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HEADER VIRAL PROTEIN/HYDROLASE 27-OCT-24 9K9N
TITLE CRYO-EM STRUCTURE OF MJHKU4R-COV-1 RECEPTOR-BINDING DOMAIN COMPLEXED
TITLE 2 WITH HUMAN CD26
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 PROTEIN S1;
COMPND 8 CHAIN: C;
COMPND 9 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: SEQUENCE REFERENCE FOR STRAIN 'TYLONYCTERIS BAT
COMPND 12 CORONAVIRUS HKU4' IS NOT AVAILABLE IN UNIPROT AT THE TIME OF
COMPND 13 BIOCURATION. CURRENT SEQUENCE REFERENCE IS FROM UNIPROT ID
COMPND 14 A0AAE8ZFM2.
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: TYLONYCTERIS BAT CORONAVIRUS HKU4;
SOURCE 10 ORGANISM_TAXID: 694007;
SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS COMPLEX, VIRAL PROTEIN/HYDROLASE, VIRAL PROTEIN-HYDROLASE COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR J.Q.SUN
REVDAT 1 03-SEP-25 9K9N 0
JRNL AUTH Y.ZHANG,M.TIAN,Y.HAN,J.SUN,W.LI,C.BAI,C.SU,P.HAN
JRNL TITL RATIONAL DESIGN OF HUMAN CD26 RECEPTOR FOR A STRONG
JRNL TITL 2 NEUTRALIZING ABILITY AGAINST MJHKU4R-COV-1 AND MERS-COV
JRNL REF HLIFE 2025
JRNL REFN ESSN 2949-9283
JRNL DOI 10.1016/J.HLIFE.2025.05.005
REMARK 2
REMARK 2 RESOLUTION. 2.61 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) : 2.610
REMARK 3 NUMBER OF PARTICLES : 237919
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 9K9N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 29-OCT-24.
REMARK 100 THE DEPOSITION ID IS D_1300053103.
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 : CRYO-EM STRUCTURE OF MJHKU4R
REMARK 245 -COV-1 RECEPTOR-BINDING DOMAIN
REMARK 245 COMPLEXED WITH HUMAN CD26
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) : 1000.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00
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) : 6000.00
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, 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 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 MET A 7
REMARK 465 GLY A 8
REMARK 465 ILE A 9
REMARK 465 LEU A 10
REMARK 465 PRO A 11
REMARK 465 SER A 12
REMARK 465 PRO A 13
REMARK 465 GLY A 14
REMARK 465 MET A 15
REMARK 465 PRO A 16
REMARK 465 ALA A 17
REMARK 465 LEU A 18
REMARK 465 LEU A 19
REMARK 465 SER A 20
REMARK 465 LEU A 21
REMARK 465 VAL A 22
REMARK 465 SER A 23
REMARK 465 LEU A 24
REMARK 465 LEU A 25
REMARK 465 SER A 26
REMARK 465 VAL A 27
REMARK 465 LEU A 28
REMARK 465 LEU A 29
REMARK 465 MET A 30
REMARK 465 GLY A 31
REMARK 465 CYS A 32
REMARK 465 VAL A 33
REMARK 465 ALA A 34
REMARK 465 GLU A 35
REMARK 465 THR A 36
REMARK 465 GLY A 37
REMARK 465 THR A 38
REMARK 465 SER A 764
REMARK 465 LEU A 765
REMARK 465 PRO A 766
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 MET B 7
REMARK 465 GLY B 8
REMARK 465 ILE B 9
REMARK 465 LEU B 10
REMARK 465 PRO B 11
REMARK 465 SER B 12
REMARK 465 PRO B 13
REMARK 465 GLY B 14
REMARK 465 MET B 15
REMARK 465 PRO B 16
REMARK 465 ALA B 17
REMARK 465 LEU B 18
REMARK 465 LEU B 19
REMARK 465 SER B 20
REMARK 465 LEU B 21
REMARK 465 VAL B 22
REMARK 465 SER B 23
REMARK 465 LEU B 24
REMARK 465 LEU B 25
REMARK 465 SER B 26
REMARK 465 VAL B 27
REMARK 465 LEU B 28
REMARK 465 LEU B 29
REMARK 465 MET B 30
REMARK 465 GLY B 31
REMARK 465 CYS B 32
REMARK 465 VAL B 33
REMARK 465 ALA B 34
REMARK 465 GLU B 35
REMARK 465 THR B 36
REMARK 465 GLY B 37
REMARK 465 THR B 38
REMARK 465 SER B 764
REMARK 465 LEU B 765
REMARK 465 PRO B 766
REMARK 465 HIS B 767
REMARK 465 HIS B 768
REMARK 465 HIS B 769
REMARK 465 HIS B 770
REMARK 465 HIS B 771
REMARK 465 HIS B 772
REMARK 465 MET C 371
