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HEADER VIRAL PROTEIN/HYDROLASE 28-SEP-23 8WKU
TITLE COMPLEX STRUCTURE OF MJHKU4R-COV-1 SPIKE RBD BOUND TO HUMAN CD26
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MJHKU4R-COV-1 SPIKE RBD;
COMPND 8 CHAIN: B;
COMPND 9 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_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MANIS JAVANICA;
SOURCE 11 ORGANISM_TAXID: 9974;
SOURCE 12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS MJHKU4R-COV-1, SPIKE RBD, HUMAN CD26, VIRAL PROTEIN/HYDROLASE, VIRAL
KEYWDS 2 PROTEIN-HYDROLASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.N.ZHAO,Y.CHAI,F.GAO
REVDAT 3 16-OCT-24 8WKU 1 REMARK
REVDAT 2 24-JUL-24 8WKU 1 JRNL
REVDAT 1 26-JUN-24 8WKU 0
JRNL AUTH Z.ZHAO,X.LI,Y.CHAI,Z.LIU,Q.WANG,G.F.GAO
JRNL TITL MOLECULAR BASIS FOR RECEPTOR RECOGNITION AND BROAD HOST
JRNL TITL 2 TROPISM FOR MERBECOVIRUS MJHKU4R-COV-1.
JRNL REF EMBO REP. V. 25 3116 2024
JRNL REFN ESSN 1469-3178
JRNL PMID 38877169
JRNL DOI 10.1038/S44319-024-00169-8
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 268.92
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 28683
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1435
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.7800 - 7.5300 0.95 3004 159 0.2144 0.2206
REMARK 3 2 7.5300 - 5.9800 0.95 2889 152 0.2129 0.2172
REMARK 3 3 5.9800 - 5.2300 0.95 2849 150 0.2152 0.2794
REMARK 3 4 5.2300 - 4.7500 0.95 2827 148 0.2034 0.2472
REMARK 3 5 4.7500 - 4.4100 0.95 2797 148 0.2035 0.2254
REMARK 3 6 4.4100 - 4.1500 0.95 2834 149 0.2226 0.2693
REMARK 3 7 4.1500 - 3.9400 0.95 2803 147 0.2524 0.2453
REMARK 3 8 3.9400 - 3.7700 0.95 2795 147 0.2818 0.2862
REMARK 3 9 3.7700 - 3.6200 0.57 1663 88 0.3027 0.3392
REMARK 3 10 3.6200 - 3.5000 0.95 2787 147 0.3279 0.3699
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 107.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 8258
REMARK 3 ANGLE : 0.679 11229
REMARK 3 CHIRALITY : 0.047 1317
REMARK 3 PLANARITY : 0.005 1370
REMARK 3 DIHEDRAL : 15.331 3118
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8WKU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 03-OCT-23.
REMARK 100 THE DEPOSITION ID IS D_1300041475.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAY-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL02U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54034
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.3100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.71
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4QZV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMINO ACIDS, 0.1 M BUFFER SYSTEM
REMARK 280 3 (TRIS BASE; BICINE) AND 30% V/V EDO_P8K, PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 163.75533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 81.87767
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 81.87767
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 163.75533
REMARK 290
REMARK 290 REMARK: NULL
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 82980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 235.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 81.87767
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 SER A 39
REMARK 465 HIS A 767
REMARK 465 HIS A 768
REMARK 465 HIS A 769
REMARK 465 HIS A 770
REMARK 465 HIS A 771
REMARK 465 HIS A 772
REMARK 465 GLU B 375
REMARK 465 ALA B 376
REMARK 465 ALA B 377
REMARK 465 ALA B 378
