| 7e3d-pdb | HEADER HYDROLASE 08-FEB-21 7E3D
TITLE CRYSTAL STRUCTURE OF HUMAN ACETYLCHOLINESTERASE
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 7E3D 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
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 71166
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 3452
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 47.1500 - 7.3000 0.99 2995 148 0.1855 0.2321
REMARK 3 2 7.3000 - 5.8000 1.00 2818 156 0.1936 0.2271
REMARK 3 3 5.8000 - 5.0700 1.00 2836 109 0.1809 0.1744
REMARK 3 4 5.0700 - 4.6000 0.88 2480 131 0.1518 0.2090
REMARK 3 5 4.6000 - 4.2700 0.96 2649 157 0.1532 0.1983
REMARK 3 6 4.2700 - 4.0200 0.99 2675 153 0.1651 0.1711
REMARK 3 7 4.0200 - 3.8200 0.99 2767 155 0.1768 0.1931
REMARK 3 8 3.8200 - 3.6500 1.00 2747 126 0.1866 0.2210
REMARK 3 9 3.6500 - 3.5100 1.00 2750 126 0.2162 0.2545
REMARK 3 10 3.5100 - 3.3900 1.00 2729 129 0.2210 0.2410
REMARK 3 11 3.3900 - 3.2900 1.00 2780 117 0.2078 0.2876
REMARK 3 12 3.2900 - 3.1900 1.00 2715 138 0.2219 0.2602
REMARK 3 13 3.1900 - 3.1100 1.00 2758 131 0.2237 0.2962
REMARK 3 14 3.1100 - 3.0300 1.00 2730 130 0.2318 0.3176
REMARK 3 15 3.0300 - 2.9600 1.00 2764 133 0.2370 0.2897
REMARK 3 16 2.9600 - 2.9000 1.00 2708 124 0.2406 0.3261
REMARK 3 17 2.9000 - 2.8400 1.00 2686 137 0.2390 0.2703
REMARK 3 18 2.8400 - 2.7900 1.00 2728 160 0.2396 0.2935
REMARK 3 19 2.7900 - 2.7400 1.00 2754 126 0.2472 0.2702
REMARK 3 20 2.7400 - 2.6900 1.00 2624 166 0.2436 0.2751
REMARK 3 21 2.6900 - 2.6500 1.00 2725 184 0.2458 0.2617
REMARK 3 22 2.6500 - 2.6100 1.00 2703 107 0.2505 0.3107
REMARK 3 23 2.6100 - 2.5700 0.94 2518 162 0.2626 0.3662
REMARK 3 24 2.5700 - 2.5300 0.92 2504 127 0.2685 0.3328
REMARK 3 25 2.5300 - 2.5000 0.96 2571 120 0.2787 0.3219
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.74
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 : 2
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 4 THROUGH 17 OR RESID
REMARK 3 19 THROUGH 53 OR RESID 55 THROUGH 80 OR
REMARK 3 (RESID 81 AND (NAME N OR NAME CA OR NAME
REMARK 3 C OR NAME O OR NAME CB )) OR RESID 82
REMARK 3 THROUGH 249 OR RESID 251 THROUGH 312 OR
REMARK 3 RESID 314 THROUGH 492 OR RESID 498
REMARK 3 THROUGH 524 OR RESID 526 THROUGH 542))
REMARK 3 SELECTION : (CHAIN B AND ((RESID 4 AND (NAME N OR
REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB ))
REMARK 3 OR RESID 5 THROUGH 17 OR RESID 19 THROUGH
REMARK 3 53 OR RESID 55 THROUGH 164 OR (RESID 165
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB )) OR RESID 166 THROUGH 249
REMARK 3 OR RESID 251 THROUGH 258 OR RESID 265
REMARK 3 THROUGH 312 OR RESID 314 THROUGH 492 OR
REMARK 3 RESID 498 THROUGH 524 OR RESID 526
REMARK 3 THROUGH 542))
REMARK 3 ATOM PAIRS NUMBER : 3158
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN C
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 42
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7E3D 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_1300020700.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-SEP-20
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 : SLS
REMARK 200 BEAMLINE : X06SA
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71274
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 47.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.13700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.70300
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: 4EY4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.33
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 107.52200
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 215.04400
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 215.04400
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 107.52200
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: 3710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 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 495
REMARK 465 LYS A 496
REMARK 465 ALA A 497
REMARK 465 THR A 543
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ARG B 493
REMARK 465 ASP B 494
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 ARG A 165 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 491 CG CD OE1 OE2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 23 CE NZ
REMARK 470 GLU B 81 CG CD OE1 OE2
REMARK 470 GLU B 491 CG CD OE1 OE2
REMARK 470 LYS B 496 CG CD CE NZ
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 VAL A 10 CG1 - CB - CG2 ANGL. DEV. = 13.1 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 ALA A 62 51.42 -109.92
REMARK 500 SER A 203 -127.71 50.71
REMARK 500 ASP A 306 -88.96 -86.90
REMARK 500 HIS A 387 58.48 -145.06
REMARK 500 VAL A 407 -60.37 -125.17
REMARK 500 ALA B 62 60.40 -101.90
REMARK 500 SER B 203 -130.19 52.93
REMARK 500 ASP B 306 -89.87 -88.26
REMARK 500 HIS B 387 57.95 -145.17
REMARK 500 VAL B 407 -65.08 -124.84
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7E3D A 4 543 UNP P22303 ACES_HUMAN 35 574
DBREF 7E3D 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 PE8 B 601 25
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FUC ALPHA-L-FUCOPYRANOSE
HETNAM PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL
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 PE8 C16 H34 O9
FORMUL 6 HOH *108(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 MET A 241 VAL A 255 1 15
HELIX 12 AB3 ASP A 266 ARG A 276 1 11
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 ALA A 318 1 8
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 ARG A 534 ALA A 542 1 9
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 ASN B 265 THR B 275 1 11
HELIX 39 AE3 PRO B 277 GLU B 285 1 9
HELIX 40 AE4 TRP B 286 LEU B 289 5 4
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 ARG B 534 ALA B 542 1 9
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 THR A 198 N VAL A 114
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 PHE A 430 N VAL A 330
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 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 145
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 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 2.08
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.05
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.03
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.05
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK ND2 ASN A 350 C1 NAG C 1 1555 1555 1.47
LINK ND2 ASN B 350 C1 NAG D 1 1555 1555 1.46
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.47
LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.47
LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 -1.87
CISPEP 2 TYR B 105 PRO B 106 0 -1.91
CISPEP 3 CYS B 257 PRO B 258 0 -10.78
CRYST1 104.931 104.931 322.566 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 0.009530 0.005502 0.000000 0.00000
SCALE2 0.000000 0.011004 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003100 0.00000
TER 4160 ALA A 542
TER 8321 ALA B 542
MASTER 334 0 7 52 34 0 0 6 8459 2 115 84
END
|
|---|