REMARK 465 HIS C 372
REMARK 465 SER C 373
REMARK 465 SER C 374
REMARK 465 ALA C 375
REMARK 465 LEU C 376
REMARK 465 LEU C 377
REMARK 465 CYS C 378
REMARK 465 CYS C 379
REMARK 465 LEU C 380
REMARK 465 VAL C 381
REMARK 465 LEU C 382
REMARK 465 LEU C 383
REMARK 465 THR C 384
REMARK 465 GLY C 385
REMARK 465 VAL C 386
REMARK 465 ARG C 387
REMARK 465 ALA C 388
REMARK 465 HIS C 596
REMARK 465 HIS C 597
REMARK 465 HIS C 598
REMARK 465 HIS C 599
REMARK 465 HIS C 600
REMARK 465 HIS C 601
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 ND2 ASN B 229 O5 NAG G 1 2.12
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 385 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 CYS B 394 CA - CB - SG ANGL. DEV. = 8.4 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 TRP A 124 -144.41 57.68
REMARK 500 ILE A 193 -58.74 -124.47
REMARK 500 VAL A 207 -62.85 -109.10
REMARK 500 SER A 242 -148.14 64.33
REMARK 500 THR A 401 55.94 -93.63
REMARK 500 LYS A 423 10.77 59.23
REMARK 500 ASN A 450 83.09 -159.38
REMARK 500 SER A 630 -112.60 57.26
REMARK 500 HIS B 66 16.98 -142.09
REMARK 500 TRP B 124 -164.78 -128.65
REMARK 500 ILE B 193 -62.74 -123.89
REMARK 500 VAL B 207 -61.10 -109.41
REMARK 500 ALA B 213 32.18 -140.25
REMARK 500 ASP B 243 165.56 73.25
REMARK 500 THR B 401 53.74 -92.77
REMARK 500 ARG B 453 -10.17 69.33
REMARK 500 SER B 630 -107.02 55.36
REMARK 500 ALA B 707 32.17 -95.81
REMARK 500 MET C 460 49.94 -84.86
REMARK 500 GLU C 521 69.11 60.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-62194 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF MJHKU4R-COV-1 RECEPTOR-BINDING DOMAIN
REMARK 900 COMPLEXED WITH HUMAN CD26
DBREF 9K9N A 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF 9K9N B 39 766 UNP P27487 DPP4_HUMAN 39 766
DBREF1 9K9N C 389 595 UNP A0AAE8ZFM2_9BETC
DBREF2 9K9N C A0AAE8ZFM2 389 595
SEQADV 9K9N MET A 7 UNP P27487 INITIATING METHIONINE
SEQADV 9K9N GLY A 8 UNP P27487 EXPRESSION TAG
SEQADV 9K9N ILE A 9 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU A 10 UNP P27487 EXPRESSION TAG
SEQADV 9K9N PRO A 11 UNP P27487 EXPRESSION TAG
SEQADV 9K9N SER A 12 UNP P27487 EXPRESSION TAG
SEQADV 9K9N PRO A 13 UNP P27487 EXPRESSION TAG
SEQADV 9K9N GLY A 14 UNP P27487 EXPRESSION TAG
SEQADV 9K9N MET A 15 UNP P27487 EXPRESSION TAG
SEQADV 9K9N PRO A 16 UNP P27487 EXPRESSION TAG
SEQADV 9K9N ALA A 17 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU A 18 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU A 19 UNP P27487 EXPRESSION TAG
SEQADV 9K9N SER A 20 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU A 21 UNP P27487 EXPRESSION TAG
SEQADV 9K9N VAL A 22 UNP P27487 EXPRESSION TAG
SEQADV 9K9N SER A 23 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU A 24 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU A 25 UNP P27487 EXPRESSION TAG
SEQADV 9K9N SER A 26 UNP P27487 EXPRESSION TAG
SEQADV 9K9N VAL A 27 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU A 28 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU A 29 UNP P27487 EXPRESSION TAG
SEQADV 9K9N MET A 30 UNP P27487 EXPRESSION TAG
SEQADV 9K9N GLY A 31 UNP P27487 EXPRESSION TAG
SEQADV 9K9N CYS A 32 UNP P27487 EXPRESSION TAG
SEQADV 9K9N VAL A 33 UNP P27487 EXPRESSION TAG
SEQADV 9K9N ALA A 34 UNP P27487 EXPRESSION TAG
SEQADV 9K9N GLU A 35 UNP P27487 EXPRESSION TAG
SEQADV 9K9N THR A 36 UNP P27487 EXPRESSION TAG
SEQADV 9K9N GLY A 37 UNP P27487 EXPRESSION TAG
