A 543 O ILE A 574
SHEET 5 AB4 8 VAL A 619 TRP A 629 1 O ALA A 625 N LEU A 544
SHEET 6 AB4 8 CYS A 649 VAL A 653 1 O ILE A 651 N GLY A 628
SHEET 7 AB4 8 GLU A 699 GLY A 705 1 O LEU A 701 N ALA A 652
SHEET 8 AB4 8 GLN A 731 TYR A 735 1 O GLN A 731 N TYR A 700
SHEET 1 AB5 2 LYS B 41 THR B 42 0
SHEET 2 AB5 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 AB6 4 LEU B 60 TRP B 62 0
SHEET 2 AB6 4 GLU B 67 GLN B 72 -1 O LEU B 69 N ARG B 61
SHEET 3 AB6 4 ASN B 75 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 4 AB6 4 SER B 86 LEU B 90 -1 O SER B 87 N VAL B 78
SHEET 1 AB7 3 ASP B 104 ILE B 107 0
SHEET 2 AB7 3 PHE B 113 LYS B 122 -1 O GLU B 117 N ASP B 104
SHEET 3 AB7 3 TYR B 128 ASP B 136 -1 O TYR B 135 N ILE B 114
SHEET 1 AB8 4 THR B 152 TRP B 157 0
SHEET 2 AB8 4 LEU B 164 TRP B 168 -1 O VAL B 167 N GLN B 153
SHEET 3 AB8 4 ASP B 171 LYS B 175 -1 O TYR B 173 N TYR B 166
SHEET 4 AB8 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 AB9 3 ILE B 194 ASN B 196 0
SHEET 2 AB9 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB9 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 AC1 4 ILE B 194 ASN B 196 0
SHEET 2 AC1 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AC1 4 THR B 265 ASN B 272 -1 O THR B 265 N ASN B 229
SHEET 4 AC1 4 ILE B 285 GLN B 286 -1 O ILE B 285 N VAL B 270
SHEET 1 AC2 2 LEU B 235 PHE B 240 0
SHEET 2 AC2 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 AC3 4 HIS B 298 TRP B 305 0
SHEET 2 AC3 4 ARG B 310 ARG B 317 -1 O LEU B 316 N TYR B 299
SHEET 3 AC3 4 TYR B 322 ASP B 329 -1 O VAL B 324 N TRP B 315
SHEET 4 AC3 4 HIS B 345 MET B 348 -1 O GLU B 347 N SER B 323
SHEET 1 AC4 4 HIS B 363 PHE B 364 0
SHEET 2 AC4 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AC4 4 ARG B 382 GLN B 388 -1 O PHE B 387 N PHE B 371
SHEET 4 AC4 4 THR B 395 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 AC5 4 VAL B 404 LEU B 410 0
SHEET 2 AC5 4 TYR B 414 SER B 419 -1 O ILE B 418 N GLY B 406
SHEET 3 AC5 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AC5 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 AC6 4 CYS B 454 PHE B 461 0
SHEET 2 AC6 4 TYR B 467 PRO B 475 -1 O ARG B 471 N SER B 458
SHEET 3 AC6 4 LEU B 479 SER B 484 -1 O LEU B 479 N CYS B 472
SHEET 4 AC6 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 AC7 8 SER B 511 LEU B 519 0
SHEET 2 AC7 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
SHEET 3 AC7 8 ILE B 574 ASP B 579 -1 O VAL B 575 N ILE B 529
SHEET 4 AC7 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 AC7 8 VAL B 619 TRP B 629 1 O TRP B 627 N LEU B 544
SHEET 6 AC7 8 CYS B 649 VAL B 653 1 O ILE B 651 N ILE B 626
SHEET 7 AC7 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 AC7 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 AC8 5 LYS G 405 PHE G 409 0
SHEET 2 AC8 5 THR G 445 ALA G 452 -1 O VAL G 448 N LEU G 407
SHEET 3 AC8 5 GLU G 573 GLN G 581 -1 O GLY G 575 N PHE G 451
SHEET 4 AC8 5 THR G 482 SER G 488 -1 N ALA G 487 O MET G 574
SHEET 5 AC8 5 ALA G 424 ASN G 431 -1 N ASN G 431 O THR G 482
SHEET 1 AC9 2 CYS G 412 TYR G 414 0
SHEET 2 AC9 2 VAL G 589 PRO G 591 1 O CYS G 590 N CYS G 412
SHEET 1 AD1 3 TYR G 501 ARG G 509 0
SHEET 2 AD1 3 LEU G 558 VAL G 566 -1 O THR G 564 N TYR G 503
SHEET 3 AD1 3 GLN G 544 THR G 549 -1 N GLN G 544 O GLY G 563
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.03
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.04
SSBOND 3 CYS A 444 CYS A 447 1555 1555 2.03
SSBOND 4 CYS A 454 CYS A 472 1555 1555 2.01
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.02
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.04
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.03
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.03
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.04
SSBOND 11 CYS G 388 CYS G 412 1555 1555 2.03
SSBOND 12 CYS G 430 CYS G 483 1555 1555 2.04
SSBOND 13 CYS G 442 CYS G 590 1555 1555 2.03
SSBOND 14 CYS G 507 CYS G 531 1555 1555 2.02
LINK ND2 ASN A 85 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 92 C1 NAG A 801 1555 1555 1.47
LINK ND2 ASN A 150 C1 NAG D 1 1555 1555 1.43
LINK ND2 ASN A 219 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN A 229 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN A 281 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN A 321 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN B 85 C1 NAG J 1 1555 1555 1.43
LINK ND2 ASN B 92 C1 NAG K 1 1555 1555 1.43
LINK ND2 ASN B 150 C1 NAG N 1 1555 1555 1.44
LINK ND2 ASN B 229 C1 NAG L 1 1555 1555 1.44
LINK ND2 ASN B 281 C1 NAG O 1 1555 1555 1.44
LINK ND2 ASN B 321 C1 NAG M 1 1555 1555 1.43
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44
LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44
LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.44
CISPEP 1 GLY B 474 PRO B 475 0 0.47
CISPEP 2 ARG B 581 GLY B 582 0 -10.76
CISPEP 3 GLY B 584 TYR B 585 0 -8.19
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
TER 5958 PRO A 766
TER 11916 PRO B 766
TER 13533 ASP G 594
MASTER 200 0 26 41 107 0 0 613891 3 402 129
END |