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HEADER HYDROLASE/HYDROLASE INHIBITOR 01-AUG-13 4M0E
TITLE STRUCTURE OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH
TITLE 2 DIHYDROTANSHINONE I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 33-574;
COMPND 5 SYNONYM: ACHE;
COMPND 6 EC: 3.1.1.7;
COMPND 7 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: HEK 293H;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PJT1 FAST DEST
KEYWDS ACETYLCHOLINESTERASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CHEUNG,E.N.GARY,K.SHIOMI,T.L.ROSENBERRY
REVDAT 1 16-OCT-13 4M0E 0
JRNL AUTH J.CHEUNG,E.N.GARY,K.SHIOMI,T.L.ROSENBERRY
JRNL TITL STRUCTURES OF HUMAN ACETYLCHOLINESTERASE BOUND TO
JRNL TITL 2 DIHYDROTANSHINONE I AND TERRITREM B SHOW PERIPHERAL SITE
JRNL TITL 3 FLEXIBILITY
JRNL REF ACS MED.CHEM.LETT 2013
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 139877
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 7058
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 45.0620 - 6.2092 0.98 4729 238 0.1738 0.2037
REMARK 3 2 6.2092 - 4.9304 1.00 4590 249 0.1481 0.1660
REMARK 3 3 4.9304 - 4.3077 1.00 4554 238 0.1168 0.1436
REMARK 3 4 4.3077 - 3.9141 1.00 4500 223 0.1262 0.1482
REMARK 3 5 3.9141 - 3.6337 1.00 4487 245 0.1389 0.1668
REMARK 3 6 3.6337 - 3.4196 1.00 4509 233 0.1533 0.1780
REMARK 3 7 3.4196 - 3.2484 1.00 4469 247 0.1550 0.1985
REMARK 3 8 3.2484 - 3.1070 1.00 4487 219 0.1620 0.2111
REMARK 3 9 3.1070 - 2.9874 1.00 4428 237 0.1624 0.1940
REMARK 3 10 2.9874 - 2.8843 1.00 4487 215 0.1588 0.1972
REMARK 3 11 2.8843 - 2.7942 1.00 4467 227 0.1543 0.2185
REMARK 3 12 2.7942 - 2.7143 1.00 4423 242 0.1580 0.2050
REMARK 3 13 2.7143 - 2.6429 1.00 4433 234 0.1588 0.2159
REMARK 3 14 2.6429 - 2.5784 1.00 4413 266 0.1610 0.2184
REMARK 3 15 2.5784 - 2.5198 1.00 4435 206 0.1581 0.2183
REMARK 3 16 2.5198 - 2.4662 1.00 4398 256 0.1633 0.1992
REMARK 3 17 2.4662 - 2.4168 1.00 4415 233 0.1685 0.2054
REMARK 3 18 2.4168 - 2.3712 1.00 4439 227 0.1772 0.2278
REMARK 3 19 2.3712 - 2.3289 1.00 4360 247 0.1769 0.2161
REMARK 3 20 2.3289 - 2.2894 1.00 4402 254 0.1768 0.2113
REMARK 3 21 2.2894 - 2.2525 1.00 4447 218 0.1818 0.2190
REMARK 3 22 2.2525 - 2.2178 1.00 4393 248 0.1811 0.2097
REMARK 3 23 2.2178 - 2.1852 1.00 4376 238 0.1888 0.2430
REMARK 3 24 2.1852 - 2.1544 1.00 4406 225 0.2066 0.2543
REMARK 3 25 2.1544 - 2.1253 1.00 4453 219 0.2166 0.2583
REMARK 3 26 2.1253 - 2.0977 1.00 4354 236 0.2253 0.2617
REMARK 3 27 2.0977 - 2.0715 0.98 4287 238 0.2317 0.2699
REMARK 3 28 2.0715 - 2.0465 0.97 4274 245 0.2420 0.2752
REMARK 3 29 2.0465 - 2.0227 0.96 4169 217 0.2589 0.2915
REMARK 3 30 2.0227 - 2.0000 0.96 4235 238 0.2743 0.2867
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.61
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 : 0.012 8923
REMARK 3 ANGLE : 1.349 12214
REMARK 3 CHIRALITY : 0.095 1306
REMARK 3 PLANARITY : 0.007 1612
REMARK 3 DIHEDRAL : 13.367 3201
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 4M0E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-13.