SEQADV 9K9N THR A 38 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS A 767 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS A 768 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS A 769 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS A 770 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS A 771 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS A 772 UNP P27487 EXPRESSION TAG
SEQADV 9K9N MET B 7 UNP P27487 INITIATING METHIONINE
SEQADV 9K9N GLY B 8 UNP P27487 EXPRESSION TAG
SEQADV 9K9N ILE B 9 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU B 10 UNP P27487 EXPRESSION TAG
SEQADV 9K9N PRO B 11 UNP P27487 EXPRESSION TAG
SEQADV 9K9N SER B 12 UNP P27487 EXPRESSION TAG
SEQADV 9K9N PRO B 13 UNP P27487 EXPRESSION TAG
SEQADV 9K9N GLY B 14 UNP P27487 EXPRESSION TAG
SEQADV 9K9N MET B 15 UNP P27487 EXPRESSION TAG
SEQADV 9K9N PRO B 16 UNP P27487 EXPRESSION TAG
SEQADV 9K9N ALA B 17 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU B 18 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU B 19 UNP P27487 EXPRESSION TAG
SEQADV 9K9N SER B 20 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU B 21 UNP P27487 EXPRESSION TAG
SEQADV 9K9N VAL B 22 UNP P27487 EXPRESSION TAG
SEQADV 9K9N SER B 23 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU B 24 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU B 25 UNP P27487 EXPRESSION TAG
SEQADV 9K9N SER B 26 UNP P27487 EXPRESSION TAG
SEQADV 9K9N VAL B 27 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU B 28 UNP P27487 EXPRESSION TAG
SEQADV 9K9N LEU B 29 UNP P27487 EXPRESSION TAG
SEQADV 9K9N MET B 30 UNP P27487 EXPRESSION TAG
SEQADV 9K9N GLY B 31 UNP P27487 EXPRESSION TAG
SEQADV 9K9N CYS B 32 UNP P27487 EXPRESSION TAG
SEQADV 9K9N VAL B 33 UNP P27487 EXPRESSION TAG
SEQADV 9K9N ALA B 34 UNP P27487 EXPRESSION TAG
SEQADV 9K9N GLU B 35 UNP P27487 EXPRESSION TAG
SEQADV 9K9N THR B 36 UNP P27487 EXPRESSION TAG
SEQADV 9K9N GLY B 37 UNP P27487 EXPRESSION TAG
SEQADV 9K9N THR B 38 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS B 767 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS B 768 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS B 769 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS B 770 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS B 771 UNP P27487 EXPRESSION TAG
SEQADV 9K9N HIS B 772 UNP P27487 EXPRESSION TAG
SEQADV 9K9N MET C 371 UNP A0AAE8ZFM INITIATING METHIONINE
SEQADV 9K9N HIS C 372 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N SER C 373 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N SER C 374 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N ALA C 375 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N LEU C 376 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N LEU C 377 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N CYS C 378 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N CYS C 379 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N LEU C 380 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N VAL C 381 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N LEU C 382 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N LEU C 383 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N THR C 384 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N GLY C 385 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N VAL C 386 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N ARG C 387 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N ALA C 388 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N ALA C 482 UNP A0AAE8ZFM SER 482 CONFLICT
SEQADV 9K9N GLU C 544 UNP A0AAE8ZFM VAL 544 CONFLICT
