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HEADER HYDROLASE 27-MAY-19 6RUA
TITLE STRUCTURE OF RECOMBINANT HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH A
TITLE 2 COUMARIN-BASED FLUORESCENT PROBE LINKED TO SULFONAMIDE TYPE
TITLE 3 INHIBITOR.
CAVEAT 6RUA NAG A 601 HAS WRONG CHIRALITY AT ATOM C1 NAG A 606 HAS WRONG
CAVEAT 2 6RUA CHIRALITY AT ATOM C1 FUC A 609 HAS WRONG CHIRALITY AT ATOM
CAVEAT 3 6RUA C1 NAG A 612 HAS WRONG CHIRALITY AT ATOM C1 NAG A 615 HAS
CAVEAT 4 6RUA WRONG CHIRALITY AT ATOM C1 NAG B 614 HAS WRONG CHIRALITY AT
CAVEAT 5 6RUA ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE
COMPND 5 ESTERASE II,PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
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: BCHE, CHE1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS HUMAN BUTYRYLCHOLINESTERASE, INSECT CELL, HYDROLASE, FLUORESCENT
KEYWDS 2 PROBES, SULFONAMIDE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR N.COQUELLE,D.KNEZ,B.BRUS,S.GOBEC,J.P.COLLETIER
REVDAT 1 22-JAN-20 6RUA 0
JRNL AUTH S.PAJK,D.KNEZ,U.KOSAK,M.ZOROVIC,X.BRAZZOLOTTO,N.COQUELLE,
JRNL AUTH 2 F.NACHON,J.P.COLLETIER,M.ZIVIN,J.STOJAN,S.GOBEC
JRNL TITL DEVELOPMENT OF POTENT REVERSIBLE SELECTIVE INHIBITORS OF
JRNL TITL 2 BUTYRYLCHOLINESTERASE AS FLUORESCENT PROBES.
JRNL REF J ENZYME INHIB MED CHEM V. 35 498 2020
JRNL REFN ESSN 1475-6374
JRNL PMID 31914836
JRNL DOI 10.1080/14756366.2019.1710502
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_3139: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 37465
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1122
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 44.9326 - 5.4971 0.98 4714 143 0.1771 0.2058
REMARK 3 2 5.4971 - 4.3644 0.99 4600 145 0.1484 0.1853
REMARK 3 3 4.3644 - 3.8131 1.00 4530 138 0.1492 0.2008
REMARK 3 4 3.8131 - 3.4646 1.00 4546 140 0.1783 0.2750
REMARK 3 5 3.4646 - 3.2163 0.98 4476 140 0.2106 0.2692
REMARK 3 6 3.2163 - 3.0267 0.99 4490 145 0.2229 0.3305
REMARK 3 7 3.0267 - 2.8752 1.00 4495 131 0.2501 0.3005
REMARK 3 8 2.8752 - 2.7500 1.00 4492 140 0.2534 0.3414
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.060
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.006 9093
REMARK 3 ANGLE : 0.793 12347
REMARK 3 CHIRALITY : 0.048 1369
REMARK 3 PLANARITY : 0.005 1546
REMARK 3 DIHEDRAL : 13.137 5280
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 6RUA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102591.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
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) : 0.8726
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37475
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 44.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.09612
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.7100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.69690
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.270
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: 1P0I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE 12% PEG 4000 PH
REMARK 280 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 -1.000000 0.000000 0.000000 38.14500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.67500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.10000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.67500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.14500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.10000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 12590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 87.0 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 GLU A 1
