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HEADER HYDROLASE 23-MAY-16 5K5E
TITLE DISCOVERY AND STRUCTURE-ACTIVITY RELATIONSHIPS OF A HIGHLY SELECTIVE
TITLE 2 BUTYRYLCHOLINESTERASE INHIBITOR BY STRUCTURE-BASED VIRTUAL SCREENING
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: INSECT CELL EXPRESSION VECTOR PTIE1;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 266783
KEYWDS HIGH SELECTIVE INHIBITOR, BUTYRYLCHOLINESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.DE LA MORA,S.N.DIGHE,G.S.DEORA,B.P.ROSS,F.NACHON,X.BRAZZOLOTTO
REVDAT 1 27-JUL-16 5K5E 0
SPRSDE 27-JUL-16 5K5E 4AQD
JRNL AUTH S.N.DIGHE,G.S.DEORA,E.DE LA MORA,F.NACHON,S.CHAN,M.O.PARAT,
JRNL AUTH 2 X.BRAZZOLOTTO,B.P.ROSS
JRNL TITL DISCOVERY AND STRUCTURE-ACTIVITY RELATIONSHIPS OF A HIGHLY
JRNL TITL 2 SELECTIVE BUTYRYLCHOLINESTERASE INHIBITOR BY STRUCTURE-BASED
JRNL TITL 3 VIRTUAL SCREENING.
JRNL REF J.MED.CHEM. 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 27405689
JRNL DOI 10.1021/ACS.JMEDCHEM.6B00356
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 35270
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 3257
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 19.9847 - 7.8084 0.98 2701 142 0.1519 0.1737
REMARK 3 2 7.8084 - 6.2604 0.99 2725 141 0.1704 0.1896
REMARK 3 3 6.2604 - 5.4878 0.99 2729 138 0.1677 0.1847
REMARK 3 4 5.4878 - 4.9946 1.00 2727 151 0.1598 0.1468
REMARK 3 5 4.9946 - 4.6414 0.99 2745 134 0.1332 0.1614
REMARK 3 6 4.6414 - 4.3708 0.99 2768 132 0.1239 0.1690
REMARK 3 7 4.3708 - 4.1540 0.98 2702 135 0.1375 0.1688
REMARK 3 8 4.1540 - 3.9746 0.99 2711 151 0.1461 0.1633
REMARK 3 9 3.9746 - 3.8227 0.99 2701 148 0.1548 0.1840
REMARK 3 10 3.8227 - 3.6916 1.00 2778 135 0.1637 0.2084
REMARK 3 11 3.6916 - 3.5769 0.99 2738 137 0.1734 0.2100
REMARK 3 12 3.5769 - 3.4752 0.99 2729 145 0.1787 0.2255
REMARK 3 13 3.4752 - 3.3841 0.99 2757 141 0.2062 0.2482
REMARK 3 14 3.3841 - 3.3019 0.99 2673 140 0.2018 0.2418
REMARK 3 15 3.3019 - 3.2272 0.99 2724 126 0.2100 0.2640
REMARK 3 16 3.2272 - 3.1588 0.99 2684 170 0.2257 0.2275
REMARK 3 17 3.1588 - 3.0958 0.99 2797 138 0.2364 0.2659
REMARK 3 18 3.0958 - 3.0376 1.00 2712 147 0.2408 0.2339
REMARK 3 19 3.0376 - 2.9835 1.00 2771 120 0.2459 0.3191
REMARK 3 20 2.9835 - 2.9331 0.99 2732 147 0.2525 0.3132
REMARK 3 21 2.9331 - 2.8860 1.00 2780 138 0.2821 0.3205
REMARK 3 22 2.8860 - 2.8417 0.99 2684 151 0.2888 0.3258
REMARK 3 23 2.8417 - 2.8000 0.99 2741 150 0.3224 0.3588
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) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 65.70
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 : 0.016 9003
REMARK 3 ANGLE : 1.876 12260
REMARK 3 CHIRALITY : 0.104 1330
REMARK 3 PLANARITY : 0.014 1562
REMARK 3 DIHEDRAL : 20.621 3289
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1721 6.3931 16.6274
REMARK 3 T TENSOR
REMARK 3 T11: 0.4027 T22: 0.4355
REMARK 3 T33: 0.3209 T12: 0.0592
REMARK 3 T13: -0.0202 T23: -0.0205
REMARK 3 L TENSOR
REMARK 3 L11: 2.7075 L22: 2.3814
REMARK 3 L33: 3.2033 L12: -0.2432
REMARK 3 L13: 0.6497 L23: -0.7368
REMARK 3 S TENSOR
REMARK 3 S11: 0.1721 S12: 0.4288 S13: -0.1253
REMARK 3 S21: -0.1047 S22: -0.1587 S23: -0.1294
REMARK 3 S31: 0.1159 S32: 0.2632 S33: -0.0135
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8698 -30.3107 44.4069
REMARK 3 T TENSOR
REMARK 3 T11: 0.4425 T22: 0.4127
REMARK 3 T33: 0.3572 T12: -0.0314
REMARK 3 T13: -0.0200 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 2.2674 L22: 3.6097
REMARK 3 L33: 3.8495 L12: -0.4294
REMARK 3 L13: 0.8248 L23: 0.2288
REMARK 3 S TENSOR
REMARK 3 S11: 0.1000 S12: 0.0719 S13: -0.2138
REMARK 3 S21: 0.1058 S22: 0.0927 S23: 0.0612
