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HEADER VIRAL PROTEIN/HYDROLASE 20-MAY-25 9V2L
TITLE COMPLEX STRUCTURE OF 2014-422 SPIKE RBD BOUND TO HUMAN DPP4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;
COMPND 8 CHAIN: B, C;
COMPND 9 SYNONYM: DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MIDDLE EAST RESPIRATORY SYNDROME-RELATED
SOURCE 3 CORONAVIRUS;
SOURCE 4 ORGANISM_TAXID: 1335626;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: DPP4, ADCP2, CD26;
SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS 2014-422 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 9V2L 0
JRNL AUTH X.WANG,Z.LIN
JRNL TITL COMPLEX STRUCTURE OF 2014-422 SPIKE RBD BOUND TO HUMAN DPP4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : PHENIX
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.000
REMARK 3 NUMBER OF PARTICLES : 591107
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 9V2L 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_1300059647.
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 2014-422
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, C, D, E, F
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 A 371
REMARK 465 VAL A 372
REMARK 465 HIS A 373
REMARK 465 SER A 374
REMARK 465 ARG A 375
REMARK 465 GLY A 376
REMARK 465 GLN A 377
REMARK 465 PHE A 378
REMARK 465 ILE A 379
REMARK 465 GLU A 380
REMARK 465 GLN A 381
REMARK 465 PRO A 382
REMARK 465 ASN A 383
REMARK 465 SER A 384
REMARK 465 MET A 592
REMARK 465 ASP A 593
REMARK 465 LEU B 765
REMARK 465 PRO B 766
REMARK 465 LEU C 765
REMARK 465 PRO C 766
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 OD2 ASP C 331 ND2 ASN C 338 2.09
REMARK 500 O TYR C 43 OG1 THR C 570 2.19
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 ASN A 402 56.69 -91.97
REMARK 500 SER A 433 67.05 36.65
REMARK 500 PRO A 434 44.73 -82.32
REMARK 500 ASP A 435 -3.54 65.63
REMARK 500 ALA A 436 165.84 179.98
REMARK 500 ALA A 438 -0.75 -140.95
REMARK 500 ASN A 472 -60.30 -101.25
REMARK 500 GLN B 72 -161.67 -78.11
REMARK 500 ASN B 74 12.03 -142.55
REMARK 500 TRP B 124 -166.46 -129.33
REMARK 500 ILE B 193 -60.03 -124.74
REMARK 500 SER B 242 -13.94 75.78
REMARK 500 ASP B 243 164.40 178.98
REMARK 500 ALA B 306 -62.79 -93.72
REMARK 500 THR B 401 59.41 -94.78
REMARK 500 ASN B 450 79.67 -156.35
REMARK 500 SER B 473 31.84 -141.57
REMARK 500 ASN B 487 24.27 -140.33
REMARK 500 ASN B 520 -28.28 75.10
REMARK 500 GLU B 521 -19.93 -152.45
REMARK 500 SER B 630 -27.07 73.85
REMARK 500 ASP B 678 -71.75 -83.29
REMARK 500 ASN B 679 30.14 -147.30
REMARK 500 TYR C 58 77.14 -101.33
REMARK 500 SER C 64 -168.76 -160.43
REMARK 500 PHE C 98 -7.54 71.10
REMARK 500 GLN C 123 -66.39 -96.93
REMARK 500 TRP C 124 -167.76 -126.38
REMARK 500 LYS C 139 -84.36 -82.79
REMARK 500 ARG C 140 2.82 -159.88
REMARK 500 ASN C 151 53.05 -92.10
REMARK 500 ILE C 193 -59.95 -123.26
REMARK 500 TYR C 241 -79.99 -79.42
REMARK 500 SER C 242 -171.24 167.59
REMARK 500 TRP C 337 79.14 -103.38