REMARK 465 ASP A 2
REMARK 465 LEU A 530
REMARK 465 GLU A 531
REMARK 465 MET A 532
REMARK 465 THR A 533
REMARK 465 GLY A 534
REMARK 465 ASN A 535
REMARK 465 ILE A 536
REMARK 465 ASP A 537
REMARK 465 GLU A 538
REMARK 465 ALA A 539
REMARK 465 GLU A 540
REMARK 465 TRP A 541
REMARK 465 GLU A 542
REMARK 465 TRP A 543
REMARK 465 LYS A 544
REMARK 465 ALA A 545
REMARK 465 GLY A 546
REMARK 465 PHE A 547
REMARK 465 HIS A 548
REMARK 465 ARG A 549
REMARK 465 TRP A 550
REMARK 465 ASN A 551
REMARK 465 ASN A 552
REMARK 465 TYR A 553
REMARK 465 MET A 554
REMARK 465 MET A 555
REMARK 465 ASP A 556
REMARK 465 TRP A 557
REMARK 465 LYS A 558
REMARK 465 ASN A 559
REMARK 465 GLN A 560
REMARK 465 PHE A 561
REMARK 465 ASN A 562
REMARK 465 ASP A 563
REMARK 465 TYR A 564
REMARK 465 THR A 565
REMARK 465 SER A 566
REMARK 465 LYS A 567
REMARK 465 LYS A 568
REMARK 465 GLU A 569
REMARK 465 SER A 570
REMARK 465 CYS A 571
REMARK 465 VAL A 572
REMARK 465 GLY A 573
REMARK 465 LEU A 574
REMARK 465 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 465 LEU B 530
REMARK 465 GLU B 531
REMARK 465 MET B 532
REMARK 465 THR B 533
REMARK 465 GLY B 534
REMARK 465 ASN B 535
REMARK 465 ILE B 536
REMARK 465 ASP B 537
REMARK 465 GLU B 538
REMARK 465 ALA B 539
REMARK 465 GLU B 540
REMARK 465 TRP B 541
REMARK 465 GLU B 542
REMARK 465 TRP B 543
REMARK 465 LYS B 544
REMARK 465 ALA B 545
REMARK 465 GLY B 546
REMARK 465 PHE B 547
REMARK 465 HIS B 548
REMARK 465 ARG B 549
REMARK 465 TRP B 550
REMARK 465 ASN B 551
REMARK 465 ASN B 552
REMARK 465 TYR B 553
REMARK 465 MET B 554
REMARK 465 MET B 555
REMARK 465 ASP B 556
REMARK 465 TRP B 557
REMARK 465 LYS B 558
REMARK 465 ASN B 559
REMARK 465 GLN B 560
REMARK 465 PHE B 561
REMARK 465 ASN B 562
REMARK 465 ASP B 563
REMARK 465 TYR B 564
REMARK 465 THR B 565
REMARK 465 SER B 566
REMARK 465 LYS B 567
REMARK 465 LYS B 568
REMARK 465 GLU B 569
REMARK 465 SER B 570
REMARK 465 CYS B 571
REMARK 465 VAL B 572
REMARK 465 GLY B 573
REMARK 465 LEU B 574
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 TYR A 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 506 CG CD OE1 OE2
REMARK 470 ILE B 4 CG1 CG2 CD1
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 SER B 53 OG
REMARK 470 TYR B 282 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR B 483 OG1 CG2
REMARK 470 GLN B 484 CG CD OE1 NE2
REMARK 470 ASN B 485 CG OD1 ND2
REMARK 470 SER B 507 OG
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 ND2 ASN B 106 O5 NAG B 603 1.71
REMARK 500 ND2 ASN A 241 O5 NAG A 607 1.84
REMARK 500 ND2 ASN B 241 O5 NAG B 604 1.99
REMARK 500 ND2 ASN B 455 O5 NAG B 611 2.02
REMARK 500 ND2 ASN A 57 O5 NAG A 603 2.05
REMARK 500 O4 NAG A 612 O5 NAG A 613 2.13
REMARK 500 O4 NAG A 610 O5 NAG A 611 2.15
REMARK 500 C6 NAG A 603 C1 FUC A 604 2.16
REMARK 500 OG SER A 198 O HOH A 701 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OH TYR A 237 O ARG B 453 1545 2.07
REMARK 500
REMARK 500 REMARK: NULL
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 LEU A 236 CB - CG - CD2 ANGL. DEV. = -12.6 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 ASP A 54 -155.92 -81.30
REMARK 500 ASN A 106 54.99 -166.13