REMARK 465 THR B 379
REMARK 465 GLY B 380
REMARK 465 THR B 381
REMARK 465 PHE B 382
REMARK 465 ILE B 383
REMARK 465 GLU B 384
REMARK 465 GLN B 385
REMARK 465 PRO B 386
REMARK 465 LYS B 387
REMARK 465 LEU B 596
REMARK 465 ASP B 597
REMARK 465 LEU B 598
REMARK 465 GLY B 599
REMARK 465 ASN B 600
REMARK 465 SER B 601
REMARK 465 SER B 602
REMARK 465 THR B 603
REMARK 465 ILE B 604
REMARK 465 THR B 605
REMARK 465 HIS B 606
REMARK 465 TYR B 607
REMARK 465 LEU B 608
REMARK 465 GLY B 609
REMARK 465 LYS B 610
REMARK 465 CYS B 611
REMARK 465 VAL B 612
REMARK 465 ASP B 613
REMARK 465 TYR B 614
REMARK 465 HIS B 615
REMARK 465 HIS B 616
REMARK 465 HIS B 617
REMARK 465 HIS B 618
REMARK 465 HIS B 619
REMARK 465 HIS B 620
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 HIS A 66 26.50 -142.39
REMARK 500 ASN A 74 -6.06 75.10
REMARK 500 GLN A 123 -66.23 -97.67
REMARK 500 HIS A 162 21.31 -141.50
REMARK 500 ILE A 193 -58.47 -125.80
REMARK 500 VAL A 207 -63.13 -107.71
REMARK 500 SER A 242 -108.79 48.29
REMARK 500 THR A 401 58.84 -91.95
REMARK 500 ASN A 450 71.55 -157.43
REMARK 500 ARG A 596 13.58 58.63
REMARK 500 ALA A 654 54.39 31.60
REMARK 500 ASP A 678 -72.20 -96.96
REMARK 500 ASN A 679 13.50 -148.49
REMARK 500 ASN B 414 65.22 60.80
REMARK 500 ASN B 476 -56.68 -120.01
REMARK 500 SER B 538 81.62 -154.95
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8WKU A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 8WKU B 375 620 PDB 8WKU 8WKU 375 620
SEQADV 8WKU HIS A 767 UNP P27487 EXPRESSION TAG
SEQADV 8WKU HIS A 768 UNP P27487 EXPRESSION TAG
SEQADV 8WKU HIS A 769 UNP P27487 EXPRESSION TAG
SEQADV 8WKU HIS A 770 UNP P27487 EXPRESSION TAG
SEQADV 8WKU HIS A 771 UNP P27487 EXPRESSION TAG
SEQADV 8WKU HIS A 772 UNP P27487 EXPRESSION TAG
SEQRES 1 A 734 SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN
SEQRES 2 A 734 THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER
SEQRES 3 A 734 ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU
SEQRES 4 A 734 VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU
SEQRES 5 A 734 GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN
SEQRES 6 A 734 ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU
SEQRES 7 A 734 GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR
SEQRES 8 A 734 ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU
SEQRES 9 A 734 ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL
SEQRES 10 A 734 THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP
SEQRES 11 A 734 ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO
SEQRES 12 A 734 SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE
SEQRES 13 A 734 TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL
SEQRES 14 A 734 PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY
SEQRES 15 A 734 THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL
SEQRES 16 A 734 PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU
SEQRES 17 A 734 GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA
SEQRES 18 A 734 GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN
SEQRES 19 A 734 THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE
SEQRES 20 A 734 GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS
SEQRES 21 A 734 TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE
SEQRES 22 A 734 SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL
SEQRES 23 A 734 MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP
SEQRES 24 A 734 ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR
