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HEADER HYDROLASE 23-NOV-17 6F25
TITLE CRYSTAL STRUCTURE OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH C35.
CAVEAT 6F25 FUC A 603 HAS WRONG CHIRALITY AT ATOM C1 FUC B 603 HAS WRONG
CAVEAT 2 6F25 CHIRALITY AT ATOM C1
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: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS ACETYLCHOLINESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.DIAS,F.NACHON
REVDAT 1 12-DEC-18 6F25 0
JRNL AUTH J.DIAS,F.NACHON
JRNL TITL CRYSTAL STRUCTURE OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX
JRNL TITL 2 WITH C35.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.338
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 55159
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.978
REMARK 3 FREE R VALUE TEST SET COUNT : 2746
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 48.8951 - 8.2717 1.00 2744 118 0.1800 0.1919
REMARK 3 2 8.2717 - 6.5705 1.00 2705 143 0.1657 0.2088
REMARK 3 3 6.5705 - 5.7414 1.00 2686 125 0.1668 0.1970
REMARK 3 4 5.7414 - 5.2171 1.00 2635 152 0.1542 0.1666
REMARK 3 5 5.2171 - 4.8436 1.00 2646 158 0.1359 0.1609
REMARK 3 6 4.8436 - 4.5582 1.00 2665 125 0.1284 0.1543
REMARK 3 7 4.5582 - 4.3301 1.00 2677 135 0.1312 0.1695
REMARK 3 8 4.3301 - 4.1417 1.00 2631 132 0.1417 0.1875
REMARK 3 9 4.1417 - 3.9823 1.00 2660 129 0.1476 0.1781
REMARK 3 10 3.9823 - 3.8450 1.00 2671 142 0.1604 0.2049
REMARK 3 11 3.8450 - 3.7248 1.00 2634 135 0.1688 0.2369
REMARK 3 12 3.7248 - 3.6183 1.00 2631 167 0.1816 0.2415
REMARK 3 13 3.6183 - 3.5231 1.00 2667 115 0.2059 0.2343
REMARK 3 14 3.5231 - 3.4372 1.00 2612 156 0.2323 0.2944
REMARK 3 15 3.4372 - 3.3591 1.00 2652 137 0.2429 0.2634
REMARK 3 16 3.3591 - 3.2876 1.00 2624 147 0.2518 0.3086
REMARK 3 17 3.2876 - 3.2218 1.00 2625 142 0.2764 0.3401
REMARK 3 18 3.2218 - 3.1611 0.97 2564 146 0.3066 0.3294
REMARK 3 19 3.1611 - 3.1046 0.93 2434 125 0.3487 0.4423
REMARK 3 20 3.1046 - 3.0520 0.85 2250 117 0.3711 0.3994
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) : 0.414
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.631
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.71
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 : 0.003 8858
REMARK 3 ANGLE : 0.734 12139
REMARK 3 CHIRALITY : 0.044 1296
REMARK 3 PLANARITY : 0.005 1579
REMARK 3 DIHEDRAL : 9.517 7009
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 6F25 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1200007596.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87313
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55240
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 48.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 11.90
REMARK 200 R MERGE (I) : 0.05284
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.66060
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: 3LII
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M LISO4, 100 MM HEPES PH 7, 60 MM
REMARK 280 MGSO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 38.57500
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 77.15000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 57.86250
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 96.43750
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 19.28750
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -300.0 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 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 GLY B 260
REMARK 465 GLY B 261
REMARK 465 THR B 262
REMARK 465 GLY B 263
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 ARG A 493 CB CG CD NE CZ NH1 NH2
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 O3 NAG A 604 O5 NAG A 605 2.09