REMARK 500 PHE A 118 11.30 59.87
REMARK 500 ALA A 162 79.68 -164.65
REMARK 500 SER A 198 -122.70 65.57
REMARK 500 LEU A 236 -53.36 -24.80
REMARK 500 ASP A 297 -71.14 -122.92
REMARK 500 TYR A 332 44.31 -98.53
REMARK 500 SER A 362 -178.70 -60.17
REMARK 500 GLU A 383 5.05 -63.75
REMARK 500 PHE A 398 -56.17 -128.04
REMARK 500 ARG A 453 4.76 -66.40
REMARK 500 GLU A 482 -77.35 -93.77
REMARK 500 LYS B 9 -3.45 -58.57
REMARK 500 PHE B 43 2.35 82.16
REMARK 500 ASP B 54 -141.27 -82.60
REMARK 500 SER B 89 145.30 -176.58
REMARK 500 ASN B 106 55.58 -149.47
REMARK 500 ALA B 162 76.28 -157.93
REMARK 500 ASN B 165 17.62 53.39
REMARK 500 SER B 198 -113.53 62.90
REMARK 500 TYR B 282 70.29 -115.77
REMARK 500 ASP B 297 -69.58 -134.67
REMARK 500 GLN B 311 72.83 -102.21
REMARK 500 PHE B 398 -58.47 -128.59
REMARK 500 ASN B 455 45.02 -68.64
REMARK 500 PRO B 480 43.67 -80.78
REMARK 500 GLU B 506 -73.53 -57.27
REMARK 500 PHE B 525 -42.45 -131.54
REMARK 500 PRO B 527 5.28 -69.38
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 B 792 DISTANCE = 6.05 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 KJT B 620
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KJT B 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 601 through NAG A 602 bound to ASN A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 603 through FUC A 604 bound to ASN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 605 through NAG A 606 bound to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 607 through FUC A 609 bound to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 615 bound
REMARK 800 to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 610 through NAG A 611 bound to ASN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 612 through FUL A 614 bound to ASN A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound
REMARK 800 to ASN B 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound
REMARK 800 to ASN B 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound
REMARK 800 to ASN B 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 604 through FUL B 606 bound to ASN B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 607 through FUL B 609 bound to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 610 bound
REMARK 800 to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 611 through FUL B 613 bound to ASN B 455
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 614 bound
REMARK 800 to ASN B 481
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DYT RELATED DB: PDB
REMARK 900 5DYT CONTAINS THE SAME PROTEIN COMPLEXED WITH THE PARENT COMPOUND
DBREF 6RUA A 1 574 UNP P06276 CHLE_HUMAN 29 602
DBREF 6RUA B 1 574 UNP P06276 CHLE_HUMAN 29 602
SEQRES 1 A 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 574 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 574 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 574 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 574 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 574 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 574 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 574 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 574 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 574 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 574 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 574 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 