SEQRES 25 A 734 THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS
SEQRES 26 A 734 PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER
SEQRES 27 A 734 ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE
SEQRES 28 A 734 ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP
SEQRES 29 A 734 GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU
SEQRES 30 A 734 TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY
SEQRES 31 A 734 ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS
SEQRES 32 A 734 VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS
SEQRES 33 A 734 GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR
SEQRES 34 A 734 TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR
SEQRES 35 A 734 THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL
SEQRES 36 A 734 LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN
SEQRES 37 A 734 VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU
SEQRES 38 A 734 ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO
SEQRES 39 A 734 HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP
SEQRES 40 A 734 VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL
SEQRES 41 A 734 PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU
SEQRES 42 A 734 ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY
SEQRES 43 A 734 TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG
SEQRES 44 A 734 LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA
SEQRES 45 A 734 ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG
SEQRES 46 A 734 ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR
SEQRES 47 A 734 SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS
SEQRES 48 A 734 GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR
SEQRES 49 A 734 ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR
SEQRES 50 A 734 PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL
SEQRES 51 A 734 MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU
SEQRES 52 A 734 LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN
SEQRES 53 A 734 GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY
SEQRES 54 A 734 VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS
SEQRES 55 A 734 GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR
SEQRES 56 A 734 HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
SEQRES 57 A 734 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 246 GLU ALA ALA ALA THR GLY THR PHE ILE GLU GLN PRO LYS
SEQRES 2 B 246 SER LYS GLU CYS ASP PHE THR PRO MET LEU VAL GLY VAL
SEQRES 3 B 246 PRO PRO GLN VAL TYR ASN PHE LYS ARG LEU VAL PHE THR
SEQRES 4 B 246 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE
SEQRES 5 B 246 MET VAL ASN GLU PHE SER CYS ASN GLY ILE SER PRO ASP
SEQRES 6 B 246 ALA ILE ALA ARG GLY CYS TYR SER SER LEU THR VAL ASP
SEQRES 7 B 246 TYR PHE ALA TYR PRO LEU SER MET ARG SER TYR ILE GLN
SEQRES 8 B 246 PRO GLY SER ALA GLY ASP ILE SER LEU TYR ASN TYR LYS
SEQRES 9 B 246 GLN SER PHE ALA ASN PRO THR CYS ARG VAL LEU ALA THR
SEQRES 10 B 246 ALA PRO ALA ASN LEU THR LEU THR LYS PRO SER ALA TYR
SEQRES 11 B 246 GLY TYR PHE GLN LYS CYS SER ARG VAL SER GLY GLU HIS
SEQRES 12 B 246 ASN SER VAL GLU THR PRO LEU TYR ILE ASN PRO GLY GLU
SEQRES 13 B 246 TYR SER ILE CYS ARG SER PHE SER PRO TYR GLY PHE SER
SEQRES 14 B 246 GLU ASP GLY GLU VAL PHE ARG ARG GLN LEU THR GLN TYR
SEQRES 15 B 246 GLU GLY GLY GLY ILE LEU VAL GLY VAL GLY ALA LYS LEU
SEQRES 16 B 246 ALA MET THR ASP LYS LEU GLU MET GLY PHE ILE ILE SER