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 -6.71 70.98
REMARK 500 ASP A 61 88.70 -66.84
REMARK 500 ALA A 62 37.08 -96.57
REMARK 500 PHE A 123 12.76 56.62
REMARK 500 PHE A 158 11.34 -144.27
REMARK 500 SER A 203 -125.21 59.40
REMARK 500 ASP A 306 -81.97 -98.78
REMARK 500 VAL A 407 -59.93 -121.49
REMARK 500 TYR A 449 30.06 -97.83
REMARK 500 ASN A 464 46.77 -94.03
REMARK 500 PHE B 47 -0.01 70.58
REMARK 500 ALA B 62 43.37 -90.01
REMARK 500 PRO B 106 87.43 -66.01
REMARK 500 PHE B 123 11.24 59.84
REMARK 500 ALA B 127 145.76 -170.09
REMARK 500 PHE B 158 15.03 -145.90
REMARK 500 ASN B 170 16.99 59.20
REMARK 500 SER B 196 64.09 -153.14
REMARK 500 SER B 203 -127.19 59.75
REMARK 500 ASP B 306 -77.97 -108.72
REMARK 500 VAL B 367 77.89 -117.19
REMARK 500 VAL B 407 -63.10 -123.06
REMARK 500 TYR B 449 32.47 -97.53
REMARK 500 ASN B 464 51.53 -103.90
REMARK 500 ARG B 493 76.55 -115.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CVZ A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 629
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CVZ B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 604 through NAG A 605 bound to ASN A 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 601 through FUC A 603 bound to ASN A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 606 bound
REMARK 800 to ASN A 464
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 601 through FUC B 603 bound to ASN B 350
DBREF 6F25 A 5 543 UNP P22303 ACES_HUMAN 36 574
DBREF 6F25 B 5 543 UNP P22303 ACES_HUMAN 36 574
SEQRES 1 A 539 ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG LEU
SEQRES 2 A 539 ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL SER
SEQRES 3 A 539 ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET GLY
SEQRES 4 A 539 PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO TRP
SEQRES 5 A 539 SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL CYS
SEQRES 6 A 539 TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU GLY
SEQRES 7 A 539 THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU ASP
SEQRES 8 A 539 CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG PRO
SEQRES 9 A 539 THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY GLY
SEQRES 10 A 539 GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR ASP
SEQRES 11 A 539 GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU VAL
SEQRES 12 A 539 SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA
SEQRES 13 A 539 LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 14 A 539 LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU ASN
SEQRES 15 A 539 VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR LEU
SEQRES 16 A 539 PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET HIS
SEQRES 17 A 539 LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG ALA
SEQRES 18 A 539 VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA THR
SEQRES 19 A 539 VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN LEU
SEQRES 20 A 539 ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY GLY
SEQRES 21 A 539 ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG PRO
SEQRES 22 A 539 ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU PRO
SEQRES 23 A 539 GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL VAL
SEQRES 24 A 539 ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU ILE
SEQRES 25 A 539 ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL GLY
SEQRES 26 A 539 VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR GLY
SEQRES 27 A 539 ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE SER
SEQRES 28 A 539 ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL PRO