REMARK 3 S31: 0.4064 S32: -0.1270 S33: -0.1782
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 5K5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221789.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-15
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 : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35273
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 9.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.68000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
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: 4AQD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM ACETATE PH 7.4, 13%
REMARK 280 POLYETHYLENGLYCOL 3350, VAPOR DIFFUSION, 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 37.90500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.31500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.03500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.31500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.90500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.03500
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: 6770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 59.0 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 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
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 OE1 GLU B 161 NH2 ARG B 265 1.59
REMARK 500 CD LYS A 348 NE2 GLN A 351 1.61
REMARK 500 CG LYS A 348 NE2 GLN A 351 1.68
REMARK 500 CE LYS B 12 O ASP B 54 1.71
REMARK 500 O VAL B 20 CZ ARG B 135 1.77
REMARK 500 CD LYS A 348 CD GLN A 351 1.79
REMARK 500 OE1 GLN B 223 CZ3 TRP B 471 1.80
REMARK 500 CG LYS B 12 CD1 ILE B 55 1.83
REMARK 500 OE2 GLU B 137 CG LYS B 469 1.85
REMARK 500 OD1 ASN B 57 C1 NAG B 602 1.87
REMARK 500 CG2 THR B 483 N2 NAG B 608 1.88
REMARK 500 OD1 ASN A 57 C1 NAG A 602 1.88
REMARK 500 CB PHE B 21 NH1 ARG B 135 1.92
REMARK 500 N GLY B 23 NH2 ARG B 135 1.92
REMARK 500 CE LYS B 12 CD1 ILE B 55 1.94
REMARK 500 OG1 THR A 8 O GLY A 11 1.95
REMARK 500 CD LYS A 348 OE1 GLN A 351 1.96
REMARK 500 NZ LYS B 12 O ASP B 54 1.96
REMARK 500 OE1 GLU B 422 OG1 THR B 502 1.97
REMARK 500 O VAL B 20 NE ARG B 135 1.98
REMARK 500 CD LYS B 12 O ASP B 54 1.99
REMARK 500 OD2 ASP A 268 OE1 GLN A 270 2.03
REMARK 500 NZ LYS B 44 OE2 GLU B 161 2.03
REMARK 500 OE1 GLU A 137 NZ LYS A 469 2.03
REMARK 500 ND2 ASN A 57 C1 NAG A 602 2.04
REMARK 500 O LEU B 463 OG SER B 466 2.06
REMARK 500 OG SER B 198 O HOH B 701 2.07
REMARK 500 O THR B 250 NZ LYS B 267 2.09
REMARK 500 CB THR A 258 NZ LYS A 262 2.10
REMARK 500 OG SER A 198 O HOH A 701 2.11
REMARK 500 ND2 ASN A 106 O5 NAG A 603 2.12
REMARK 500 NH1 ARG B 240 OE2 GLU B 257 2.15
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 ND2 ASN B 455 1565 1.11
REMARK 500 OH TYR A 237 CG ASN B 455 1565 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 497 CD GLU B 497 OE1 -0.070
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 LYS A 348 C - N - CA ANGL. DEV. = -30.0 DEGREES
REMARK 500 LYS A 348 O - C - N ANGL. DEV. = -22.9 DEGREES
REMARK 500 SER A 466 O - C - N ANGL. DEV. = -11.3 DEGREES
REMARK 500 ASN A 485 C - N - CA ANGL. DEV. = -28.8 DEGREES
REMARK 500 ASN A 485 O - C - N ANGL. DEV. = -30.3 DEGREES
REMARK 500 ASN B 10 C - N - CA ANGL. DEV. = -19.8 DEGREES
REMARK 500 ASN B 10 CA - C - N ANGL. DEV. = -23.7 DEGREES
REMARK 500 SER B 53 C - N - CA ANGL. DEV. = -26.6 DEGREES
REMARK 500 SER B 53 CA - C - N ANGL. DEV. = -31.2 DEGREES
REMARK 500 GLU B 161 C - N - CA ANGL. DEV. = -27.9 DEGREES
REMARK 500 ARG B 240 C - N - CA ANGL. DEV. = -17.5 DEGREES
REMARK 500 GLU B 255 O - C - N ANGL. DEV. = -11.8 DEGREES
REMARK 500 LYS B 348 O - C - N ANGL. DEV. = -11.7 DEGREES