SEQADV 9K9N HIS C 596 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N HIS C 597 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N HIS C 598 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N HIS C 599 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N HIS C 600 UNP A0AAE8ZFM EXPRESSION TAG
SEQADV 9K9N HIS C 601 UNP A0AAE8ZFM EXPRESSION TAG
SEQRES 1 A 766 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU
SEQRES 2 A 766 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS
SEQRES 3 A 766 VAL ALA GLU THR GLY THR SER ARG LYS THR TYR THR LEU
SEQRES 4 A 766 THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR
SEQRES 5 A 766 SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS
SEQRES 6 A 766 GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY
SEQRES 7 A 766 ASN SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU
SEQRES 8 A 766 PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP
SEQRES 9 A 766 GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN
SEQRES 10 A 766 TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP
SEQRES 11 A 766 LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO
SEQRES 12 A 766 ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS
SEQRES 13 A 766 LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS
SEQRES 14 A 766 ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR
SEQRES 15 A 766 GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP
SEQRES 16 A 766 VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU
SEQRES 17 A 766 TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN
SEQRES 18 A 766 PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE
SEQRES 19 A 766 TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG
SEQRES 20 A 766 VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL
SEQRES 21 A 766 LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL
SEQRES 22 A 766 THR ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER
SEQRES 23 A 766 MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP
SEQRES 24 A 766 ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG
SEQRES 25 A 766 ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP
SEQRES 26 A 766 GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN
SEQRES 27 A 766 HIS ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE
SEQRES 28 A 766 ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER
SEQRES 29 A 766 PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS
SEQRES 30 A 766 ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE
SEQRES 31 A 766 ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA
SEQRES 32 A 766 LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR
SEQRES 33 A 766 LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN
SEQRES 34 A 766 LEU SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU
SEQRES 35 A 766 LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE
SEQRES 36 A 766 SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY
SEQRES 37 A 766 PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN
SEQRES 38 A 766 ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU
SEQRES 39 A 766 ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS
SEQRES 40 A 766 LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR
SEQRES 41 A 766 GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS
SEQRES 42 A 766 TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER
SEQRES 43 A 766 GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR
SEQRES 44 A 766 TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE
SEQRES 45 A 766 ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET
SEQRES 46 A 766 HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU
SEQRES 47 A 766 ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY
SEQRES 48 A 766 PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER
SEQRES 49 A 766 TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY
SEQRES 50 A 766 SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL
SEQRES 51 A 766 SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG
SEQRES 52 A 766 TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS
SEQRES 53 A 766 TYR ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE
SEQRES 54 A 766 LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP
SEQRES 55 A 766 ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS
SEQRES 56 A 766 ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP
SEQRES 57 A 766 TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA
SEQRES 58 A 766 HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS
SEQRES 59 A 766 GLN CYS PHE SER LEU PRO HIS HIS HIS HIS HIS HIS
SEQRES 1 B 766 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU
SEQRES 2 B 766 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS
SEQRES 3 B 766 VAL ALA GLU THR GLY THR SER ARG LYS THR TYR THR LEU
SEQRES 4 B 766 THR ASP TYR LEU LYS ASN THR TYR ARG LEU LYS LEU TYR
SEQRES 5 B 766 SER LEU ARG TRP ILE SER ASP HIS GLU TYR LEU TYR LYS
SEQRES 6 B 766 GLN GLU ASN ASN ILE LEU VAL PHE ASN ALA GLU TYR GLY
SEQRES 7 B 766 ASN SER SER VAL PHE LEU GLU ASN SER THR PHE ASP GLU
SEQRES 8 B 766 PHE GLY HIS SER ILE ASN ASP TYR SER ILE SER PRO ASP
SEQRES 9 B 766 GLY GLN PHE ILE LEU LEU GLU TYR ASN TYR VAL LYS GLN
SEQRES 10 B 766 TRP ARG HIS SER TYR THR ALA SER TYR ASP ILE TYR ASP
SEQRES 11 B 766 LEU ASN LYS ARG GLN LEU ILE THR GLU GLU ARG ILE PRO
SEQRES 12 B 766 ASN ASN THR GLN TRP VAL THR TRP SER PRO VAL GLY HIS
SEQRES 13 B 766 LYS LEU ALA TYR VAL TRP ASN ASN ASP ILE TYR VAL LYS
SEQRES 14 B 766 ILE GLU PRO ASN LEU PRO SER TYR ARG ILE THR TRP THR
SEQRES 15 B 766 GLY LYS GLU ASP ILE ILE TYR ASN GLY ILE THR ASP TRP
SEQRES 16 B 766 VAL TYR GLU GLU GLU VAL PHE SER ALA TYR SER ALA LEU
SEQRES 17 B 766 TRP TRP SER PRO ASN GLY THR PHE LEU ALA TYR ALA GLN
SEQRES 18 B 766 PHE ASN ASP THR GLU VAL PRO LEU ILE GLU TYR SER PHE
SEQRES 19 B 766 TYR SER ASP GLU SER LEU GLN TYR PRO LYS THR VAL ARG
SEQRES 20 B 766 VAL PRO TYR PRO LYS ALA GLY ALA VAL ASN PRO THR VAL
SEQRES 21 B 766 LYS PHE PHE VAL VAL ASN THR ASP SER LEU SER SER VAL
SEQRES 22 B 766 THR ASN ALA THR SER ILE GLN ILE THR ALA PRO ALA SER
SEQRES 23 B 766 MET LEU ILE GLY ASP HIS TYR LEU CYS ASP VAL THR TRP
SEQRES 24 B 766 ALA THR GLN GLU ARG ILE SER LEU GLN TRP LEU ARG ARG
SEQRES 25 B 766 ILE GLN ASN TYR SER VAL MET ASP ILE CYS ASP TYR ASP
SEQRES 26 B 766 GLU SER SER GLY ARG TRP ASN CYS LEU VAL ALA ARG GLN
SEQRES 27 B 766 HIS ILE GLU MET SER THR THR GLY TRP VAL GLY ARG PHE
SEQRES 28 B 766 ARG PRO SER GLU PRO HIS PHE THR LEU ASP GLY ASN SER
SEQRES 29 B 766 PHE TYR LYS ILE ILE SER ASN GLU GLU GLY TYR ARG HIS
SEQRES 30 B 766 ILE CYS TYR PHE GLN ILE ASP LYS LYS ASP CYS THR PHE
SEQRES 31 B 766 ILE THR LYS GLY THR TRP GLU VAL ILE GLY ILE GLU ALA
SEQRES 32 B 766 LEU THR SER ASP TYR LEU TYR TYR ILE SER ASN GLU TYR
SEQRES 33 B 766 LYS GLY MET PRO GLY GLY ARG ASN LEU TYR LYS ILE GLN
SEQRES 34 B 766 LEU SER ASP TYR THR LYS VAL THR CYS LEU SER CYS GLU
SEQRES 35 B 766 LEU ASN PRO GLU ARG CYS GLN TYR TYR SER VAL SER PHE
SEQRES 36 B 766 SER LYS GLU ALA LYS TYR TYR GLN LEU ARG CYS SER GLY
SEQRES 37 B 766 PRO GLY LEU PRO LEU TYR THR LEU HIS SER SER VAL ASN
