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HEADER HYDROLASE 08-FEB-21 7E3H
TITLE CRYSTAL STRUCTURE OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH
TITLE 2 DONEPEZIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 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: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS HUMAN ACETYLCHOLINESTERASE, HACHE, ALZHEIMER'S DISEASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.V.DILEEP,K.IHARA,C.MISHIMA-TSUMAGARI,M.KUKIMOTO-NIINO,M.YONEMOCHI,
AUTHOR 2 K.HANADA,M.SHIROUZU,K.Y.J.ZHANG
REVDAT 1 16-FEB-22 7E3H 0
JRNL AUTH K.V.DILEEP,K.IHARA,C.MISHIMA-TSUMAGARI,M.KUKIMOTO-NIINO,
JRNL AUTH 2 M.YONEMOCHI,K.HANADA,M.SHIROUZU,K.Y.J.ZHANG
JRNL TITL CRYSTAL STRUCTURE OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX
JRNL TITL 2 WITH DONEPEZIL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 76908
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3872
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 47.2000 - 7.4300 1.00 2847 167 0.1719 0.1778
REMARK 3 2 7.4300 - 5.9000 1.00 2706 142 0.1766 0.2210
REMARK 3 3 5.9000 - 5.1600 1.00 2669 160 0.1772 0.2013
REMARK 3 4 5.1600 - 4.6900 1.00 2607 177 0.1549 0.1910
REMARK 3 5 4.6900 - 4.3500 1.00 2604 155 0.1448 0.1662
REMARK 3 6 4.3500 - 4.0900 1.00 2624 166 0.1608 0.1852
REMARK 3 7 4.0900 - 3.8900 1.00 2566 157 0.1683 0.1905
REMARK 3 8 3.8900 - 3.7200 1.00 2614 166 0.1829 0.2110
REMARK 3 9 3.7200 - 3.5800 1.00 2641 104 0.1968 0.2566
REMARK 3 10 3.5800 - 3.4500 1.00 2625 137 0.2077 0.2307
REMARK 3 11 3.4500 - 3.3500 1.00 2645 92 0.2113 0.2688
REMARK 3 12 3.3400 - 3.2500 1.00 2581 122 0.2218 0.2430
REMARK 3 13 3.2500 - 3.1600 1.00 2601 137 0.2271 0.2403
REMARK 3 14 3.1600 - 3.0900 1.00 2571 136 0.2260 0.2877
REMARK 3 15 3.0900 - 3.0200 1.00 2623 120 0.2326 0.2831
REMARK 3 16 3.0200 - 2.9500 1.00 2611 143 0.2237 0.2586
REMARK 3 17 2.9500 - 2.8900 1.00 2532 142 0.2255 0.2666
REMARK 3 18 2.8900 - 2.8400 1.00 2583 124 0.2199 0.2841
REMARK 3 19 2.8400 - 2.7900 1.00 2620 151 0.2277 0.3278
REMARK 3 20 2.7900 - 2.7400 1.00 2620 101 0.2245 0.2498
REMARK 3 21 2.7400 - 2.7000 1.00 2527 139 0.2242 0.2954
REMARK 3 22 2.7000 - 2.6600 1.00 2601 147 0.2247 0.2945
REMARK 3 23 2.6600 - 2.6200 1.00 2560 134 0.2198 0.2677
REMARK 3 24 2.6200 - 2.5800 1.00 2552 157 0.2301 0.2755
REMARK 3 25 2.5800 - 2.5400 1.00 2578 134 0.2247 0.2561
REMARK 3 26 2.5400 - 2.5100 1.00 2567 113 0.2380 0.2963
REMARK 3 27 2.5100 - 2.4800 1.00 2595 127 0.2370 0.2938
REMARK 3 28 2.4800 - 2.4500 1.00 2566 122 0.2498 0.2848
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.010
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.22
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 7E3H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-21.