REMARK 500 THR B 483 C - N - CA ANGL. DEV. = -26.4 DEGREES
REMARK 500 THR B 483 O - C - N ANGL. DEV. = -24.1 DEGREES
REMARK 500 ASN B 485 C - N - CA ANGL. DEV. = -27.6 DEGREES
REMARK 500 ASN B 485 O - C - N ANGL. DEV. = -20.0 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 THR A 50 -83.89 -104.39
REMARK 500 ASP A 70 109.32 -49.31
REMARK 500 PHE A 118 12.73 56.54
REMARK 500 PHE A 153 15.12 -140.26
REMARK 500 SER A 198 -129.28 57.01
REMARK 500 SER A 226 148.16 -171.05
REMARK 500 TYR A 282 -127.41 56.71
REMARK 500 PRO A 285 -9.77 -59.21
REMARK 500 ASP A 297 -70.36 -124.00
REMARK 500 LYS A 339 -17.21 -48.77
REMARK 500 PHE A 398 -54.85 -130.30
REMARK 500 GLU A 482 -66.07 -91.25
REMARK 500 SER A 507 125.76 -171.19
REMARK 500 LYS B 12 116.61 -163.58
REMARK 500 PHE B 43 -3.60 86.67
REMARK 500 ASP B 54 -160.02 -162.13
REMARK 500 CYS B 92 -1.88 -142.81
REMARK 500 PHE B 118 10.44 51.81
REMARK 500 SER B 198 -123.91 59.43
REMARK 500 ASN B 266 36.21 -98.50
REMARK 500 TYR B 282 76.57 -115.09
REMARK 500 ASP B 297 -77.68 -119.82
REMARK 500 ASP B 301 -169.76 -124.49
REMARK 500 ASP B 324 56.26 -118.70
REMARK 500 ARG B 381 118.46 -34.51
REMARK 500 GLU B 383 26.91 -75.14
REMARK 500 PHE B 398 -57.26 -130.25
REMARK 500 GLU B 411 27.03 -79.98
REMARK 500 ASN B 455 6.25 90.20
REMARK 500 PRO B 480 38.11 -81.02
REMARK 500 PHE B 525 -57.02 -125.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 348 GLU A 349 124.57
REMARK 500 LYS B 9 ASN B 10 141.67
REMARK 500 ASN B 485 ASN B 486 139.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 TYR A 237 14.92
REMARK 500 LYS A 348 -32.19
REMARK 500 SER A 466 -11.53
REMARK 500 ASN A 485 -34.73
REMARK 500 ASN B 10 -20.53
REMARK 500 SER B 53 -20.51
REMARK 500 ARG B 240 -13.20
REMARK 500 GLU B 255 -14.28
REMARK 500 LYS B 348 -12.12
REMARK 500 THR B 483 -31.36
REMARK 500 ASN B 485 -29.17
REMARK 500
REMARK 500 REMARK: NULL
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 NAG A 602
REMARK 610 NAG B 602
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6QS A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6QS B 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound
REMARK 800 to ASN A 17
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 603 through NAG A 604 bound to ASN A 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 605 bound
REMARK 800 to ASN A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 606 bound
REMARK 800 to ASN A 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A
REMARK 800 607 through NAG A 608 bound to ASN A 481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
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: AD7
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: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound
REMARK 800 to ASN B 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 605 bound
REMARK 800 to ASN B 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B
REMARK 800 606 through NAG B 607 bound to ASN B 341
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 608 bound
REMARK 800 to ASN B 481
DBREF 5K5E A 1 529 UNP P06276 CHLE_HUMAN 29 557
DBREF 5K5E B 1 529 UNP P06276 CHLE_HUMAN 29 557
SEQRES 1 A 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 529 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 529 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 A 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 A 529 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 529 PHE TRP THR SER PHE PHE PRO LYS VAL