SEQRES 38 B 766 ASP LYS GLY LEU ARG VAL LEU GLU ASP ASN SER ALA LEU
SEQRES 39 B 766 ASP LYS MET LEU GLN ASN VAL GLN MET PRO SER LYS LYS
SEQRES 40 B 766 LEU ASP PHE ILE ILE LEU ASN GLU THR LYS PHE TRP TYR
SEQRES 41 B 766 GLN MET ILE LEU PRO PRO HIS PHE ASP LYS SER LYS LYS
SEQRES 42 B 766 TYR PRO LEU LEU LEU ASP VAL TYR ALA GLY PRO CYS SER
SEQRES 43 B 766 GLN LYS ALA ASP THR VAL PHE ARG LEU ASN TRP ALA THR
SEQRES 44 B 766 TYR LEU ALA SER THR GLU ASN ILE ILE VAL ALA SER PHE
SEQRES 45 B 766 ASP GLY ARG GLY SER GLY TYR GLN GLY ASP LYS ILE MET
SEQRES 46 B 766 HIS ALA ILE ASN ARG ARG LEU GLY THR PHE GLU VAL GLU
SEQRES 47 B 766 ASP GLN ILE GLU ALA ALA ARG GLN PHE SER LYS MET GLY
SEQRES 48 B 766 PHE VAL ASP ASN LYS ARG ILE ALA ILE TRP GLY TRP SER
SEQRES 49 B 766 TYR GLY GLY TYR VAL THR SER MET VAL LEU GLY SER GLY
SEQRES 50 B 766 SER GLY VAL PHE LYS CYS GLY ILE ALA VAL ALA PRO VAL
SEQRES 51 B 766 SER ARG TRP GLU TYR TYR ASP SER VAL TYR THR GLU ARG
SEQRES 52 B 766 TYR MET GLY LEU PRO THR PRO GLU ASP ASN LEU ASP HIS
SEQRES 53 B 766 TYR ARG ASN SER THR VAL MET SER ARG ALA GLU ASN PHE
SEQRES 54 B 766 LYS GLN VAL GLU TYR LEU LEU ILE HIS GLY THR ALA ASP
SEQRES 55 B 766 ASP ASN VAL HIS PHE GLN GLN SER ALA GLN ILE SER LYS
SEQRES 56 B 766 ALA LEU VAL ASP VAL GLY VAL ASP PHE GLN ALA MET TRP
SEQRES 57 B 766 TYR THR ASP GLU ASP HIS GLY ILE ALA SER SER THR ALA
SEQRES 58 B 766 HIS GLN HIS ILE TYR THR HIS MET SER HIS PHE ILE LYS
SEQRES 59 B 766 GLN CYS PHE SER LEU PRO HIS HIS HIS HIS HIS HIS
SEQRES 1 C 231 MET HIS SER SER ALA LEU LEU CYS CYS LEU VAL LEU LEU
SEQRES 2 C 231 THR GLY VAL ARG ALA LYS GLU CYS ASP PHE THR PRO MET
SEQRES 3 C 231 LEU VAL GLY VAL PRO PRO GLN VAL TYR ASN PHE LYS ARG
SEQRES 4 C 231 LEU VAL PHE THR ASN CYS ASN TYR ASN LEU THR LYS LEU
SEQRES 5 C 231 LEU SER LEU PHE MET VAL ASN GLU PHE SER CYS ASN GLY
SEQRES 6 C 231 ILE SER PRO ASP ALA ILE ALA ARG GLY CYS TYR SER SER
SEQRES 7 C 231 LEU THR VAL ASP TYR PHE ALA TYR PRO LEU SER MET ARG
SEQRES 8 C 231 SER TYR ILE GLN PRO GLY SER ALA GLY ASP ILE SER LEU
SEQRES 9 C 231 TYR ASN TYR LYS GLN SER PHE ALA ASN PRO THR CYS ARG
SEQRES 10 C 231 VAL LEU ALA THR ALA PRO ALA ASN LEU THR LEU THR LYS
SEQRES 11 C 231 PRO SER ALA TYR GLY TYR PHE GLN LYS CYS SER ARG VAL
SEQRES 12 C 231 SER GLY GLU HIS ASN SER VAL GLU THR PRO LEU TYR ILE
SEQRES 13 C 231 ASN PRO GLY GLU TYR SER ILE CYS ARG SER PHE SER PRO
SEQRES 14 C 231 TYR GLY PHE SER GLU ASP GLY GLU VAL PHE ARG ARG GLN
SEQRES 15 C 231 LEU THR GLN TYR GLU GLY GLY GLY ILE LEU VAL GLY VAL
SEQRES 16 C 231 GLY ALA LYS LEU ALA MET THR ASP LYS LEU GLU MET GLY
SEQRES 17 C 231 PHE ILE ILE SER VAL GLN TYR GLY THR ASP THR ASN SER
SEQRES 18 C 231 VAL CYS PRO MET HIS HIS HIS HIS HIS HIS
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 G 1 14
HET NAG G 2 14
HET BMA G 3 11
HET MAN G 4 11
HET MAN G 5 11
HET NAG H 1 14
HET NAG H 2 14
HET FUC H 3 10
HET NAG I 1 14
HET NAG I 2 14
HET NAG A 801 14
HET NAG A 802 14
HET NAG A 803 14
HET NAG A 804 14
HET NAG A 805 14
HET NAG A 806 14
HET NAG B 801 14
HET NAG B 802 14
HET NAG B 803 14
HET NAG B 804 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
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 MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
FORMUL 4 NAG 22(C8 H15 N O6)
FORMUL 7 BMA C6 H12 O6
FORMUL 7 MAN 2(C6 H12 O6)
FORMUL 8 FUC C6 H12 O5
HELIX 1 AA1 THR A 44 ASN A 51 1 8
HELIX 2 AA2 GLU A 91 GLU A 97 1 7
HELIX 3 AA3 ASP A 200 GLU A 206 1 7
HELIX 4 AA4 LEU A 340 GLN A 344 5 5
HELIX 5 AA5 GLU A 421 MET A 425 5 5
HELIX 6 AA6 ASN A 497 GLN A 505 1 9
HELIX 7 AA7 ASN A 562 THR A 570 1 9