SEQRES 29 A 539 GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU HIS
SEQRES 30 A 539 TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG LEU
SEQRES 31 A 539 ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN VAL
SEQRES 32 A 539 VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA ALA
SEQRES 33 A 539 GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS ARG
SEQRES 34 A 539 ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL PRO
SEQRES 35 A 539 HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO LEU
SEQRES 36 A 539 ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE PHE
SEQRES 37 A 539 ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA ARG
SEQRES 38 A 539 THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA PRO
SEQRES 39 A 539 GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR VAL
SEQRES 40 A 539 SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY LEU
SEQRES 41 A 539 ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU PRO
SEQRES 42 A 539 LYS LEU LEU SER ALA THR
SEQRES 1 B 539 ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG LEU
SEQRES 2 B 539 ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL SER
SEQRES 3 B 539 ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET GLY
SEQRES 4 B 539 PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO TRP
SEQRES 5 B 539 SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL CYS
SEQRES 6 B 539 TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU GLY
SEQRES 7 B 539 THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU ASP
SEQRES 8 B 539 CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG PRO
SEQRES 9 B 539 THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY GLY
SEQRES 10 B 539 GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR ASP
SEQRES 11 B 539 GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU VAL
SEQRES 12 B 539 SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA
SEQRES 13 B 539 LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 14 B 539 LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU ASN
SEQRES 15 B 539 VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR LEU
SEQRES 16 B 539 PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET HIS
SEQRES 17 B 539 LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG ALA
SEQRES 18 B 539 VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA THR
SEQRES 19 B 539 VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN LEU
SEQRES 20 B 539 ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY GLY
SEQRES 21 B 539 ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG PRO
SEQRES 22 B 539 ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU PRO
SEQRES 23 B 539 GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL VAL
SEQRES 24 B 539 ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU ILE
SEQRES 25 B 539 ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL GLY
SEQRES 26 B 539 VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR GLY
SEQRES 27 B 539 ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE SER
SEQRES 28 B 539 ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL PRO
SEQRES 29 B 539 GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU HIS
SEQRES 30 B 539 TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG LEU
SEQRES 31 B 539 ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN VAL
SEQRES 32 B 539 VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA ALA
SEQRES 33 B 539 GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS ARG
SEQRES 34 B 539 ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL PRO
SEQRES 35 B 539 HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO LEU