REMARK 100 THE RCSB ID CODE IS RCSB081307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 140295
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.58700
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
REMARK 200 STARTING MODEL: PDB ENTRY 4EY4
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: 12 TO 18% PEG 3350, 0.2M POTASSIUM
REMARK 280 NITRATE, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 107.86233
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 215.72467
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 215.72467
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 107.86233
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: 4880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 GLY A 2
REMARK 465 ARG A 3
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 THR A 543
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 ARG B 493
REMARK 465 ASP B 494
REMARK 465 THR B 543
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 O HOH A 912 O HOH A 1004 2.08
REMARK 500 O HOH A 1025 O HOH A 1296 2.10
REMARK 500 O HOH A 920 O HOH A 1248 2.11
REMARK 500 O HOH B 895 O HOH B 1281 2.11
REMARK 500 O HOH B 954 O HOH B 1144 2.11
REMARK 500 OD1 ASP B 304 O HOH B 768 2.11
REMARK 500 ND2 ASN A 350 O5 NAG A 602 2.14
REMARK 500 O HOH B 761 O HOH B 888 2.18
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 PHE A 47 -8.04 72.89
REMARK 500 ALA A 62 51.55 -108.45
REMARK 500 SER A 203 -121.84 57.74
REMARK 500 ASP A 306 -87.89 -93.80
REMARK 500 VAL A 407 -64.25 -126.46
REMARK 500 PRO A 498 161.04 -49.49
REMARK 500 PHE B 47 -8.50 80.51
REMARK 500 ALA B 167 76.35 -151.45
REMARK 500 ASN B 170 13.85 57.73
REMARK 500 SER B 203 -120.69 55.22
REMARK 500 ASP B 306 -86.02 -97.49
REMARK 500 VAL B 407 -61.07 -129.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1284 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH B 948 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH B1131 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH B1176 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH B1199 DISTANCE = 7.09 ANGSTROMS
REMARK 525 HOH B1258 DISTANCE = 7.69 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1YL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1YL B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A
REMARK 800 350 RESIDUES 601 TO 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 604 BOUND
REMARK 800 TO ASN B 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B
REMARK 800 350 RESIDUES 601 TO 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4M0F RELATED DB: PDB
DBREF 4M0E A 2 543 UNP P22303 ACES_HUMAN 33 574
DBREF 4M0E B 2 543 UNP P22303 ACES_HUMAN 33 574
SEQRES 1 A 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 A 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 A 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 A 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 A 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 A 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 A 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 A 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 A 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 A 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 A 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 A 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 A 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 A 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 A 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 A 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 A 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 A 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 A 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 A 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 A 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 A 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 A 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 A 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 A 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 A 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 A 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 A 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 A 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 A 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 A 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 A 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 A 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 A 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 A 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 A 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 A 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 A 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 A 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 A 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 A 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 A 542 PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 542 GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY
SEQRES 2 B 542 GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY
SEQRES 3 B 542 PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO
SEQRES 4 B 542 PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS
SEQRES 5 B 542 GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN
SEQRES 6 B 542 SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY
SEQRES 7 B 542 PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU
SEQRES 8 B 542 SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR
SEQRES 9 B 542 PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE
SEQRES 10 B 542 TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP
SEQRES 11 B 542 VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR
SEQRES 12 B 542 VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY
SEQRES 13 B 542 PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN
SEQRES 14 B 542 VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL
SEQRES 15 B 542 GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER
SEQRES 16 B 542 VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL
SEQRES 17 B 542 GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE
SEQRES 18 B 542 HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO
SEQRES 19 B 542 TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA
SEQRES 20 B 542 THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY
SEQRES 21 B 542 THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG
SEQRES 22 B 542 THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS
SEQRES 23 B 542 VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL
SEQRES 24 B 542 PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU
SEQRES 25 B 542 ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL
SEQRES 26 B 542 LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU
SEQRES 27 B 542 VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER
SEQRES 28 B 542 LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL
SEQRES 29 B 542 GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL
SEQRES 30 B 542 VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO
SEQRES 31 B 542 ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP
SEQRES 32 B 542 HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG
SEQRES 33 B 542 LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE
SEQRES 34 B 542 GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET
SEQRES 35 B 542 GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY
SEQRES 36 B 542 ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU
SEQRES 37 B 542 LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN
SEQRES 38 B 542 PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO
SEQRES 39 B 542 LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN
SEQRES 40 B 542 GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG
SEQRES 41 B 542 ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG
SEQRES 42 B 542 PHE LEU PRO LYS LEU LEU SER ALA THR
MODRES 4M0E ASN B 350 ASN GLYCOSYLATION SITE
MODRES 4M0E ASN A 350 ASN GLYCOSYLATION SITE
MODRES 4M0E ASN B 265 ASN GLYCOSYLATION SITE
HET FUC A 601 10
HET NAG A 602 14
HET NAG A 603 14
HET 1YL A 604 21
HET EDO A 605 4
HET EDO A 606 4
HET FUC B 601 10
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET 1YL B 605 21
HET EDO B 606 4
HET NO3 B 607 4
HET NO3 B 608 4
HETNAM FUC ALPHA-L-FUCOSE
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM 1YL DIHYDROTANSHINONE I
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NO3 NITRATE ION
HETSYN 1YL (1R)-1,6-DIMETHYL-1,2-DIHYDROPHENANTHRO[1,2-B]FURAN-10,
HETSYN 2 1YL 11-DIONE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 3 NAG 5(C8 H15 N O6)
FORMUL 4 1YL 2(C18 H14 O3)
FORMUL 5 EDO 3(C2 H6 O2)
FORMUL 11 NO3 2(N O3 1-)
FORMUL 13 HOH *1254(H2 O)
HELIX 1 1 ASP A 5 GLU A 7 5 3
HELIX 2 2 MET A 42 ARG A 46 5 5
HELIX 3 3 PHE A 80 MET A 85 1 6
HELIX 4 4 LEU A 130 ASP A 134 5 5
HELIX 5 5 GLY A 135 ARG A 143 1 9
HELIX 6 6 VAL A 153 LEU A 159 1 7
HELIX 7 7 ASN A 170 VAL A 187 1 18
HELIX 8 8 ALA A 188 PHE A 190 5 3
HELIX 9 9 SER A 203 LEU A 214 1 12
HELIX 10 10 SER A 215 GLY A 220 1 6
HELIX 11 11 MET A 241 VAL A 255 1 15
HELIX 12 12 ASP A 266 ARG A 276 1 11
HELIX 13 13 PRO A 277 GLU A 285 1 9
HELIX 14 14 TRP A 286 LEU A 289 5 4
HELIX 15 15 THR A 311 GLY A 319 1 9
HELIX 16 16 GLY A 335 VAL A 340 1 6
HELIX 17 17 SER A 355 VAL A 367 1 13
HELIX 18 18 SER A 371 THR A 383 1 13
HELIX 19 19 ASP A 390 VAL A 407 1 18
HELIX 20 20 VAL A 407 GLN A 421 1 15
HELIX 21 21 PRO A 440 GLY A 444 5 5
HELIX 22 22 GLU A 450 PHE A 455 1 6
HELIX 23 23 GLY A 456 ASP A 460 5 5
HELIX 24 24 THR A 466 GLY A 487 1 22
HELIX 25 25 ARG A 525 ARG A 534 1 10
HELIX 26 26 PHE A 535 ALA A 542 1 8
HELIX 27 27 ASP B 5 GLU B 7 5 3
HELIX 28 28 MET B 42 ARG B 46 5 5