SEQRES 17 B 246 VAL GLN TYR GLY THR ASP THR ASN SER VAL CYS PRO MET
SEQRES 18 B 246 LEU ASP LEU GLY ASN SER SER THR ILE THR HIS TYR LEU
SEQRES 19 B 246 GLY LYS CYS VAL ASP TYR HIS HIS HIS HIS HIS HIS
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET FUC C 4 10
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET MAN D 5 11
HET FUC D 6 10
HET NAG E 1 14
HET NAG E 2 14
HET BMA E 3 11
HET MAN E 4 11
HET MAN E 5 11
HET NAG F 1 14
HET NAG F 2 14
HET BMA F 3 11
HET MAN F 4 11
HET MAN F 5 11
HET MAN F 6 11
HET MAN F 7 11
HET MAN F 8 11
HET NAG G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET MAN G 4 11
HET FUC G 5 10
HET NAG H 1 14
HET NAG H 2 14
HET BMA H 3 11
HET MAN H 4 11
HET MAN H 5 11
HET NAG I 1 14
HET NAG I 2 14
HET BMA I 3 11
HET NAG A 801 14
HET NAG A 802 14
HET NAG B 701 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM MAN ALPHA-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
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 3 NAG 17(C8 H15 N O6)
FORMUL 3 BMA 7(C6 H12 O6)
FORMUL 3 FUC 3(C6 H12 O5)
FORMUL 4 MAN 12(C6 H12 O6)
HELIX 1 AA1 THR A 44 LYS A 50 1 7
HELIX 2 AA2 GLU A 91 PHE A 98 5 8
HELIX 3 AA3 ASP A 200 VAL A 207 1 8
HELIX 4 AA4 PRO A 290 ILE A 295 1 6
HELIX 5 AA5 VAL A 341 GLN A 344 5 4
HELIX 6 AA6 GLU A 421 MET A 425 5 5
HELIX 7 AA7 ASN A 497 ASN A 506 1 10
HELIX 8 AA8 ASN A 562 THR A 570 1 9
HELIX 9 AA9 GLY A 587 HIS A 592 1 6
HELIX 10 AB1 ALA A 593 ASN A 595 5 3
HELIX 11 AB2 THR A 600 GLY A 617 1 18
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 ASN A 685 1 7
HELIX 16 AB7 SER A 686 THR A 687 5 2
HELIX 17 AB8 VAL A 688 VAL A 698 5 11
HELIX 18 AB9 HIS A 712 VAL A 726 1 15
HELIX 19 AC1 SER A 744 PHE A 763 1 20
HELIX 20 AC2 PHE B 393 VAL B 398 5 6
HELIX 21 AC3 GLN B 403 PHE B 407 5 5
HELIX 22 AC4 ASN B 418 PHE B 426 1 9
HELIX 23 AC5 SER B 437 ALA B 442 1 6
HELIX 24 AC6 PRO B 457 GLN B 465 5 9
HELIX 25 AC7 GLY B 470 ASN B 476 1 7
HELIX 26 AC8 SER B 532 PHE B 537 5 6
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 GLN A 72 -1 O LEU A 69 N ARG A 61
SHEET 3 AA2 4 ASN A 75 ASN A 80 -1 O LEU A 77 N TYR A 70
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 GLU A 117 N ASP A 104
SHEET 3 AA3 4 TYR A 128 ASP A 136 -1 O ASP A 133 N LEU A 116
SHEET 4 AA3 4 GLN A 141 LEU A 142 -1 O GLN A 141 N ASP A 136
SHEET 1 AA4 4 TRP A 154 TRP A 157 0
SHEET 2 AA4 4 LEU A 164 TRP A 168 -1 O VAL A 167 N TRP A 154
SHEET 3 AA4 4 ASP A 171 LYS A 175 -1 O LYS A 175 N LEU A 164
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 PHE A 269 N TYR A 225
SHEET 4 AA6 4 SER A 284 ILE A 287 -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 SER A 312 N THR A 304
SHEET 3 AA8 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 AA8 4 TRP A 337 CYS A 339 -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 SER A 312 N THR A 304
SHEET 3 AA9 4 TYR A 322 TYR A 330 -1 O ASP A 326 N LEU A 313
SHEET 4 AA9 4 HIS A 345 MET A 348 -1 O GLU A 347 N SER A 323
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 HIS A 383 N ILE A 375
SHEET 4 AB1 4 LYS A 391 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 TYR A 416 N ALA A 409
SHEET 3 AB2 4 ASN A 430 GLN A 435 -1 O TYR A 432 N TYR A 417
SHEET 4 AB2 4 ASP A 438 CYS A 444 -1 O THR A 443 N LYS A 433
SHEET 1 AB3 4 CYS A 454 PHE A 461 0
SHEET 2 AB3 4 TYR A 467 PRO A 475 -1 O GLY A 474 N GLN A 455
SHEET 3 AB3 4 LEU A 479 SER A 484 -1 O THR A 481 N LEU A 470
