HEADER TRANSFERASE/TRANSFERASE INHIBITOR 06-JAN-16 5HEX
TITLE CRYSTAL STRUCTURE OF HUMAN HEXOKINASE 2 WITH CMPD 30, A 2-AMINO-6-
TITLE 2 BENZENESULFONAMIDE GLUCOSAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEXOKINASE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HEXOKINASE TYPE II,HK II,MUSCLE FORM HEXOKINASE;
COMPND 5 EC: 2.7.1.1;
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: HK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28LIC.H6.TEV.HUHK2
KEYWDS INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.CAMPOBASSO,B.ZHAO,A.SMALLWOOD
REVDAT 3 06-MAR-24 5HEX 1 HETSYN
REVDAT 2 29-JUL-20 5HEX 1 COMPND REMARK HETNAM SITE
REVDAT 2 2 1 ATOM
REVDAT 1 30-MAR-16 5HEX 0
JRNL AUTH H.LIN,J.ZENG,R.XIE,M.J.SCHULZ,R.TEDESCO,J.QU,K.F.ERHARD,
JRNL AUTH 2 J.F.MACK,K.RAHA,A.R.RENDINA,L.M.SZEWCZUK,P.M.KRATZ,
JRNL AUTH 3 A.J.JUREWICZ,T.CECCONIE,S.MARTENS,P.J.MCDEVITT,J.D.MARTIN,
JRNL AUTH 4 S.B.CHEN,Y.JIANG,L.NICKELS,B.J.SCHWARTZ,A.SMALLWOOD,B.ZHAO,
JRNL AUTH 5 N.CAMPOBASSO,Y.QIAN,J.BRIAND,C.M.ROMINGER,C.OLEYKOWSKI,
JRNL AUTH 6 M.A.HARDWICKE,J.I.LUENGO
JRNL TITL DISCOVERY OF A NOVEL 2,6-DISUBSTITUTED GLUCOSAMINE SERIES OF
JRNL TITL 2 POTENT AND SELECTIVE HEXOKINASE 2 INHIBITORS.
JRNL REF ACS MED.CHEM.LETT. V. 7 217 2016
JRNL REFN ISSN 1948-5875
JRNL PMID 26985301
JRNL DOI 10.1021/ACSMEDCHEMLETT.5B00214
REMARK 2
REMARK 2 RESOLUTION. 2.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_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) : 2.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 114.12
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 59830
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 2918
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
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) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.150
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 : 0.009 13964
REMARK 3 ANGLE : 1.205 18826
REMARK 3 CHIRALITY : 0.060 2112
REMARK 3 PLANARITY : 0.007 2461
REMARK 3 DIHEDRAL : 13.915 8376
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 5HEX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216838.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5 - 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59924
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.730
REMARK 200 RESOLUTION RANGE LOW (A) : 114.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.42000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN CONDITIONS: 10MGS/ML, 50MM
REMARK 280 TRIS HCL, PH 7.5, 250MM NACL, 2MM DTT, 2MM MGCL2. AND 1MM CMPD30
REMARK 280 RESERVOIR: 0.1M NA CITRATE PH=5, 14% PEG 3350, 10 % ETHYLENE
REMARK 280 GLYCOL CRYO PROTECTANT 20% ETHYLENE GLYCOL IN MOTHER LIQUOR, PH
REMARK 280 5, VAPOR DIFFUSION, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 77.44650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 GLY A 7
REMARK 465 LEU A 8