HELIX 29 29 PHE B 80 MET B 85 1 6
HELIX 30 30 LEU B 130 ASP B 134 5 5
HELIX 31 31 GLY B 135 ARG B 143 1 9
HELIX 32 32 VAL B 153 LEU B 159 1 7
HELIX 33 33 ASN B 170 VAL B 187 1 18
HELIX 34 34 ALA B 188 PHE B 190 5 3
HELIX 35 35 SER B 203 LEU B 214 1 12
HELIX 36 36 SER B 215 GLY B 220 1 6
HELIX 37 37 MET B 241 VAL B 255 1 15
HELIX 38 38 ASN B 265 ARG B 274 1 10
HELIX 39 39 PRO B 277 GLU B 285 1 9
HELIX 40 40 TRP B 286 LEU B 289 5 4
HELIX 41 41 THR B 311 GLY B 319 1 9
HELIX 42 42 GLY B 335 VAL B 340 1 6
HELIX 43 43 SER B 355 VAL B 367 1 13
HELIX 44 44 SER B 371 THR B 383 1 13
HELIX 45 45 ASP B 390 VAL B 407 1 18
HELIX 46 46 VAL B 407 GLN B 421 1 15
HELIX 47 47 PRO B 440 GLY B 444 5 5
HELIX 48 48 GLU B 450 PHE B 455 1 6
HELIX 49 49 GLY B 456 ASP B 460 5 5
HELIX 50 50 THR B 466 GLY B 487 1 22
HELIX 51 51 ARG B 525 ARG B 534 1 10
HELIX 52 52 PHE B 535 ALA B 542 1 8
SHEET 1 A 3 LEU A 9 VAL A 12 0
SHEET 2 A 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 A 3 VAL A 59 ASP A 61 1 O VAL A 60 N ARG A 16
SHEET 1 B11 ILE A 20 LEU A 22 0
SHEET 2 B11 VAL A 29 PRO A 36 -1 O VAL A 29 N LEU A 22
SHEET 3 B11 TYR A 98 PRO A 104 -1 O VAL A 101 N PHE A 32
SHEET 4 B11 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 B11 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 B11 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 B11 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 B11 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 B11 ARG A 424 PHE A 430 1 O TYR A 426 N VAL A 328
SHEET 10 B11 GLN A 509 LEU A 513 1 O LEU A 513 N VAL A 429
SHEET 11 B11 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 C 2 VAL A 68 CYS A 69 0
SHEET 2 C 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 D 2 VAL A 239 GLY A 240 0
SHEET 2 D 2 VAL A 302 VAL A 303 1 O VAL A 303 N VAL A 239
SHEET 1 E 3 LEU B 9 VAL B 12 0
SHEET 2 E 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 E 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 16
SHEET 1 F11 ILE B 20 LEU B 22 0
SHEET 2 F11 VAL B 29 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 F11 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 4 F11 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 F11 THR B 112 ILE B 118 1 N LEU B 115 O VAL B 145
SHEET 6 F11 GLY B 192 GLU B 202 1 O ASP B 193 N THR B 112
SHEET 7 F11 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 F11 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 F11 ARG B 424 PHE B 430 1 O TYR B 426 N VAL B 328
SHEET 10 F11 GLN B 509 LEU B 513 1 O LEU B 513 N VAL B 429
SHEET 11 F11 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 G 2 VAL B 68 CYS B 69 0
SHEET 2 G 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 H 2 VAL B 239 GLY B 240 0
SHEET 2 H 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 2.10
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.10
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.10
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.09
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK O4 NAG A 602 C1 NAG A 603 1555 1555 1.43
LINK C1 FUC B 601 O6 NAG B 602 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B 602 1555 1555 1.45
LINK ND2 ASN A 350 C1 NAG A 602 1555 1555 1.45
LINK C1 FUC A 601 O6 NAG A 602 1555 1555 1.46
LINK O4 NAG B 602 C1 NAG B 603 1555 1555 1.51
LINK ND2 ASN B 265 C1 NAG B 604 1555 1555 1.59
CISPEP 1 TYR A 105 PRO A 106 0 -1.86
CISPEP 2 CYS A 257 PRO A 258 0 -2.92
CISPEP 3 ALA A 497 PRO A 498 0 -0.10
CISPEP 4 TYR B 105 PRO B 106 0 2.63
CISPEP 5 CYS B 257 PRO B 258 0 -3.29
SITE 1 AC1 11 TYR A 72 ASP A 74 TYR A 124 TRP A 286
SITE 2 AC1 11 SER A 293 VAL A 294 PHE A 295 TYR A 337
SITE 3 AC1 11 PHE A 338 TYR A 341 HOH A 715
SITE 1 AC2 8 TYR A 382 ASP A 384 HIS A 387 PRO A 388
SITE 2 AC2 8 ARG A 393 LEU A 394 ALA A 397 HOH A 745
SITE 1 AC3 7 GLN A 508 ALA A 526 ALA A 530 ARG A 534
SITE 2 AC3 7 HOH A 814 HOH A 818 HOH B 812
SITE 1 AC4 12 TYR B 72 ASP B 74 TYR B 124 TRP B 286
SITE 2 AC4 12 SER B 293 VAL B 294 PHE B 295 PHE B 297
SITE 3 AC4 12 TYR B 337 PHE B 338 TYR B 341 HOH B 713
SITE 1 AC5 9 TYR B 382 THR B 383 ASP B 384 HIS B 387
SITE 2 AC5 9 PRO B 388 ARG B 393 LEU B 394 ALA B 397
SITE 3 AC5 9 HOH B 796
SITE 1 AC6 8 VAL A 255 VAL A 280 HIS A 284 HOH A 951
SITE 2 AC6 8 PRO B 162 MET B 241 GLY B 242 ARG B 245
SITE 1 AC7 5 HOH A 746 ALA B 526 ALA B 530 ARG B 534
SITE 2 AC7 5 HOH B 814
SITE 1 AC8 8 PRO A 344 GLY A 345 SER A 347 ASN A 350
SITE 2 AC8 8 HOH A 849 HOH A1077 HOH A1183 HOH A1348
SITE 1 AC9 3 ASN B 265 GLU B 268 HOH B1241
SITE 1 BC1 7 PRO B 344 GLY B 345 SER B 347 ASN B 350
SITE 2 BC1 7 HOH B 900 HOH B1097 HOH B1263
CRYST1 105.063 105.063 323.587 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 0.009518 0.005495 0.000000 0.00000
SCALE2 0.000000 0.010991 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003090 0.00000
TER 4244 ALA A 542
TER 8480 ALA B 542
MASTER 363 0 14 52 36 0 22 6 9710 2 167 84
END |