HELIX 8 AA8 GLY A 587 HIS A 592 1 6
HELIX 9 AA9 ALA A 593 ASN A 595 5 3
HELIX 10 AB1 THR A 600 MET A 616 1 17
HELIX 11 AB2 SER A 630 GLY A 641 1 12
HELIX 12 AB3 ARG A 658 TYR A 662 5 5
HELIX 13 AB4 ASP A 663 GLY A 672 1 10
HELIX 14 AB5 LEU A 680 SER A 686 1 7
HELIX 15 AB6 THR A 687 VAL A 698 5 12
HELIX 16 AB7 HIS A 712 GLY A 727 1 16
HELIX 17 AB8 SER A 744 PHE A 763 1 20
HELIX 18 AB9 THR B 44 ASN B 51 1 8
HELIX 19 AC1 GLU B 91 PHE B 98 1 8
HELIX 20 AC2 ASP B 200 VAL B 207 1 8
HELIX 21 AC3 PRO B 290 ILE B 295 1 6
HELIX 22 AC4 VAL B 341 GLN B 344 5 4
HELIX 23 AC5 GLU B 421 MET B 425 5 5
HELIX 24 AC6 ASN B 497 GLN B 505 1 9
HELIX 25 AC7 ASN B 562 THR B 570 1 9
HELIX 26 AC8 GLY B 587 HIS B 592 1 6
HELIX 27 AC9 ALA B 593 ASN B 595 5 3
HELIX 28 AD1 THR B 600 LYS B 615 1 16
HELIX 29 AD2 SER B 630 GLY B 641 1 12
HELIX 30 AD3 ARG B 658 TYR B 662 5 5
HELIX 31 AD4 ASP B 663 MET B 671 1 9
HELIX 32 AD5 LEU B 680 SER B 686 1 7
HELIX 33 AD6 THR B 687 VAL B 698 5 12
HELIX 34 AD7 HIS B 712 GLY B 727 1 16
HELIX 35 AD8 SER B 744 PHE B 763 1 20
HELIX 36 AD9 PHE C 393 VAL C 398 5 6
HELIX 37 AE1 ASN C 418 PHE C 426 1 9
HELIX 38 AE2 SER C 437 ARG C 443 1 7
HELIX 39 AE3 GLY C 470 TYR C 475 1 6
HELIX 40 AE4 SER C 532 PHE C 537 5 6
HELIX 41 AE5 GLY C 586 ASN C 590 5 5
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 PHE A 89 N ILE A 76
SHEET 1 AA3 4 ASP A 104 ILE A 107 0
SHEET 2 AA3 4 PHE A 113 GLN A 123 -1 O LEU A 115 N SER A 106
SHEET 3 AA3 4 SER A 127 ASP A 136 -1 O SER A 131 N TYR A 118
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 VAL A 167 -1 O VAL A 167 N TRP A 154
SHEET 3 AA4 4 ILE A 172 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 VAL A 271 N LEU A 223
SHEET 4 AA6 4 ILE A 285 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 THR A 307 0
SHEET 2 AA8 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 AA8 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 AA8 4 ARG A 336 ASN A 338 -1 O ARG A 336 N ASP A 331
SHEET 1 AA9 4 HIS A 298 THR A 307 0
SHEET 2 AA9 4 ARG A 310 ARG A 317 -1 O LEU A 316 N TYR A 299
SHEET 3 AA9 4 TYR A 322 ASP A 331 -1 O ASP A 326 N LEU A 313
SHEET 4 AA9 4 HIS A 345 MET A 348 -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 HIS A 383 N ILE A 375
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 ILE A 405
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 HIS A 483 N TYR A 468
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 PHE A 578 -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 TRP A 629 1 O ASP A 620 N TYR A 540
SHEET 6 AB4 8 CYS A 649 VAL A 653 1 O VAL A 653 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 ARG B 61 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 LEU B 77 N TYR B 70
SHEET 4 AB6 4 SER B 86 LEU B 90 -1 O PHE B 89 N ILE B 76
SHEET 1 AB7 4 ASP B 104 ILE B 107 0
SHEET 2 AB7 4 PHE B 113 LYS B 122 -1 O LEU B 115 N SER B 106
SHEET 3 AB7 4 TYR B 128 ASP B 136 -1 O SER B 131 N TYR B 118
SHEET 4 AB7 4 GLN B 141 LEU B 142 -1 O GLN B 141 N ASP B 136
SHEET 1 AB8 4 TRP B 154 TRP B 157 0
SHEET 2 AB8 4 LEU B 164 TRP B 168 -1 O VAL B 167 N TRP B 154
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 VAL B 271 N LEU B 223
SHEET 4 AC1 4 SER B 284 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 THR B 307 0
SHEET 2 AC3 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 AC3 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 AC3 4 TRP B 337 CYS B 339 -1 O ASN B 338 N ASP B 329
SHEET 1 AC4 4 HIS B 298 THR B 307 0
SHEET 2 AC4 4 ARG B 310 ARG B 317 -1 O SER B 312 N THR B 304