REMARK 500 THR C 401 51.81 -91.56
REMARK 500 SER C 473 16.32 -142.22
REMARK 500 ASN C 520 -27.02 74.99
REMARK 500 GLU C 521 -19.20 -150.38
REMARK 500 ALA C 548 17.39 54.25
REMARK 500 SER C 630 -145.52 -159.89
REMARK 500 TYR C 631 -31.00 -38.89
REMARK 500 ASP C 678 -66.08 -94.48
REMARK 500 ILE C 742 109.53 -56.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL B 546 TYR B 547 148.20
REMARK 500 LYS C 139 ARG C 140 145.11
REMARK 500 SER C 242 ASP C 243 148.06
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-64732 RELATED DB: EMDB
REMARK 900 COMPLEX STRUCTURE OF 2014-422 SPIKE RBD BOUND TO HUMAN DPP4
DBREF1 9V2L A 371 593 UNP A0A2R4KP93_MERS
DBREF2 9V2L A A0A2R4KP93 371 593
DBREF 9V2L B 40 766 UNP P27487 DPP4_HUMAN 40 766
DBREF 9V2L C 40 766 UNP P27487 DPP4_HUMAN 40 766
SEQRES 1 A 223 GLU VAL HIS SER ARG GLY GLN PHE ILE GLU GLN PRO ASN
SEQRES 2 A 223 SER VAL GLU CYS ASP PHE THR LYS LEU LEU SER GLY THR
SEQRES 3 A 223 PRO PRO GLN VAL TYR ASN PHE ASN ARG LEU VAL PHE THR
SEQRES 4 A 223 ASN CYS ASN TYR ASN LEU THR LYS LEU LEU SER LEU PHE
SEQRES 5 A 223 MET VAL ASN GLU PHE SER CYS ASP GLY ILE SER PRO ASP
SEQRES 6 A 223 ALA ILE ALA ARG GLY CYS TYR SER SER LEU THR VAL ASP
SEQRES 7 A 223 TYR PHE ALA TYR PRO LEU SER MET LYS SER TYR MET GLN
SEQRES 8 A 223 PRO GLY SER ALA GLY VAL ILE SER GLN TYR ASN TYR LYS
SEQRES 9 A 223 GLN SER PHE ALA ASN PRO THR CYS ARG ILE PHE ALA THR
SEQRES 10 A 223 ALA PRO ALA ASN LEU THR ILE THR LYS PRO SER SER TYR
SEQRES 11 A 223 SER PHE ILE SER LYS CYS SER ARG LEU THR GLY ASP ASN
SEQRES 12 A 223 SER HIS ILE GLU THR PRO ILE VAL ILE ASN PRO GLY GLU
SEQRES 13 A 223 TYR SER ILE CYS LYS ASN PHE ALA PRO ASN GLY PHE SER
SEQRES 14 A 223 GLN ASP GLY ASP TYR PHE THR ARG GLN LEU SER GLN LEU
SEQRES 15 A 223 GLU GLY GLY GLY ILE LEU VAL GLY VAL GLY SER VAL THR
SEQRES 16 A 223 PRO MET THR ASP THR LEU GLN MET GLY PHE ILE ILE SER
SEQRES 17 A 223 VAL GLN TYR GLY THR ASP THR ASN SER VAL CYS PRO MET
SEQRES 18 A 223 MET ASP
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 C 727 ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR
SEQRES 2 C 727 TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP
SEQRES 3 C 727 HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL
SEQRES 4 C 727 PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU
SEQRES 5 C 727 ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP
SEQRES 6 C 727 TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU
SEQRES 7 C 727 TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA
SEQRES 8 C 727 SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE
SEQRES 9 C 727 THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR
SEQRES 10 C 727 TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN
SEQRES 11 C 727 ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER
SEQRES 12 C 727 TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR
SEQRES 13 C 727 ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE
SEQRES 14 C 727 SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR
SEQRES 15 C 727 PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO
SEQRES 16 C 727 LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN
SEQRES 17 C 727 TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY
SEQRES 18 C 727 ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR
SEQRES 19 C 727 ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN
SEQRES 20 C 727 ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR
SEQRES 21 C 727 LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER
SEQRES 22 C 727 LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET
SEQRES 23 C 727 ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN
SEQRES 24 C 727 CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR
SEQRES 25 C 727 GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE
SEQRES 26 C 727 THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN
SEQRES 27 C 727 GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP
SEQRES 28 C 727 LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU
SEQRES 29 C 727 VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR
SEQRES 30 C 727 TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG
SEQRES 31 C 727 ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL
SEQRES 32 C 727 THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN
SEQRES 33 C 727 TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR
SEQRES 34 C 727 GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR
SEQRES 35 C 727 LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU
SEQRES 36 C 727 GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL
SEQRES 37 C 727 GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN
SEQRES 38 C 727 GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS
SEQRES 39 C 727 PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL
SEQRES 40 C 727 TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE
SEQRES 41 C 727 ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN
SEQRES 42 C 727 ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR
SEQRES 43 C 727 GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU
SEQRES 44 C 727 GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG
SEQRES 45 C 727 GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE
SEQRES 46 C 727 ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER
SEQRES 47 C 727 MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY
SEQRES 48 C 727 ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP
SEQRES 49 C 727 SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO
SEQRES 50 C 727 GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET
SEQRES 51 C 727 SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU
SEQRES 52 C 727 ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN
SEQRES 53 C 727 SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL
SEQRES 54 C 727 ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY
SEQRES 55 C 727 ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS
SEQRES 56 C 727 MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO
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 B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HET NAG C 801 14
HET NAG C 802 14
HET NAG C 803 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
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
FORMUL 4 NAG 13(C8 H15 N O6)
HELIX 1 AA1 ASN A 414 PHE A 422 1 9
HELIX 2 AA2 PRO A 453 GLN A 461 5 9
HELIX 3 AA3 GLY A 466 ASN A 472 1 7
HELIX 4 AA4 GLY A 511 HIS A 515 5 5
HELIX 5 AA5 SER A 528 ALA A 534 5 7
HELIX 6 AA6 THR B 44 LYS B 50 1 7
HELIX 7 AA7 ASP B 200 GLU B 206 1 7
HELIX 8 AA8 ASP B 274 LEU B 276 5 3
HELIX 9 AA9 PRO B 290 ILE B 295 1 6
HELIX 10 AB1 GLU B 421 MET B 425 5 5
HELIX 11 AB2 LYS B 463 ALA B 465 5 3
HELIX 12 AB3 ASN B 497 GLN B 505 1 9
HELIX 13 AB4 ASN B 562 GLU B 571 1 10
HELIX 14 AB5 ILE B 590 ASN B 595 5 6
HELIX 15 AB6 THR B 600 MET B 616 1 17
HELIX 16 AB7 SER B 630 GLY B 641 1 12
HELIX 17 AB8 ASP B 663 GLY B 672 1 10
HELIX 18 AB9 ASN B 679 ASN B 685 1 7
HELIX 19 AC1 VAL B 688 VAL B 698 5 11
HELIX 20 AC2 HIS B 712 ASP B 725 1 14
HELIX 21 AC3 SER B 744 PHE B 763 1 20
HELIX 22 AC4 THR C 44 LYS C 50 1 7
HELIX 23 AC5 ASP C 200 GLU C 206 1 7
HELIX 24 AC6 PRO C 290 ILE C 295 1 6
HELIX 25 AC7 GLU C 421 MET C 425 5 5
HELIX 26 AC8 LYS C 463 ALA C 465 5 3
HELIX 27 AC9 ASN C 497 LEU C 504 1 8
HELIX 28 AD1 ASN C 562 GLU C 571 1 10
HELIX 29 AD2 GLY C 587 HIS C 592 1 6
HELIX 30 AD3 ALA C 593 ASN C 595 5 3
HELIX 31 AD4 THR C 600 LYS C 615 1 16
HELIX 32 AD5 SER C 630 GLY C 641 1 12
HELIX 33 AD6 ASP C 663 MET C 671 1 9
HELIX 34 AD7 LEU C 680 SER C 686 1 7
HELIX 35 AD8 THR C 687 VAL C 698 5 12
HELIX 36 AD9 PHE C 713 GLY C 727 1 15
HELIX 37 AE1 SER C 744 SER C 764 1 21
SHEET 1 AA1 2 ASN A 412 TYR A 413 0
SHEET 2 AA1 2 CYS A 589 PRO A 590 1 O CYS A 589 N TYR A 413
SHEET 1 AA2 4 MET A 423 PHE A 427 0
SHEET 2 AA2 4 THR A 481 ALA A 488 -1 O THR A 487 N MET A 423
SHEET 3 AA2 4 LEU A 571 GLN A 580 -1 O LEU A 571 N ALA A 488
SHEET 4 AA2 4 SER A 444 VAL A 447 -1 N THR A 446 O SER A 578
SHEET 1 AA3 4 ILE A 516 GLU A 517 0
SHEET 2 AA3 4 TYR A 500 THR A 510 -1 N THR A 510 O ILE A 516
SHEET 3 AA3 4 ILE A 557 THR A 565 -1 O SER A 563 N PHE A 502
SHEET 4 AA3 4 ASP A 543 TYR A 544 -1 N ASP A 543 O GLY A 562
SHEET 1 AA4 4 ILE A 516 GLU A 517 0
SHEET 2 AA4 4 TYR A 500 THR A 510 -1 N THR A 510 O ILE A 516
SHEET 3 AA4 4 ILE A 557 THR A 565 -1 O SER A 563 N PHE A 502
SHEET 4 AA4 4 ARG A 547 GLN A 548 -1 N ARG A 547 O LEU A 558
SHEET 1 AA5 2 LYS B 41 THR B 42 0
SHEET 2 AA5 2 VAL B 507 GLN B 508 1 O GLN B 508 N LYS B 41
SHEET 1 AA6 3 GLU B 67 LYS B 71 0
SHEET 2 AA6 3 ILE B 76 ASN B 80 -1 O PHE B 79 N TYR B 68
SHEET 3 AA6 3 SER B 87 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 AA7 3 ASP B 104 ILE B 107 0
SHEET 2 AA7 3 PHE B 113 LYS B 122 -1 O GLU B 117 N ASP B 104
SHEET 3 AA7 3 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 1 AA8 4 TRP B 154 TRP B 157 0
SHEET 2 AA8 4 LEU B 164 VAL B 167 -1 O VAL B 167 N TRP B 154
