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HEADER HYDROLASE 14-OCT-20 7D9P
TITLE CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE IN COMPLEX
TITLE 2 WITH COMPOUND 12
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
KEYWDS ACHE INHIBITOR, COMPLEX STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.F.LIU,W.C.YIN
REVDAT 1 25-AUG-21 7D9P 0
JRNL AUTH Y.ZHOU,Y.FU,W.YIN,J.LI,W.WANG,F.BAI,S.XU,Q.GONG,T.PENG,
JRNL AUTH 2 Y.HONG,D.ZHANG,D.ZHANG,Q.LIU,Y.XU,H.E.XU,H.ZHANG,H.JIANG,
JRNL AUTH 3 H.LIU
JRNL TITL KINETICS-DRIVEN DRUG DESIGN STRATEGY FOR NEXT-GENERATION
JRNL TITL 2 ACETYLCHOLINESTERASE INHIBITORS TO CLINICAL CANDIDATE.
JRNL REF J.MED.CHEM. V. 64 1844 2021
JRNL REFN ISSN 0022-2623
JRNL PMID 33570950
JRNL DOI 10.1021/ACS.JMEDCHEM.0C01863
REMARK 2
REMARK 2 RESOLUTION. 2.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX V1.18.2
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) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 45742
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2301
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 35.9600 - 7.1700 0.93 2962 132 0.1689 0.1721
REMARK 3 2 7.1700 - 5.7000 1.00 2991 154 0.1753 0.1791
REMARK 3 3 5.7000 - 4.9800 1.00 2964 158 0.1600 0.1869
REMARK 3 4 4.9800 - 4.5300 1.00 2940 147 0.1386 0.1908
REMARK 3 5 4.5200 - 4.2000 1.00 2911 145 0.1429 0.1692
REMARK 3 6 4.2000 - 3.9500 1.00 2894 185 0.1583 0.2115
REMARK 3 7 3.9500 - 3.7600 1.00 2923 149 0.1641 0.2158
REMARK 3 8 3.7600 - 3.5900 1.00 2937 147 0.1782 0.2147
REMARK 3 9 3.5900 - 3.4500 1.00 2866 180 0.2028 0.2764
REMARK 3 10 3.4500 - 3.3400 1.00 2917 116 0.2078 0.2638
REMARK 3 11 3.3400 - 3.2300 1.00 2868 152 0.2260 0.2373
REMARK 3 12 3.2300 - 3.1400 0.99 2849 160 0.2353 0.3064
REMARK 3 13 3.1400 - 3.0600 0.90 2608 158 0.2476 0.3165
REMARK 3 14 3.0600 - 2.9800 0.84 2352 137 0.2534 0.3195
REMARK 3 15 2.9800 - 2.9100 0.67 1905 102 0.2484 0.3224
REMARK 3 16 2.9100 - 2.8500 0.53 1554 79 0.2594 0.3282
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.60
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 7D9P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1300019001.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49281
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 17.30
REMARK 200 R MERGE (I) : 0.24400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : 1.02700
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 2.8.3
REMARK 200 STARTING MODEL: 4EY7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16-0.22M POTASSIUM NITRATE, 16-20%
REMARK 280 POLYETHYLENE GLYCOL (PEG) 3350, VAPOR DIFFUSION, TEMPERATURE 293K
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 107.87200
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 215.74400
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 215.74400
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 107.87200
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: 3620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLY A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 GLU A 1
REMARK 465 GLY A 2
REMARK 465 ARG A 3
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 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 GLY B -9
REMARK 465 SER B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
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 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 SER B 541
REMARK 465 ALA B 542
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 GLU A 4 CG CD OE1 OE2
REMARK 470 GLU A 91 CG CD OE1 OE2
REMARK 470 GLU A 313 CG CD OE1 OE2
REMARK 470 GLU A 389 CG CD OE1 OE2
REMARK 470 GLU A 468 CG CD OE1 OE2
REMARK 470 GLU B 4 CG CD OE1 OE2
REMARK 470 GLU B 51 CG CD OE1 OE2
REMARK 470 GLN B 54 CG CD OE1 NE2
REMARK 470 GLU B 81 CG CD OE1 OE2
REMARK 470 ARG B 143 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 166 CG CD OE1 OE2
REMARK 470 HIS B 253 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 313 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 67 152.32 -44.46
REMARK 500 ALA A 167 74.92 -152.86
REMARK 500 SER A 203 -121.30 56.43
REMARK 500 ASP A 306 -84.41 -87.24
REMARK 500 HIS A 387 56.23 -140.37
REMARK 500 VAL A 407 -57.52 -127.38
REMARK 500 SER A 462 20.97 -73.42
REMARK 500 ASN A 464 40.91 -99.09
REMARK 500 PHE B 47 -1.03 71.49
REMARK 500 PRO B 55 150.80 -49.39
REMARK 500 ALA B 62 74.65 -104.61
REMARK 500 ALA B 167 70.13 -151.77
REMARK 500 SER B 203 -124.23 50.62
REMARK 500 ASP B 306 -84.98 -94.14
REMARK 500 ASN B 350 -157.37 -117.48
REMARK 500 VAL B 367 77.52 -119.20
REMARK 500 VAL B 407 -66.67 -128.08
REMARK 500 ASN B 464 48.36 -104.81
REMARK 500 GLN B 508 58.79 34.26
REMARK 500 ARG B 525 57.49 39.82
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7D9P A 1 543 UNP P22303 ACES_HUMAN 32 574
DBREF 7D9P B 1 543 UNP P22303 ACES_HUMAN 32 574
SEQADV 7D9P GLY A -9 UNP P22303 EXPRESSION TAG