SEQRES 36 B 539 ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE PHE
SEQRES 37 B 539 ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA ARG
SEQRES 38 B 539 THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA PRO
SEQRES 39 B 539 GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR VAL
SEQRES 40 B 539 SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY LEU
SEQRES 41 B 539 ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU PRO
SEQRES 42 B 539 LYS LEU LEU SER ALA THR
HET NAG A 601 14
HET NAG A 602 14
HET FUC A 603 10
HET NAG A 604 14
HET NAG A 605 14
HET NAG A 606 14
HET SO4 A 607 5
HET SO4 A 608 5
HET SO4 A 609 5
HET SO4 A 610 5
HET SO4 A 611 5
HET SO4 A 612 5
HET CVZ A 613 45
HET CL A 614 1
HET CL A 615 1
HET CL A 616 1
HET CL A 617 1
HET CL A 618 1
HET CL A 619 1
HET CL A 620 1
HET CL A 621 1
HET CL A 622 1
HET CL A 623 1
HET CL A 624 1
HET CL A 625 1
HET CL A 626 1
HET CL A 627 1
HET CL A 628 1
HET CL A 629 1
HET NAG B 601 14
HET NAG B 602 14
HET FUC B 603 10
HET SO4 B 604 5
HET SO4 B 605 5
HET SO4 B 606 5
HET SO4 B 607 5
HET SO4 B 608 5
HET SO4 B 609 5
HET CVZ B 610 45
HET CL B 611 1
HET CL B 612 1
HET CL B 613 1
HET CL B 614 1
HET CL B 615 1
HET CL B 616 1
HET CL B 617 1
HET CL B 618 1
HET CL B 619 1
HET CL B 620 1
HET CL B 621 1
HET CL B 622 1
HET CL B 623 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM SO4 SULFATE ION
HETNAM CVZ 3-[(~{E})-5-[ETHYL-[(2-NITROPHENYL)METHYL]AMINO]PENT-1-
HETNAM 2 CVZ ENYL]-1-[5-[ETHYL-[(2-NITROPHENYL)
HETNAM 3 CVZ METHYL]AMINO]PENTYL]-6-METHYL-PYRIMIDINE-2,4-DIONE
HETNAM CL CHLORIDE ION
FORMUL 3 NAG 7(C8 H15 N O6)
FORMUL 3 FUC 2(C6 H12 O5)
FORMUL 6 SO4 12(O4 S 2-)
FORMUL 12 CVZ 2(C33 H44 N6 O6)
FORMUL 13 CL 29(CL 1-)
FORMUL 50 HOH *205(H2 O)
HELIX 1 AA1 MET A 42 ARG A 46 5 5
HELIX 2 AA2 PHE A 80 MET A 85 1 6
HELIX 3 AA3 LEU A 130 ASP A 134 5 5
HELIX 4 AA4 GLY A 135 ARG A 143 1 9
HELIX 5 AA5 GLY A 154 LEU A 159 1 6
HELIX 6 AA6 ASN A 170 VAL A 187 1 18
HELIX 7 AA7 ALA A 188 PHE A 190 5 3
HELIX 8 AA8 SER A 203 SER A 215 1 13
HELIX 9 AA9 SER A 215 GLY A 220 1 6
HELIX 10 AB1 MET A 241 VAL A 255 1 15
HELIX 11 AB2 ASP A 266 ARG A 274 1 9
HELIX 12 AB3 PRO A 277 ASN A 283 1 7
HELIX 13 AB4 HIS A 284 LEU A 289 5 6
HELIX 14 AB5 THR A 311 GLY A 319 1 9
HELIX 15 AB6 PHE A 338 GLY A 342 5 5
HELIX 16 AB7 SER A 355 VAL A 367 1 13
HELIX 17 AB8 SER A 371 THR A 383 1 13
HELIX 18 AB9 ASP A 390 VAL A 407 1 18
HELIX 19 AC1 VAL A 407 ALA A 420 1 14
HELIX 20 AC2 PRO A 440 GLY A 444 5 5
HELIX 21 AC3 GLU A 450 PHE A 455 1 6
HELIX 22 AC4 GLY A 456 ASP A 460 5 5
HELIX 23 AC5 THR A 466 GLY A 487 1 22
HELIX 24 AC6 ARG A 525 ARG A 534 1 10
HELIX 25 AC7 ARG A 534 SER A 541 1 8
HELIX 26 AC8 MET B 42 ARG B 46 5 5
HELIX 27 AC9 PHE B 80 MET B 85 1 6
HELIX 28 AD1 LEU B 130 ASP B 134 5 5
HELIX 29 AD2 GLY B 135 ARG B 143 1 9
HELIX 30 AD3 VAL B 153 LEU B 159 1 7
HELIX 31 AD4 ASN B 170 VAL B 187 1 18
HELIX 32 AD5 ALA B 188 PHE B 190 5 3
HELIX 33 AD6 SER B 203 SER B 215 1 13
HELIX 34 AD7 SER B 215 GLY B 220 1 6
HELIX 35 AD8 MET B 241 VAL B 255 1 15
HELIX 36 AD9 ASN B 265 ARG B 274 1 10
HELIX 37 AE1 PRO B 277 HIS B 284 1 8
HELIX 38 AE2 GLU B 285 LEU B 289 5 5
HELIX 39 AE3 THR B 311 ALA B 318 1 8
HELIX 40 AE4 SER B 336 GLY B 342 5 7
HELIX 41 AE5 SER B 355 VAL B 367 1 13
HELIX 42 AE6 SER B 371 THR B 383 1 13
HELIX 43 AE7 ASP B 390 VAL B 407 1 18
HELIX 44 AE8 VAL B 407 GLN B 421 1 15
HELIX 45 AE9 PRO B 440 GLY B 444 5 5
HELIX 46 AF1 GLU B 450 PHE B 455 1 6
HELIX 47 AF2 GLY B 456 ASP B 460 5 5
HELIX 48 AF3 THR B 466 GLY B 487 1 22
HELIX 49 AF4 ARG B 525 ARG B 534 1 10
HELIX 50 AF5 ARG B 534 SER B 541 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 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 LEU A 99 N ILE A 35