SEQRES 1 B 529 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 B 529 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 B 529 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 B 529 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 B 529 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 B 529 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 B 529 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 B 529 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 B 529 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 B 529 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 B 529 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 B 529 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 B 529 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 B 529 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 B 529 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 B 529 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 B 529 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 B 529 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 B 529 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 B 529 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 B 529 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 B 529 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 B 529 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 B 529 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 B 529 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 B 529 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 B 529 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 B 529 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 B 529 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 B 529 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 B 529 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 B 529 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 B 529 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 B 529 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 B 529 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 B 529 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 B 529 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 B 529 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 B 529 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 B 529 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 B 529 PHE TRP THR SER PHE PHE PRO LYS VAL
HET NAG A 601 14
HET NAG A 602 14
HET NAG A 603 14
HET NAG A 604 14
HET NAG A 605 14
HET NAG A 606 14
HET NAG A 607 14
HET NAG A 608 14
HET 6QS A 609 36
HET EDO A 610 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 NAG B 606 14
HET NAG B 607 14
HET NAG B 608 14
HET 6QS B 609 36
HET EDO B 610 4
HET EDO B 611 4
HET GOL B 612 6
HET GOL B 613 6
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM 6QS [(2~{R})-OXOLAN-2-YL]METHYL 4-(9-ETHYLCARBAZOL-3-YL)-2-
HETNAM 2 6QS METHYL-5-OXIDANYLIDENE-4,6,7,8-TETRAHYDRO-1~{H}-
HETNAM 3 6QS QUINOLINE-3-CARBOXYLATE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 16(C8 H15 N O6)
FORMUL 9 6QS 2(C30 H32 N2 O4)
FORMUL 10 EDO 3(C2 H6 O2)
FORMUL 21 GOL 2(C3 H8 O3)
FORMUL 23 HOH *127(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 VAL A 148 LEU A 154 1 7
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 PRO A 211 PHE A 217 5 7
HELIX 10 AB1 SER A 235 GLY A 251 1 17
HELIX 11 AB2 ASN A 256 ASN A 266 1 11
HELIX 12 AB3 ASP A 268 ALA A 277 1 10
HELIX 13 AB4 PHE A 278 VAL A 280 5 3
HELIX 14 AB5 MET A 302 GLY A 310 1 9
HELIX 15 AB6 GLY A 326 VAL A 331 1 6
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 GLU A 451 5 5
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 ALA B 183 PHE B 185 5 3
HELIX 33 AD6 SER B 198 LEU B 208 1 11
HELIX 34 AD7 SER B 210 PHE B 217 5 8
HELIX 35 AD8 SER B 235 THR B 250 1 16