SHEET 3 AA8 4 ILE B 172 LYS B 175 -1 O LYS B 175 N LEU B 164
SHEET 4 AA8 4 TYR B 183 ARG B 184 -1 O TYR B 183 N VAL B 174
SHEET 1 AA9 3 ILE B 194 ASN B 196 0
SHEET 2 AA9 3 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AA9 3 LEU B 214 TRP B 216 -1 N TRP B 215 O ALA B 224
SHEET 1 AB1 4 ILE B 194 ASN B 196 0
SHEET 2 AB1 4 PHE B 222 ASN B 229 -1 O PHE B 228 N TYR B 195
SHEET 3 AB1 4 THR B 265 ASN B 272 -1 O LYS B 267 N GLN B 227
SHEET 4 AB1 4 SER B 284 ILE B 287 -1 O ILE B 287 N PHE B 268
SHEET 1 AB2 2 LEU B 235 PHE B 240 0
SHEET 2 AB2 2 LYS B 250 PRO B 255 -1 O LYS B 250 N PHE B 240
SHEET 1 AB3 4 HIS B 298 THR B 307 0
SHEET 2 AB3 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 AB3 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 AB3 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 AB4 4 HIS B 298 THR B 307 0
SHEET 2 AB4 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 AB4 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 AB4 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 AB5 4 HIS B 363 PHE B 364 0
SHEET 2 AB5 4 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AB5 4 ARG B 382 GLN B 388 -1 O CYS B 385 N LYS B 373
SHEET 4 AB5 4 CYS B 394 PHE B 396 -1 O THR B 395 N TYR B 386
SHEET 1 AB6 4 VAL B 404 LEU B 410 0
SHEET 2 AB6 4 TYR B 414 SER B 419 -1 O ILE B 418 N ILE B 405
SHEET 3 AB6 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AB6 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 AB7 4 TYR B 457 PHE B 461 0
SHEET 2 AB7 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 AB7 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 AB7 4 LYS B 489 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 AB8 8 LYS B 513 LEU B 519 0
SHEET 2 AB8 8 THR B 522 ILE B 529 -1 O PHE B 524 N ILE B 517
SHEET 3 AB8 8 ILE B 574 PHE B 578 -1 O SER B 577 N GLN B 527
SHEET 4 AB8 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 AB8 8 VAL B 619 TRP B 629 1 O ASP B 620 N TYR B 540
SHEET 6 AB8 8 CYS B 649 VAL B 653 1 O VAL B 653 N GLY B 628
SHEET 7 AB8 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 AB8 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 AB9 2 LYS C 41 THR C 42 0
SHEET 2 AB9 2 VAL C 507 GLN C 508 1 O GLN C 508 N LYS C 41
SHEET 1 AC1 3 GLU C 67 LYS C 71 0
SHEET 2 AC1 3 ILE C 76 ASN C 80 -1 O LEU C 77 N TYR C 70
SHEET 3 AC1 3 SER C 86 LEU C 90 -1 O SER C 87 N VAL C 78
SHEET 1 AC2 4 TYR C 105 ILE C 107 0
SHEET 2 AC2 4 PHE C 113 LYS C 122 -1 O LEU C 115 N SER C 106
SHEET 3 AC2 4 TYR C 128 ASP C 136 -1 O SER C 131 N TYR C 118
SHEET 4 AC2 4 LEU C 142 ILE C 143 -1 O ILE C 143 N ILE C 134
SHEET 1 AC3 4 THR C 152 TRP C 157 0
SHEET 2 AC3 4 LEU C 164 TRP C 168 -1 O VAL C 167 N GLN C 153
SHEET 3 AC3 4 ILE C 172 LYS C 175 -1 O LYS C 175 N LEU C 164
SHEET 4 AC3 4 TYR C 183 ARG C 184 -1 O TYR C 183 N VAL C 174
SHEET 1 AC4 3 ILE C 194 ASN C 196 0
SHEET 2 AC4 3 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AC4 3 LEU C 214 TRP C 216 -1 N TRP C 215 O ALA C 224