SHEET 4 AA211 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 AA211 THR A 112 ILE A 118 1 N TRP A 117 O VAL A 147
SHEET 6 AA211 GLY A 192 GLU A 202 1 O SER A 196 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 ARG A 424 N VAL A 326
SHEET 10 AA211 GLN A 509 LEU A 513 1 O VAL A 511 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 GLY B 15 N VAL B 12
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O VAL B 60 N ARG B 18
SHEET 1 AA511 ILE B 20 THR B 24 0
SHEET 2 AA511 GLY B 27 PRO B 36 -1 O VAL B 29 N LEU B 22
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
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 145
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 VAL B 226 N LEU B 199
SHEET 8 AA511 LEU B 324 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ALA B 423 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 GLU B 519 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 2.03
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.03
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.03
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.03
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.03
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.03
LINK ND2 ASN A 265 C1 NAG A 604 1555 1555 1.44
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 464 C1 NAG A 606 1555 1555 1.44
LINK ND2 ASN B 350 C1 NAG B 601 1555 1555 1.45
LINK O4 NAG A 601 C1 NAG A 602 1555 1555 1.45
LINK O6 NAG A 601 C1 FUC A 603 1555 1555 1.45
LINK O3 NAG A 604 C1 NAG A 605 1555 1555 1.46
LINK O4 NAG B 601 C1 NAG B 602 1555 1555 1.44
LINK O6 NAG B 601 C1 FUC B 603 1555 1555 1.44
SITE 1 AC1 2 THR A 466 ALA A 467
SITE 1 AC2 3 GLN A 413 ARG A 417 HOH A 763
SITE 1 AC3 3 ARG A 356 LEU A 360 ARG B 534
SITE 1 AC4 3 THR A 504 GLY A 506 ALA A 507
SITE 1 AC5 3 HIS A 322 HOH A 756 ARG B 276
SITE 1 AC6 2 MET A 241 GLY A 242
SITE 1 AC7 10 TRP A 86 TYR A 124 GLU A 202 SER A 203
SITE 2 AC7 10 TRP A 286 HIS A 287 PHE A 295 TYR A 337
SITE 3 AC7 10 PHE A 338 HIS A 447
SITE 1 AC8 2 ARG A 424 ARG B 276
SITE 1 AC9 1 LEU A 441
SITE 1 AD1 2 ARG A 16 GLY A 58
SITE 1 AD2 1 ARG A 143
SITE 1 AD3 1 ASP A 372
SITE 1 AD4 1 ARG A 136
SITE 1 AD5 1 ARG A 393
SITE 1 AD6 2 ARG A 534 LYS A 538
SITE 1 AD7 2 PRO A 312 GLU A 313
SITE 1 AD8 2 ARG A 165 THR A 267
SITE 1 AD9 1 ARG A 417
SITE 1 AE1 1 ARG A 522
SITE 1 AE2 2 GLN A 527 ALA A 528
SITE 1 AE3 3 THR B 504 GLY B 506 ALA B 507
SITE 1 AE4 5 ARG A 534 ARG B 356 LEU B 360 TRP B 385
SITE 2 AE4 5 HOH B 706
SITE 1 AE5 1 ARG B 478
SITE 1 AE6 4 GLY B 240 MET B 241 GLY B 242 HOH B 730
SITE 1 AE7 3 GLN B 413 ARG B 417 HOH B 739
SITE 1 AE8 2 PRO B 108 THR B 109
SITE 1 AE9 18 PRO A 492 ARG A 493 PRO A 495 LYS A 496
SITE 2 AE9 18 TRP B 86 GLY B 121 TYR B 124 GLU B 202
SITE 3 AE9 18 SER B 203 TRP B 286 HIS B 287 PRO B 290
SITE 4 AE9 18 GLN B 291 GLU B 292 TYR B 337 PHE B 338
SITE 5 AE9 18 TYR B 341 HIS B 447
SITE 1 AF1 2 PRO B 162 ARG B 245
SITE 1 AF2 1 ARG B 393
SITE 1 AF3 1 ARG B 525
SITE 1 AF4 2 LYS B 23 ARG B 136
SITE 1 AF5 1 LYS B 53
SITE 1 AF6 1 ARG B 393
SITE 1 AF7 1 ARG B 16
SITE 1 AF8 1 MET A 42
SITE 1 AF9 2 GLN B 527 ALA B 528
SITE 1 AG1 2 ALA B 497 GLN B 499
SITE 1 AG2 1 GLU B 243
SITE 1 AG3 2 ASN A 265 GLU A 268
SITE 1 AG4 4 GLY A 345 PHE A 346 SER A 347 ASN A 350
SITE 1 AG5 2 SER A 462 ASN A 464
SITE 1 AG6 3 GLY B 345 SER B 347 ASN B 350
CRYST1 211.074 211.074 115.725 90.00 90.00 120.00 P 61 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 0.004738 0.002735 0.000000 0.00000
SCALE2 0.000000 0.005471 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008641 0.00000
TER 4154 THR A 543
TER 8326 THR B 543
MASTER 467 0 52 50 32 0 49 6 8806 2 284 84
END |