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 ILE A 518 0
SHEET 2 AB4 8 LYS A 523 LEU A 530 -1 O PHE A 524 N ILE A 517
SHEET 3 AB4 8 ILE A 574 ASP A 579 -1 O VAL A 575 N ILE A 529
SHEET 4 AB4 8 TYR A 540 ASP A 545 1 N LEU A 543 O ILE A 574
SHEET 5 AB4 8 VAL A 619 GLY A 628 1 O ASP A 620 N TYR A 540
SHEET 6 AB4 8 CYS A 649 VAL A 653 1 O ILE A 651 N ILE A 626
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 LEU A 702
SHEET 1 AB5 5 LYS B 408 PHE B 412 0
SHEET 2 AB5 5 LEU B 449 ALA B 455 -1 O LEU B 449 N PHE B 412
SHEET 3 AB5 5 GLU B 576 SER B 582 -1 O SER B 582 N THR B 450
SHEET 4 AB5 5 THR B 485 THR B 491 -1 N ALA B 490 O MET B 577
SHEET 5 AB5 5 MET B 427 ASN B 434 -1 N SER B 432 O ARG B 487
SHEET 1 AB6 2 CYS B 415 TYR B 417 0
SHEET 2 AB6 2 VAL B 592 PRO B 594 1 O CYS B 593 N TYR B 417
SHEET 1 AB7 4 VAL B 520 PRO B 523 0
SHEET 2 AB7 4 TYR B 504 SER B 514 -1 N SER B 514 O VAL B 520
SHEET 3 AB7 4 ILE B 561 LEU B 569 -1 O ILE B 561 N VAL B 513
SHEET 4 AB7 4 GLU B 547 GLN B 552 -1 N PHE B 549 O GLY B 564
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 2.03
SSBOND 5 CYS A 649 CYS A 762 1555 1555 2.03
SSBOND 6 CYS B 391 CYS B 415 1555 1555 2.03
SSBOND 7 CYS B 433 CYS B 486 1555 1555 2.03
SSBOND 8 CYS B 445 CYS B 593 1555 1555 2.03
SSBOND 9 CYS B 510 CYS B 534 1555 1555 2.03
LINK ND2 ASN A 85 C1 NAG C 1 1555 1555 1.45
LINK ND2 ASN A 150 C1 NAG D 1 1555 1555 1.43
LINK ND2 ASN A 219 C1 NAG E 1 1555 1555 1.45
LINK ND2 ASN A 229 C1 NAG F 1 1555 1555 1.44
LINK ND2 ASN A 281 C1 NAG G 1 1555 1555 1.44
LINK ND2 ASN A 321 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN A 520 C1 NAG A 801 1555 1555 1.44
LINK ND2 ASN A 685 C1 NAG A 802 1555 1555 1.46
LINK ND2 ASN B 418 C1 NAG I 1 1555 1555 1.45
LINK ND2 ASN B 495 C1 NAG B 701 1555 1555 1.51
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
LINK O6 NAG C 1 C1 FUC C 4 1555 1555 1.45
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O6 NAG D 1 C1 FUC D 6 1555 1555 1.44
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44
LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.44
LINK O6 BMA D 3 C1 MAN D 5 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.45
LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44
LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.44
LINK O6 BMA E 3 C1 MAN E 5 1555 1555 1.45
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O4 NAG F 2 C1 BMA F 3 1555 1555 1.44
LINK O3 BMA F 3 C1 MAN F 4 1555 1555 1.44
LINK O6 BMA F 3 C1 MAN F 7 1555 1555 1.44
LINK O2 MAN F 4 C1 MAN F 5 1555 1555 1.45
LINK O2 MAN F 5 C1 MAN F 6 1555 1555 1.45
LINK O6 MAN F 7 C1 MAN F 8 1555 1555 1.45
LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.43
LINK O6 NAG G 1 C1 FUC G 5 1555 1555 1.44
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45
LINK O6 BMA G 3 C1 MAN G 4 1555 1555 1.45
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG H 2 C1 BMA H 3 1555 1555 1.45
LINK O3 BMA H 3 C1 MAN H 4 1555 1555 1.44
LINK O6 BMA H 3 C1 MAN H 5 1555 1555 1.45
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45
CISPEP 1 GLY A 474 PRO A 475 0 -0.71
CRYST1 127.501 127.501 245.633 90.00 90.00 120.00 P 32 2 1 6
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 0.007843 0.004528 0.000000 0.00000
SCALE2 0.000000 0.009056 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004071 0.00000
TER 5958 PRO A 766
TER 7570 MET B 595
MASTER 298 0 39 26 62 0 0 6 8045 2 505 76
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