REMARK 465 GLU A 9
REMARK 465 ASN A 10
REMARK 465 LEU A 11
REMARK 465 TYR A 12
REMARK 465 PHE A 13
REMARK 465 GLN A 14
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 MET A 119
REMARK 465 ARG A 120
REMARK 465 GLY A 121
REMARK 465 SER A 170
REMARK 465 TRP A 171
REMARK 465 THR A 172
REMARK 465 LYS A 173
REMARK 465 GLY A 174
REMARK 465 PHE A 175
REMARK 465 LYS A 176
REMARK 465 SER A 177
REMARK 465 SER A 178
REMARK 465 GLY A 179
REMARK 465 VAL A 180
REMARK 465 GLU A 181
REMARK 465 ARG A 912
REMARK 465 GLU A 913
REMARK 465 ALA A 914
REMARK 465 GLY A 915
REMARK 465 GLN A 916
REMARK 465 ARG A 917
REMARK 465 MET B -5
REMARK 465 GLY B -4
REMARK 465 SER B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 HIS B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 GLY B 7
REMARK 465 LEU B 8
REMARK 465 GLU B 9
REMARK 465 ASN B 10
REMARK 465 LEU B 11
REMARK 465 TYR B 12
REMARK 465 PHE B 13
REMARK 465 GLN B 14
REMARK 465 GLY B 15
REMARK 465 SER B 16
REMARK 465 TRP B 171
REMARK 465 THR B 172
REMARK 465 LYS B 173
REMARK 465 GLY B 174
REMARK 465 PHE B 175
REMARK 465 LYS B 176
REMARK 465 ALA B 914
REMARK 465 GLY B 915
REMARK 465 GLN B 916
REMARK 465 ARG B 917
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 THR A 88 OG1 CG2
REMARK 470 ASN A 89 CG OD1 ND2
REMARK 470 ILE A 114 CG1 CG2 CD1
REMARK 470 GLU A 116 CG CD OE1 OE2
REMARK 470 ILE A 118 CG1 CG2 CD1
REMARK 470 GLU A 132 CG CD OE1 OE2
REMARK 470 ASN A 136 CG OD1 ND2
REMARK 470 VAL A 169 CG1 CG2
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 GLN A 279 OE1 NE2
REMARK 470 GLU A 345 CG CD OE1 OE2
REMARK 470 GLN A 365 CG CD OE1 NE2
REMARK 470 GLU A 366 CG CD OE1 OE2
REMARK 470 GLU A 404 CG CD OE1 OE2
REMARK 470 LYS A 472 CG CD CE NZ
REMARK 470 LYS A 501 CD CE NZ
REMARK 470 LYS A 525 CG CD CE NZ
REMARK 470 ILE A 562 CG1 CG2 CD1
REMARK 470 GLU A 565 CG CD OE1 OE2
REMARK 470 LYS A 592 CB CG CD CE NZ
REMARK 470 LYS A 624 CG CD CE NZ
REMARK 470 ASP A 648 CG OD1 OD2
REMARK 470 LEU A 649 CD1 CD2
REMARK 470 GLU A 668 CG CD OE1 OE2
REMARK 470 GLU A 697 CG CD OE1 OE2
REMARK 470 GLU A 774 OE1 OE2
REMARK 470 LYS A 855 NZ
REMARK 470 LYS A 873 CD CE NZ
REMARK 470 LYS A 880 NZ
REMARK 470 LYS B 21 CD CE NZ
REMARK 470 LYS B 41 CD CE NZ
REMARK 470 LYS B 45 CD CE NZ
REMARK 470 GLU B 116 CG CD OE1 OE2
REMARK 470 ARG B 120 CG CD NE CZ NH1 NH2
REMARK 470 SER B 177 OG
REMARK 470 SER B 178 OG
REMARK 470 LYS B 346 CD CE NZ
REMARK 470 GLU B 404 CG CD OE1 OE2
REMARK 470 LYS B 425 CD CE NZ
REMARK 470 LYS B 472 CG CD CE NZ
REMARK 470 THR B 536 OG1 CG2
REMARK 470 ASN B 537 CG OD1 ND2
REMARK 470 ARG B 544 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 549 CD CE NZ
REMARK 470 GLU B 587 CG CD OE1 OE2
REMARK 470 LYS B 592 CB CG CD CE NZ
REMARK 470 LYS B 624 CG CD CE NZ
REMARK 470 GLU B 668 CG CD OE1 OE2
REMARK 470 GLU B 697 OE1 OE2
REMARK 470 GLU B 700 CG CD OE1 OE2
REMARK 470 ARG B 769 NE CZ NH1 NH2