SHEET 1 AC5 4 ILE C 194 ASN C 196 0
SHEET 2 AC5 4 PHE C 222 ASN C 229 -1 O PHE C 228 N TYR C 195
SHEET 3 AC5 4 THR C 265 ASN C 272 -1 O PHE C 269 N TYR C 225
SHEET 4 AC5 4 SER C 284 GLN C 286 -1 O ILE C 285 N VAL C 270
SHEET 1 AC6 2 LEU C 235 PHE C 240 0
SHEET 2 AC6 2 LYS C 250 PRO C 255 -1 O VAL C 252 N TYR C 238
SHEET 1 AC7 4 HIS C 298 ASP C 302 0
SHEET 2 AC7 4 ILE C 311 ARG C 317 -1 O LEU C 316 N TYR C 299
SHEET 3 AC7 4 TYR C 322 CYS C 328 -1 O ASP C 326 N LEU C 313
SHEET 4 AC7 4 GLN C 344 MET C 348 -1 O GLU C 347 N SER C 323
SHEET 1 AC8 4 HIS C 363 PHE C 364 0
SHEET 2 AC8 4 SER C 370 SER C 376 -1 O TYR C 372 N HIS C 363
SHEET 3 AC8 4 ARG C 382 GLN C 388 -1 O CYS C 385 N LYS C 373
SHEET 4 AC8 4 THR C 395 PHE C 396 -1 O THR C 395 N TYR C 386
SHEET 1 AC9 4 VAL C 404 LEU C 410 0
SHEET 2 AC9 4 TYR C 414 SER C 419 -1 O TYR C 416 N ALA C 409
SHEET 3 AC9 4 ASN C 430 GLN C 435 -1 O TYR C 432 N TYR C 417
SHEET 4 AC9 4 VAL C 442 CYS C 444 -1 O THR C 443 N LYS C 433
SHEET 1 AD1 4 TYR C 457 PHE C 461 0
SHEET 2 AD1 4 TYR C 467 CYS C 472 -1 O ARG C 471 N SER C 458
SHEET 3 AD1 4 LEU C 479 SER C 484 -1 O HIS C 483 N TYR C 468
SHEET 4 AD1 4 LYS C 489 GLU C 495 -1 O LEU C 491 N LEU C 482
SHEET 1 AD2 8 LYS C 513 LEU C 519 0
SHEET 2 AD2 8 THR C 522 ILE C 529 -1 O THR C 522 N LEU C 519
SHEET 3 AD2 8 ILE C 574 PHE C 578 -1 O SER C 577 N GLN C 527
SHEET 4 AD2 8 TYR C 540 ASP C 545 1 N LEU C 543 O ILE C 574
SHEET 5 AD2 8 VAL C 619 GLY C 628 1 O ASP C 620 N TYR C 540
SHEET 6 AD2 8 CYS C 649 VAL C 653 1 O VAL C 653 N GLY C 628
SHEET 7 AD2 8 GLU C 699 GLY C 705 1 O LEU C 701 N GLY C 650
SHEET 8 AD2 8 GLN C 731 TYR C 735 1 O GLN C 731 N TYR C 700
SSBOND 1 CYS A 387 CYS A 411 1555 1555 2.03
SSBOND 2 CYS A 429 CYS A 482 1555 1555 2.04
SSBOND 3 CYS A 441 CYS A 589 1555 1555 2.03
SSBOND 4 CYS A 506 CYS A 530 1555 1555 2.03
SSBOND 5 CYS B 328 CYS B 339 1555 1555 2.03
SSBOND 6 CYS B 385 CYS B 394 1555 1555 2.02
SSBOND 7 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 8 CYS B 454 CYS B 472 1555 1555 2.03
SSBOND 9 CYS B 649 CYS B 762 1555 1555 2.04
SSBOND 10 CYS C 328 CYS C 339 1555 1555 2.04
SSBOND 11 CYS C 385 CYS C 394 1555 1555 2.04
SSBOND 12 CYS C 444 CYS C 447 1555 1555 2.03
SSBOND 13 CYS C 454 CYS C 472 1555 1555 2.03
SSBOND 14 CYS C 649 CYS C 762 1555 1555 2.04
LINK ND2 ASN B 85 C1 NAG B 801 1555 1555 1.44
LINK ND2 ASN B 92 C1 NAG B 804 1555 1555 1.44
LINK ND2 ASN B 150 C1 NAG B 802 1555 1555 1.44
LINK ND2 ASN B 219 C1 NAG D 1 1555 1555 1.43
LINK ND2 ASN B 229 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN B 281 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN B 321 C1 NAG B 803 1555 1555 1.44
LINK ND2 ASN C 150 C1 NAG C 801 1555 1555 1.44
LINK ND2 ASN C 229 C1 NAG C 802 1555 1555 1.44
LINK ND2 ASN C 685 C1 NAG C 803 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.45
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
TER 1587 MET A 591
TER 7530 SER B 764
TER 13473 SER C 764
MASTER 212 0 13 37 109 0 0 613652 3 220 130
END |