574 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 574 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 574 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 574 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 574 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 574 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 574 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 574 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 574 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 574 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 574 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 574 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 574 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 574 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 574 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 574 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 574 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 574 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 574 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 574 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 574 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 574 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 574 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 A 574 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 574 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 A 574 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 574 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 574 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 574 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 A 574 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY
SEQRES 43 A 574 PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN
SEQRES 44 A 574 GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL
SEQRES 45 A 574 GLY LEU
SEQRES 1 B 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 B 574 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 B 574 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 B 574 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 B 574 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 B 574 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 B 574 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 B 574 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 B 574 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 B 574 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 B 574 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 B 574 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 B 574 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 B 574 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 B 574 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 B 574 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 B 574 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 B 574 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 B 574 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 B 574 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 B 574 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 B 574 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 B 574 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 B 574 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 B 574 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 B 574 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 B 574 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 B 574 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 B 574 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 B 574 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 B 574 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 B 574 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 B 574 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 B 574 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 B 574 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 B 574 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 B 574 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 B 574 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 B 574 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 B 574 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 B 574 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 B 574 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY
SEQRES 43 B 574 PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN
SEQRES 44 B 574 GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL
SEQRES 45 B 574 GLY LEU
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET FUC A 604 10
HET NAG A 605 14
HET NAG A 606 14
HET NAG A 607 14
HET NAG A 608 14
HET FUC A 609 10
HET NAG A 610 14
HET NAG A 611 14
HET NAG A 612 14
HET NAG A 613 14
HET FUL A 614 10
HET NAG A 615 14
HET EDO A 616 4
HET EDO A 617 4
HET EDO A 618 4
HET EDO A 619 4
HET CL A 620 1
HET EDO A 621 4
HET CL A 622 1
HET EDO A 623 4
HET NAG B 601 14
HET NAG B 602 14
HET NAG B 603 14
HET NAG B 604 14
HET NAG B 605 14
HET FUL B 606 10
HET NAG B 607 14
HET NAG B 608 14
HET FUL B 609 10
HET NAG B 610 14
HET NAG B 611 14
HET NAG B 612 14
HET FUL B 613 10
HET NAG B 614 14
HET PEG B 615 7
HET EDO B 616 4
HET EDO B 617 4
HET EDO B 618 4
HET CL B 619 1
HET KJT B 620 29
HET CL B 621 1
HET CL B 622 1
HET PGE B 623 10
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM FUC ALPHA-L-FUCOSE
HETNAM FUL BETA-L-FUCOSE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM KJT DIETHYL-[6-[[2-[2-[2-[NAPHTHALEN-2-YLSULFONYL-
HETNAM 2 KJT [[(3~{R})-1-(PHENYLMETHYL)PIPERIDIN-3-
HETNAM 3 KJT YL]METHYL]AMINO]ETHOXY]ETHOXY]ETHYLAMINO]-OXIDANYL-
HETNAM 4 KJT METHYL]-7-OXIDANYLIDENE-1,3,4,4~{A},5,6,8,8~{A}-
HETNAM 5 KJT OCTAHYDRONAPHTHALEN-2-YLIDENE]AZANIUM
HETNAM PGE TRIETHYLENE GLYCOL
HETSYN FUL 6-DEOXY-BETA-L-GALACTOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 23(C8 H15 N O6)
FORMUL 4 FUC 2(C6 H12 O5)
FORMUL 8 FUL 4(C6 H12 O5)
FORMUL 10 EDO 9(C2 H6 O2)
FORMUL 14 CL 5(CL 1-)
FORMUL 26 PEG C4 H10 O3
FORMUL 31 KJT C44 H63 N4 O6 S 1+
FORMUL 34 PGE C6 H14 O4
FORMUL 35 HOH *175(H2 O)
HELIX 1 AA1 LEU A 38 ARG A 42 5 5
HELIX 2 AA2 PHE A 76 MET A 81 1 6
HELIX 3 AA3 LEU A 125 ASP A 129 5 5
HELIX 4 AA4 GLY A 130 ARG A 138 1 9
HELIX 5 AA5 GLY A 149 LEU A 154 1 6
HELIX 6 AA6 ASN A 165 ILE A 182 1 18
HELIX 7 AA7 ALA A 183 PHE A 185 5 3
HELIX 8 AA8 SER A 198 SER A 210 1 13
HELIX 9 AA9 SER A 210 SER A 215 1 6
HELIX 10 AB1 SER A 235 GLY A 251 1 17
HELIX 11 AB2 ASN A 256 ARG A 265 1 10
HELIX 12 AB3 ASP A 268 LEU A 274 1 7
HELIX 13 AB4 ASN A 275 VAL A 280 5 6
HELIX 14 AB5 MET A 302 LEU A 309 1 8
HELIX 15 AB6 GLY A 326 LEU A 330 5 5
HELIX 16 AB7 THR A 346 PHE A 358 1 13
HELIX 17 AB8 SER A 362 TYR A 373 1 12