REMARK 100 THE DEPOSITION ID IS D_1300020699.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0 - 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77020
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 47.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 22.20
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 22.60
REMARK 200 R MERGE FOR SHELL (I) : 0.95400
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 1.17.1-3600
REMARK 200 STARTING MODEL: 4EY7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS HCL BUFFER PH 9.0, 20 %
REMARK 280 PEG 3350, 200 MM KNO3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 107.38333
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 214.76667
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 214.76667
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 107.38333
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 THR A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 PRO A 492
REMARK 465 ARG A 493
REMARK 465 ASP A 494
REMARK 465 PRO A 495
REMARK 465 LYS A 496
REMARK 465 ALA A 497
REMARK 465 THR A 543
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 PRO B 492
REMARK 465 ARG B 493
REMARK 465 ASP B 494
REMARK 465 PRO B 495
REMARK 465 LYS B 496
REMARK 465 ALA B 497
REMARK 465 THR B 543
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 23 NZ
REMARK 470 ARG A 165 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 268 CG CD OE1 OE2
REMARK 470 GLU A 491 CG CD OE1 OE2
REMARK 470 GLU B 4 CG CD OE1 OE2
REMARK 470 GLU B 51 CG CD OE1 OE2
REMARK 470 GLU B 468 CG CD OE1 OE2
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 SER A 203 -120.51 53.02
REMARK 500 ASP A 306 -90.23 -97.33
REMARK 500 HIS A 387 57.94 -141.26
REMARK 500 VAL A 407 -66.51 -125.33
REMARK 500 ASN A 464 51.14 -114.03
REMARK 500 PRO B 25 -19.47 -49.74
REMARK 500 PHE B 47 -1.45 72.45
REMARK 500 ALA B 62 56.14 -105.44
REMARK 500 SER B 203 -119.62 54.00
REMARK 500 ASP B 306 -90.45 -95.76
REMARK 500 VAL B 407 -63.92 -125.39
REMARK 500 ASN B 464 50.23 -114.51
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7E3H A 4 543 UNP P22303 ACES_HUMAN 35 574
DBREF 7E3H B 4 543 UNP P22303 ACES_HUMAN 35 574
SEQRES 1 A 540 GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG
SEQRES 2 A 540 LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL
SEQRES 3 A 540 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET
SEQRES 4 A 540 GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO
SEQRES 5 A 540 TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL
SEQRES 6 A 540 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 A 540 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 A 540 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 A 540 PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY
SEQRES 10 A 540 GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR
SEQRES 11 A 540 ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU
SEQRES 12 A 540 VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 A 540 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 A 540 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 A 540 ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR
SEQRES 16 A 540 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 A 540 HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG
SEQRES 18 A 540 ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA
SEQRES 19 A 540 THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN
SEQRES 20 A 540 LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY
SEQRES 21 A 540 GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG
SEQRES 22 A 540 PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU
SEQRES 23 A 540 PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 A 540 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 A 540 ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL
SEQRES 26 A 540 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 A 540 GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 A 540 SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL
SEQRES 29 A 540 PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 A 540 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG
SEQRES 31 A 540 LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN
SEQRES 32 A 540 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 A 540 ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS
SEQRES 34 A 540 ARG ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL
SEQRES 35 A 540 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO
SEQRES 36 A 540 LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE
SEQRES 37 A 540 PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA
SEQRES 38 A 540 ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA
SEQRES 39 A 540 PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR
SEQRES 40 A 540 VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 A 540 LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 A 540 PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 540 GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG
SEQRES 2 B 540 LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL
SEQRES 3 B 540 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET
SEQRES 4 B 540 GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO
SEQRES 5 B 540 TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL
SEQRES 6 B 540 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 7 B 540 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 8 B 540 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 9 B 540 PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY
SEQRES 10 B 540 GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR
SEQRES 11 B 540 ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU
SEQRES 12 B 540 VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 13 B 540 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 14 B 540 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 15 B 540 ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR
SEQRES 16 B 540 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 17 B 540 HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG
SEQRES 18 B 540 ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA
SEQRES 19 B 540 THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN
SEQRES 20 B 540 LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY
SEQRES 21 B 540 GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG
SEQRES 22 B 540 PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU
SEQRES 23 B 540 PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 24 B 540 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 25 B 540 ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL
SEQRES 26 B 540 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 27 B 540 GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 28 B 540 SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL
SEQRES 29 B 540 PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 30 B 540 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG
SEQRES 31 B 540 LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN
SEQRES 32 B 540 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 33 B 540 ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS
SEQRES 34 B 540 ARG ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL
SEQRES 35 B 540 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO
SEQRES 36 B 540 LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE
SEQRES 37 B 540 PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA
SEQRES 38 B 540 ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA
SEQRES 39 B 540 PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR
SEQRES 40 B 540 VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY
SEQRES 41 B 540 LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 42 B 540 PRO LYS LEU LEU SER ALA THR
HET NAG C 1 14
HET NAG C 2 14
HET FUC C 3 10
HET NAG D 1 14
HET NAG D 2 14
HET FUC D 3 10
HET E20 A 601 28
HET E20 B 601 28
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM E20 1-BENZYL-4-[(5,6-DIMETHOXY-1-INDANON-2-YL)
HETNAM 2 E20 METHYL]PIPERIDINE
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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-
HETSYN 2 FUC FUCOSE; FUCOSE
HETSYN E20 E2020
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 5 E20 2(C24 H29 N O3)
FORMUL 7 HOH *57(H2 O)
HELIX 1 AA1 ASP A 5 GLU A 7 5 3
HELIX 2 AA2 MET A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 ARG A 143 1 9
HELIX 6 AA6 VAL A 153 LEU A 159 1 7
HELIX 7 AA7 ASN A 170 VAL A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SER A 203 LEU A 214 1 12
HELIX 10 AB1 SER A 215 GLY A 220 1 6
HELIX 11 AB2 GLY A 240 VAL A 255 1 16
HELIX 12 AB3 ASP A 266 THR A 275 1 10
HELIX 13 AB4 PRO A 277 GLU A 285 1 9
HELIX 14 AB5 TRP A 286 LEU A 289 5 4
HELIX 15 AB6 THR A 311 GLY A 319 1 9
HELIX 16 AB7 GLY A 335 VAL A 340 1 6
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASP A 460 5 5
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 PHE A 535 ALA A 542 1 8
HELIX 27 AC9 ASP B 5 GLU B 7 5 3
HELIX 28 AD1 MET B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 ARG B 143 1 9
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 VAL B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SER B 203 LEU B 214 1 12
HELIX 36 AD9 SER B 215 GLY B 220 1 6
HELIX 37 AE1 MET B 241 VAL B 255 1 15
HELIX 38 AE2 ASP B 266 THR B 275 1 10
HELIX 39 AE3 PRO B 277 HIS B 284 1 8
HELIX 40 AE4 GLU B 285 LEU B 289 5 5
HELIX 41 AE5 THR B 311 ALA B 318 1 8
HELIX 42 AE6 GLY B 335 VAL B 340 1 6
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 THR B 383 1 13
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 GLN B 421 1 15
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASP B 460 5 5
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 PHE B 535 ALA B 542 1 8
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 AA211 ILE A 20 LEU A 22 0
SHEET 2 AA211 VAL A 29 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 AA211 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O TYR A 426 N VAL A 328
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N VAL A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 3 LEU B 9 VAL B 12 0
SHEET 2 AA4 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 16
SHEET 1 AA511 ILE B 20 LEU B 22 0
SHEET 2 AA511 VAL B 29 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
SHEET 4 AA511 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA511 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O THR B 198 N VAL B 114
SHEET 7 AA511 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA511 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ARG B 424 PHE B 430 1 O TYR B 426 N VAL B 328
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 68 CYS B 69 0
SHEET 2 AA6 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 AA7 2 VAL B 239 GLY B 240 0
SHEET 2 AA7 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.03
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.08
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.05
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.12
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.07
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK ND2 ASN A 350 C1 NAG C 1 1555 1555 1.46
LINK ND2 ASN B 350 C1 NAG D 1 1555 1555 1.48
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.46
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.48
LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 -0.70
CISPEP 2 TYR B 105 PRO B 106 0 -3.31
CISPEP 3 CYS B 257 PRO B 258 0 -18.25
CRYST1 105.105 105.105 322.150 90.00 90.00 120.00 P 31 2 1 12
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 0.009514 0.005493 0.000000 0.00000
SCALE2 0.000000 0.010986 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003104 0.00000
TER 4138 ALA A 542
TER 8250 ALA B 542
MASTER 303 0 8 52 34 0 0 6 8370 2 146 84
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