SHEET 3 AC4 4 TYR B 322 TYR B 330 -1 O ASP B 326 N LEU B 313
SHEET 4 AC4 4 HIS B 345 MET B 348 -1 O HIS B 345 N MET B 325
SHEET 1 AC5 3 HIS B 363 PHE B 364 0
SHEET 2 AC5 3 SER B 370 SER B 376 -1 O TYR B 372 N HIS B 363
SHEET 3 AC5 3 ARG B 382 GLN B 388 -1 O HIS B 383 N ILE B 375
SHEET 1 AC6 4 VAL B 404 LEU B 410 0
SHEET 2 AC6 4 TYR B 414 SER B 419 -1 O ILE B 418 N ILE B 405
SHEET 3 AC6 4 ASN B 430 GLN B 435 -1 O TYR B 432 N TYR B 417
SHEET 4 AC6 4 VAL B 442 CYS B 444 -1 O THR B 443 N LYS B 433
SHEET 1 AC7 4 TYR B 457 PHE B 461 0
SHEET 2 AC7 4 TYR B 467 CYS B 472 -1 O ARG B 471 N SER B 458
SHEET 3 AC7 4 LEU B 479 SER B 484 -1 O HIS B 483 N TYR B 468
SHEET 4 AC7 4 GLY B 490 GLU B 495 -1 O GLU B 495 N TYR B 480
SHEET 1 AC8 8 SER B 511 LEU B 519 0
SHEET 2 AC8 8 THR B 522 LEU B 530 -1 O THR B 522 N LEU B 519
SHEET 3 AC8 8 ILE B 574 PHE B 578 -1 O VAL B 575 N ILE B 529
SHEET 4 AC8 8 TYR B 540 VAL B 546 1 N LEU B 543 O ILE B 574
SHEET 5 AC8 8 VAL B 619 TRP B 629 1 O ASP B 620 N TYR B 540
SHEET 6 AC8 8 CYS B 649 VAL B 653 1 O ILE B 651 N ILE B 626
SHEET 7 AC8 8 GLU B 699 GLY B 705 1 O LEU B 701 N ALA B 652
SHEET 8 AC8 8 GLN B 731 TYR B 735 1 O GLN B 731 N TYR B 700
SHEET 1 AC9 5 LYS C 408 THR C 413 0
SHEET 2 AC9 5 SER C 448 ALA C 455 -1 O VAL C 451 N LEU C 410
SHEET 3 AC9 5 GLU C 576 GLN C 584 -1 O SER C 582 N THR C 450
SHEET 4 AC9 5 THR C 485 THR C 491 -1 N VAL C 488 O PHE C 579
SHEET 5 AC9 5 MET C 427 ASN C 434 -1 N ASN C 434 O THR C 485
SHEET 1 AD1 2 ASN C 416 TYR C 417 0
SHEET 2 AD1 2 CYS C 593 PRO C 594 1 O CYS C 593 N TYR C 417
SHEET 1 AD2 4 THR C 522 PRO C 523 0
SHEET 2 AD2 4 TYR C 504 VAL C 513 -1 N ARG C 512 O THR C 522
SHEET 3 AD2 4 ILE C 561 LEU C 569 -1 O ALA C 567 N TYR C 506
SHEET 4 AD2 4 VAL C 548 GLN C 552 -1 N ARG C 551 O LEU C 562
SSBOND 1 CYS A 328 CYS A 339 1555 1555 2.03
SSBOND 2 CYS A 385 CYS A 394 1555 1555 2.03
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 2.04
SSBOND 6 CYS B 328 CYS B 339 1555 1555 2.03
SSBOND 7 CYS B 385 CYS B 394 1555 1555 2.05
SSBOND 8 CYS B 444 CYS B 447 1555 1555 2.03
SSBOND 9 CYS B 454 CYS B 472 1555 1555 2.04
SSBOND 10 CYS B 649 CYS B 762 1555 1555 2.04
SSBOND 11 CYS C 391 CYS C 415 1555 1555 2.03
SSBOND 12 CYS C 433 CYS C 486 1555 1555 2.03
SSBOND 13 CYS C 445 CYS C 593 1555 1555 2.03
SSBOND 14 CYS C 510 CYS C 534 1555 1555 2.03
LINK ND2 ASN A 85 C1 NAG D 1 1555 1555 1.44
LINK ND2 ASN A 92 C1 NAG A 801 1555 1555 1.44
LINK ND2 ASN A 150 C1 NAG A 802 1555 1555 1.44
LINK ND2 ASN A 219 C1 NAG A 803 1555 1555 1.44
LINK ND2 ASN A 229 C1 NAG A 804 1555 1555 1.44
LINK ND2 ASN A 281 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN A 321 C1 NAG A 805 1555 1555 1.45
LINK ND2 ASN A 520 C1 NAG A 806 1555 1555 1.44
LINK ND2 ASN B 85 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN B 92 C1 NAG B 801 1555 1555 1.44
LINK ND2 ASN B 150 C1 NAG B 802 1555 1555 1.44
LINK ND2 ASN B 219 C1 NAG B 803 1555 1555 1.44
LINK ND2 ASN B 229 C1 NAG G 1 1555 1555 1.45
LINK ND2 ASN B 281 C1 NAG H 1 1555 1555 1.44
LINK ND2 ASN B 321 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN B 520 C1 NAG B 804 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 G 1 C1 NAG G 2 1555 1555 1.45
LINK O4 NAG G 2 C1 BMA G 3 1555 1555 1.45
LINK O3 BMA G 3 C1 MAN G 4 1555 1555 1.45
LINK O2 MAN G 4 C1 MAN G 5 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O6 NAG H 1 C1 FUC H 3 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
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 5943 PHE A 763
TER 11886 PHE B 763
TER 13492 MET C 595
MASTER 282 0 26 41 112 0 0 613840 3 395 136
END |