HELIX 18 AB9 GLU A 383 PHE A 398 1 16
HELIX 19 AC1 PHE A 398 GLU A 411 1 14
HELIX 20 AC2 PRO A 431 GLY A 435 5 5
HELIX 21 AC3 GLU A 441 PHE A 446 1 6
HELIX 22 AC4 GLY A 447 ASN A 455 5 9
HELIX 23 AC5 THR A 457 GLY A 478 1 22
HELIX 24 AC6 ARG A 515 PHE A 525 1 11
HELIX 25 AC7 PHE A 526 VAL A 529 5 4
HELIX 26 AC8 LEU B 38 ARG B 42 5 5
HELIX 27 AC9 PHE B 76 MET B 81 1 6
HELIX 28 AD1 LEU B 125 ASP B 129 5 5
HELIX 29 AD2 GLY B 130 ARG B 138 1 9
HELIX 30 AD3 GLY B 149 LEU B 154 1 6
HELIX 31 AD4 ASN B 165 ILE B 182 1 18
HELIX 32 AD5 SER B 198 LEU B 208 1 11
HELIX 33 AD6 SER B 210 PHE B 217 5 8
HELIX 34 AD7 SER B 235 THR B 250 1 16
HELIX 35 AD8 ASN B 256 ARG B 265 1 10
HELIX 36 AD9 ASP B 268 LEU B 274 1 7
HELIX 37 AE1 ASN B 275 VAL B 279 5 5
HELIX 38 AE2 MET B 302 GLY B 310 1 9
HELIX 39 AE3 GLY B 326 VAL B 331 1 6
HELIX 40 AE4 THR B 346 PHE B 358 1 13
HELIX 41 AE5 SER B 362 TYR B 373 1 12
HELIX 42 AE6 GLU B 383 PHE B 398 1 16
HELIX 43 AE7 PHE B 398 GLU B 411 1 14
HELIX 44 AE8 PRO B 431 GLY B 435 5 5
HELIX 45 AE9 GLU B 441 GLY B 447 1 7
HELIX 46 AF1 LEU B 448 GLU B 451 5 4
HELIX 47 AF2 THR B 457 GLY B 478 1 22
HELIX 48 AF3 ARG B 515 PHE B 525 1 11
HELIX 49 AF4 PHE B 526 VAL B 529 5 4
SHEET 1 AA1 3 ILE A 5 THR A 8 0
SHEET 2 AA1 3 GLY A 11 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 AA1 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 AA211 MET A 16 THR A 19 0
SHEET 2 AA211 THR A 24 PRO A 32 -1 O ALA A 27 N MET A 16
SHEET 3 AA211 TYR A 94 ALA A 101 -1 O LEU A 95 N ILE A 31
SHEET 4 AA211 ILE A 140 MET A 144 -1 O VAL A 141 N TRP A 98
SHEET 5 AA211 ALA A 107 ILE A 113 1 N LEU A 110 O ILE A 140
SHEET 6 AA211 GLY A 187 GLU A 197 1 O ASN A 188 N ALA A 107
SHEET 7 AA211 ARG A 219 GLN A 223 1 O GLN A 223 N GLY A 196
SHEET 8 AA211 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 AA211 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 AA211 LYS A 499 LEU A 503 1 O LEU A 503 N TYR A 420
SHEET 11 AA211 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 AA3 3 ILE B 5 THR B 8 0
SHEET 2 AA3 3 GLY B 11 ARG B 14 -1 O GLY B 11 N THR B 8
SHEET 3 AA3 3 ILE B 55 ASN B 57 1 O TRP B 56 N LYS B 12
SHEET 1 AA411 MET B 16 VAL B 20 0
SHEET 2 AA411 GLY B 23 PRO B 32 -1 O VAL B 25 N LEU B 18
SHEET 3 AA411 TYR B 94 PRO B 100 -1 O VAL B 97 N PHE B 28
SHEET 4 AA411 ILE B 140 MET B 144 -1 O SER B 143 N ASN B 96
SHEET 5 AA411 ALA B 107 ILE B 113 1 N TRP B 112 O VAL B 142
SHEET 6 AA411 GLY B 187 GLU B 197 1 O ASN B 188 N ALA B 107
SHEET 7 AA411 ARG B 219 GLN B 223 1 O ARG B 219 N LEU B 194
SHEET 8 AA411 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 AA411 ALA B 416 PHE B 421 1 O PHE B 421 N VAL B 321
SHEET 10 AA411 LYS B 499 LEU B 503 1 O LEU B 503 N TYR B 420
SHEET 11 AA411 ILE B 510 THR B 512 -1 O MET B 511 N TYR B 500
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.03
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.04
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.05
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.04
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.03
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.04
LINK ND2 ASN A 17 C1 NAG A 601 1555 1555 1.46
LINK ND2 ASN A 57 C1 NAG A 603 1555 1555 1.47
LINK ND2 ASN A 106 C1 NAG A 605 1555 1555 1.44
LINK ND2 ASN A 241 C1 NAG A 607 1555 1555 1.41
LINK ND2 ASN A 341 C1 NAG A 615 1555 1555 1.47
LINK ND2 ASN A 481 C1 NAG A 610 1555 1555 1.47