HELIX 36 AD9 ASN B 256 ASN B 266 1 11
HELIX 37 AE1 ASP B 268 ALA B 277 1 10
HELIX 38 AE2 MET B 302 GLY B 310 1 9
HELIX 39 AE3 GLY B 326 TYR B 332 5 7
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 PHE B 446 1 6
HELIX 46 AF1 GLY B 447 GLU B 451 5 5
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 VAL A 20 0
SHEET 2 AA211 GLY A 23 PRO A 32 -1 O ALA A 27 N MET A 16
SHEET 3 AA211 TYR A 94 PRO A 100 -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 TRP A 112 O VAL A 142
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 ILE A 221 N LEU A 194
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 421 N VAL A 321
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 TRP B 56 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 LEU B 95 N ILE B 31
SHEET 4 AA411 ILE B 140 MET B 144 -1 O VAL B 141 N TRP B 98
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 PHE B 195 N ILE B 111
SHEET 7 AA411 ARG B 219 GLN B 223 1 O ILE B 221 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 417 N VAL B 319
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
SHEET 1 AA5 2 SER B 64 CYS B 65 0
SHEET 2 AA5 2 LEU B 88 SER B 89 1 O SER B 89 N SER B 64
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.03
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.05
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.06
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.03
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.05
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.06
LINK ND2 ASN A 17 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 106 C1 NAG A 603 1555 1555 1.38
LINK ND2 ASN A 241 C1 NAG A 605 1555 1555 1.45
LINK ND2 ASN A 341 C1 NAG A 606 1555 1555 1.46
LINK ND2 ASN A 481 C1 NAG A 607 1555 1555 1.44
LINK ND2 ASN B 17 C1 NAG B 601 1555 1555 1.44
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 605 1555 1555 1.45
LINK ND2 ASN B 341 C1 NAG B 606 1555 1555 1.45
LINK ND2 ASN B 481 C1 NAG B 608 1555 1555 1.46
LINK O4 NAG A 603 C1 NAG A 604 1555 1555 1.44
LINK O4 NAG A 607 C1 NAG A 608 1555 1555 1.44
LINK O4 NAG B 606 C1 NAG B 607 1555 1555 1.45
LINK CZ TYR A 237 ND2 ASN B 455 1555 1565 1.57
CISPEP 1 ALA A 101 PRO A 102 0 -0.75
CISPEP 2 ALA B 101 PRO B 102 0 2.09
SITE 1 AC1 2 ARG A 14 ASN A 57
SITE 1 AC2 14 TRP A 82 GLY A 115 GLY A 116 GLY A 117
SITE 2 AC2 14 GLU A 197 SER A 198 PRO A 285 SER A 287
SITE 3 AC2 14 ALA A 328 PHE A 398 HIS A 438 HOH A 701
SITE 4 AC2 14 HOH A 731 HOH A 749
SITE 1 AC3 2 TYR A 396 PRO A 401
SITE 1 AC4 2 ARG B 14 ASN B 57
SITE 1 AC5 12 TRP B 82 GLY B 115 GLY B 116 GLY B 117
SITE 2 AC5 12 GLU B 197 SER B 198 PRO B 285 SER B 287
SITE 3 AC5 12 ALA B 328 PHE B 329 TYR B 332 HIS B 438
SITE 1 AC6 2 HIS B 77 GLU B 443
SITE 1 AC7 2 ASN B 245 PHE B 278
SITE 1 AC8 4 TYR B 61 TRP B 98 ASP B 129 LYS B 131
SITE 1 AC9 5 GLU A 411 TRP A 412 LYS B 248 GLY B 251
SITE 2 AC9 5 SER B 253
SITE 1 AD1 3 ILE A 4 ASN A 17 THR A 24
SITE 1 AD2 2 ASN A 106 ASN A 188
SITE 1 AD3 3 GLU A 238 ASN A 241 ASN A 245
SITE 1 AD4 2 SER A 338 ASN A 341
SITE 1 AD5 7 ASN A 473 TYR A 477 ASN A 481 GLU A 482
SITE 2 AD5 7 ASP B 87 LEU B 88 GLN B 270
SITE 1 AD6 3 ILE B 4 ASN B 17 THR B 24
SITE 1 AD7 2 ASN B 106 ASN B 188
SITE 1 AD8 3 ASN B 241 ASN B 245 PRO B 281
SITE 1 AD9 1 ASN B 256
SITE 1 AE1 3 GLY B 336 SER B 338 ASN B 341
SITE 1 AE2 3 ASN B 481 GLU B 482 THR B 483
CRYST1 75.810 80.070 230.630 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 0.013191 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012489 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004336 0.00000
TER 4216 VAL A 529
TER 8417 VAL B 529
MASTER 557 0 23 49 30 0 27 6 8837 2 343 82
END |