SEQADV 7D9P SER A -8 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS A -7 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS A -6 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS A -5 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS A -4 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS A -3 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS A -2 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS A -1 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS A 0 UNP P22303 EXPRESSION TAG
SEQADV 7D9P GLY B -9 UNP P22303 EXPRESSION TAG
SEQADV 7D9P SER B -8 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS B -7 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS B -6 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS B -5 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS B -4 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS B -3 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS B -2 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS B -1 UNP P22303 EXPRESSION TAG
SEQADV 7D9P HIS B 0 UNP P22303 EXPRESSION TAG
SEQRES 1 A 553 GLY SER HIS HIS HIS HIS HIS HIS HIS HIS GLU GLY ARG
SEQRES 2 A 553 GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG
SEQRES 3 A 553 LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL
SEQRES 4 A 553 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET
SEQRES 5 A 553 GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO
SEQRES 6 A 553 TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL
SEQRES 7 A 553 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 8 A 553 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 9 A 553 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 10 A 553 PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY
SEQRES 11 A 553 GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR
SEQRES 12 A 553 ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU
SEQRES 13 A 553 VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 14 A 553 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 15 A 553 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 16 A 553 ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR
SEQRES 17 A 553 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 18 A 553 HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG
SEQRES 19 A 553 ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA
SEQRES 20 A 553 THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN
SEQRES 21 A 553 LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY
SEQRES 22 A 553 GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG
SEQRES 23 A 553 PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU
SEQRES 24 A 553 PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 25 A 553 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 26 A 553 ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL
SEQRES 27 A 553 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 28 A 553 GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 29 A 553 SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL
SEQRES 30 A 553 PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 31 A 553 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG
SEQRES 32 A 553 LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN
SEQRES 33 A 553 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 34 A 553 ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS
SEQRES 35 A 553 ARG ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL
SEQRES 36 A 553 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO
SEQRES 37 A 553 LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE
SEQRES 38 A 553 PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA
SEQRES 39 A 553 ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA
SEQRES 40 A 553 PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR
SEQRES 41 A 553 VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY
SEQRES 42 A 553 LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 43 A 553 PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 553 GLY SER HIS HIS HIS HIS HIS HIS HIS HIS GLU GLY ARG
SEQRES 2 B 553 GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG
SEQRES 3 B 553 LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL
SEQRES 4 B 553 SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET
SEQRES 5 B 553 GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO
SEQRES 6 B 553 TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL
SEQRES 7 B 553 CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU
SEQRES 8 B 553 GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU
SEQRES 9 B 553 ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG
SEQRES 10 B 553 PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY
SEQRES 11 B 553 GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR
SEQRES 12 B 553 ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU
SEQRES 13 B 553 VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU
SEQRES 14 B 553 ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY
SEQRES 15 B 553 LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU
SEQRES 16 B 553 ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR
SEQRES 17 B 553 LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET
SEQRES 18 B 553 HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG
SEQRES 19 B 553 ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA
SEQRES 20 B 553 THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN
SEQRES 21 B 553 LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY
SEQRES 22 B 553 GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG
SEQRES 23 B 553 PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU
SEQRES 24 B 553 PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL
SEQRES 25 B 553 VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU
SEQRES 26 B 553 ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL
SEQRES 27 B 553 GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR
SEQRES 28 B 553 GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE
SEQRES 29 B 553 SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL
SEQRES 30 B 553 PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU
SEQRES 31 B 553 HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG
SEQRES 32 B 553 LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN
SEQRES 33 B 553 VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA
SEQRES 34 B 553 ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS
SEQRES 35 B 553 ARG ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL
SEQRES 36 B 553 PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO
SEQRES 37 B 553 LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE
SEQRES 38 B 553 PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA
SEQRES 39 B 553 ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA
SEQRES 40 B 553 PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR
SEQRES 41 B 553 VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY
SEQRES 42 B 553 LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU
SEQRES 43 B 553 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 H0R A 601 30
HET H0R B 601 30
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM H0R (2S)-2-[[4-FLUORANYL-1-[(2-FLUOROPHENYL)
HETNAM 2 H0R METHYL]PIPERIDIN-4-YL]METHYL]-5,6-DIMETHOXY-2,3-
HETNAM 3 H0R DIHYDROINDEN-1-ONE
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
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 5 H0R 2(C24 H27 F2 N O3)
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 MET A 241 VAL A 255 1 15
HELIX 12 AB3 ASP A 266 THR A 275 1 10
HELIX 13 AB4 PRO A 277 HIS A 284 1 8
HELIX 14 AB5 GLU A 285 LEU A 289 5 5
HELIX 15 AB6 THR A 311 ALA A 318 1 8
HELIX 16 AB7 GLY A 335 GLY A 342 5 8
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 ALA A 420 1 14
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 ARG A 534 SER A 541 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 GLY B 154 LEU B 159 1 6
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 ARG B 274 1 9
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 GLY B 319 1 9
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 ARG B 534 LEU B 540 1 7
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
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 THR A 24 0
SHEET 2 AA211 GLY A 27 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 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O THR A 198 N VAL A 114
SHEET 7 AA211 ARG A 224 GLN A 228 1 O ARG A 224 N LEU A 199
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 239 GLY A 240 0
SHEET 2 AA3 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
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 THR B 24 0
SHEET 2 AA511 GLY B 27 PRO B 36 -1 O ALA B 31 N ILE B 20
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 LEU B 146 N TRP B 102
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 ASP B 193 N THR B 112
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 PHE B 430 N VAL B 330
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 AA511 VAL B 520 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 239 GLY B 240 0
SHEET 2 AA6 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 2.06
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.06
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.06
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.06
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.07
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.06
LINK ND2 ASN A 350 C1 NAG C 1 1555 1555 1.42
LINK ND2 ASN B 350 C1 NAG D 1 1555 1555 1.41
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 -3.30
CISPEP 2 TYR B 105 PRO B 106 0 3.41
CRYST1 104.944 104.944 323.616 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 0.009529 0.005502 0.000000 0.00000
SCALE2 0.000000 0.011003 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003090 0.00000
TER 4127 ALA A 542
TER 8219 LEU B 540
MASTER 334 0 8 52 32 0 0 6 8292 2 150 86
END |