LINK ND2 ASN A 486 C1 NAG A 612 1555 1555 1.49
LINK ND2 ASN B 17 C1 NAG B 601 1555 1555 1.47
LINK ND2 ASN B 57 C1 NAG B 602 1555 1555 1.48
LINK ND2 ASN B 106 C1 NAG B 603 1555 1555 1.47
LINK ND2 ASN B 241 C1 NAG B 604 1555 1555 1.46
LINK ND2 ASN B 256 C1 NAG B 607 1555 1555 1.45
LINK ND2 ASN B 341 C1 NAG B 610 1555 1555 1.49
LINK ND2 ASN B 455 C1 NAG B 611 1555 1555 1.55
LINK ND2 ASN B 481 C1 NAG B 614 1555 1555 1.49
LINK O4 NAG A 601 C1 NAG A 602 1555 1555 1.46
LINK O6 NAG A 603 C1 FUC A 604 1555 1555 1.43
LINK O4 NAG A 605 C1 NAG A 606 1555 1555 1.48
LINK O4 NAG A 607 C1 NAG A 608 1555 1555 1.45
LINK O6 NAG A 607 C1 FUC A 609 1555 1555 1.47
LINK O4 NAG A 610 C1 NAG A 611 1555 1555 1.51
LINK O4 NAG A 612 C1 NAG A 613 1555 1555 1.50
LINK O6 NAG A 612 C1 FUL A 614 1555 1555 1.47
LINK O4 NAG B 604 C1 NAG B 605 1555 1555 1.45
LINK O6 NAG B 604 C1 FUL B 606 1555 1555 1.52
LINK O4 NAG B 607 C1 NAG B 608 1555 1555 1.46
LINK O6 NAG B 607 C1 FUL B 609 1555 1555 1.45
LINK O4 NAG B 611 C1 NAG B 612 1555 1555 1.45
LINK O6 NAG B 611 C1 FUL B 613 1555 1555 1.46
CISPEP 1 ALA A 101 PRO A 102 0 3.88
CISPEP 2 ALA B 101 PRO B 102 0 3.33
SITE 1 AC1 2 HIS A 77 GLU A 443
SITE 1 AC2 3 LYS A 494 THR A 496 HOH A 757
SITE 1 AC3 1 GLY A 116
SITE 1 AC4 5 TYR A 33 SER A 48 LEU A 49 GLN A 176
SITE 2 AC4 5 LYS A 180
SITE 1 AC5 1 ARG A 386
SITE 1 AC6 4 ASN A 106 THR A 108 ASN A 188 LYS A 476
SITE 1 AC7 5 ASN A 228 CYS A 400 PRO A 401 THR A 523
SITE 2 AC7 5 HOH A 708
SITE 1 AC8 7 HIS B 77 SER B 425 LYS B 427 LEU B 428
SITE 2 AC8 7 PRO B 429 GLU B 443 TYR B 456
SITE 1 AC9 6 PHE A 525 HOH A 744 SER B 368 PHE B 371
SITE 2 AC9 6 HIS B 372 PHE B 525
SITE 1 AD1 5 THR B 284 LEU B 286 PHE B 357 ASN B 397
SITE 2 AD1 5 HOH B 730
SITE 1 AD2 7 GLN B 35 PRO B 37 LEU B 41 LYS B 44
SITE 2 AD2 7 LYS B 45 PRO B 46 GLN B 47
SITE 1 AD3 14 GLY B 116 GLY B 117 GLN B 119 THR B 120
SITE 2 AD3 14 SER B 198 TRP B 231 LEU B 286 SER B 287
SITE 3 AD3 14 PHE B 329 TRP B 430 MET B 437 HIS B 438
SITE 4 AD3 14 TYR B 440 HOH B 720
SITE 1 AD4 2 GLU B 197 HOH B 789
SITE 1 AD5 3 ARG B 42 LYS B 267 PRO B 269
SITE 1 AD6 13 LYS B 323 ASP B 324 GLU B 325 GLY B 326
SITE 2 AD6 13 THR B 327 ARG B 386 GLU B 387 GLY B 390
SITE 3 AD6 13 ASP B 391 GLY B 394 ASP B 395 ILE B 399
SITE 4 AD6 13 HOH B 708
SITE 1 AD7 2 ASN A 17 THR A 24
SITE 1 AD8 2 ILE A 55 ASN A 57
SITE 1 AD9 4 ASN A 106 ASN A 188 LYS A 190 HOH A 710
SITE 1 AE1 5 ASN A 241 ASN A 245 PHE A 278 PRO A 281
SITE 2 AE1 5 FUL B 613
SITE 1 AE2 5 SER A 338 ASN A 341 HOH A 711 HOH A 754
SITE 2 AE2 5 HOH A 759
SITE 1 AE3 7 ASN A 479 ASN A 481 GLU A 482 GLN A 484
SITE 2 AE3 7 HOH A 725 LEU B 88 GLN B 270
SITE 1 AE4 4 ASN A 486 SER A 487 THR A 488 THR A 508
SITE 1 AE5 1 ASN B 17
SITE 1 AE6 2 ARG B 14 ASN B 57
SITE 1 AE7 2 ASN B 106 ASN B 188
SITE 1 AE8 5 TYR B 237 ASN B 241 ASN B 245 LYS B 248
SITE 2 AE8 5 PHE B 278
SITE 1 AE9 2 ASN B 256 GLU B 259
SITE 1 AF1 2 ASN B 341 HOH B 711
SITE 1 AF2 6 ARG A 240 LEU A 244 NAG A 607 LYS B 427
SITE 2 AF2 6 ASP B 454 ASN B 455
SITE 1 AF3 2 TYR B 477 ASN B 481
CRYST1 76.290 80.200 231.350 90.00 90.00 90.00 P 21 21 21 8
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 0.013108 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012469 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004322 0.00000
TER 4211 VAL A 529
TER 8385 VAL B 529
MASTER 580 0 46 49 28 0 47 6 8996 2 491 90
END |