REMARK 470 ARG B 771 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 805 CD OE1 NE2
REMARK 470 GLU B 810 CG CD OE1 OE2
REMARK 470 LYS B 873 CD CE NZ
REMARK 470 LYS B 880 NZ
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 OH TYR A 27 OE2 GLU B 399 2.08
REMARK 500 O ASP A 793 NZ LYS A 820 2.09
REMARK 500 NH1 ARG B 274 O HOH B 1101 2.11
REMARK 500 OE1 GLU B 240 NH1 ARG B 396 2.17
REMARK 500 OH TYR A 865 NE2 HIS A 876 2.19
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 CYS A 386 CB CYS A 386 SG -0.122
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 PHE A 423 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 846 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 846 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 GLU B 645 N - CA - C ANGL. DEV. = 17.0 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 88 -14.81 65.64
REMARK 500 GLN A 142 -12.03 87.96
REMARK 500 GLU A 165 148.83 173.60
REMARK 500 ASP A 198 -70.77 -54.30
REMARK 500 ASP A 202 -159.83 -91.22
REMARK 500 TRP A 550 -135.23 58.27
REMARK 500 LEU A 617 -71.82 -92.93
REMARK 500 LYS A 621 -1.02 65.45
REMARK 500 GLU A 645 -31.75 73.87
REMARK 500 PHE A 647 -71.83 -76.15
REMARK 500 ASP A 648 74.30 50.20
REMARK 500 LEU A 795 -117.20 56.13
REMARK 500 ASP A 852 -72.95 -121.14
REMARK 500 SER A 893 -64.38 -122.91
REMARK 500 GLU A 894 -145.17 51.04
REMARK 500 ASP A 895 -3.22 62.35
REMARK 500 SER A 897 -114.15 60.64
REMARK 500 ASP B 164 79.37 -107.80
REMARK 500 ASP B 202 -153.03 -94.95
REMARK 500 TYR B 515 19.43 59.09
REMARK 500 LYS B 549 -35.48 72.50
REMARK 500 LYS B 621 -41.76 69.85
REMARK 500 PHE B 647 -42.13 -152.39
REMARK 500 ASP B 648 145.84 -37.10
REMARK 500 LEU B 795 -114.69 50.86
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 THR A 523 GLU A 524 -148.57
REMARK 500 GLU A 646 PHE A 647 -134.78
REMARK 500 GLY B 622 PHE B 623 -140.74
REMARK 500 ARG B 644 GLU B 645 -126.84
REMARK 500 GLU B 645 GLU B 646 121.14
REMARK 500 PHE B 647 ASP B 648 -135.43
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 610 604 B 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5HFU RELATED DB: PDB
DBREF 5HEX A 17 917 UNP P52789 HXK2_HUMAN 17 917
DBREF 5HEX B 17 917 UNP P52789 HXK2_HUMAN 17 917
SEQADV 5HEX MET A -5 UNP P52789 INITIATING METHIONINE
SEQADV 5HEX GLY A -4 UNP P52789 EXPRESSION TAG
SEQADV 5HEX SER A -3 UNP P52789 EXPRESSION TAG
SEQADV 5HEX SER A -2 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS A -1 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS A 0 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS A 1 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS A 2 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS A 3 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS A 4 UNP P52789 EXPRESSION TAG
SEQADV 5HEX SER A 5 UNP P52789 EXPRESSION TAG
SEQADV 5HEX SER A 6 UNP P52789 EXPRESSION TAG
SEQADV 5HEX GLY A 7 UNP P52789 EXPRESSION TAG
SEQADV 5HEX LEU A 8 UNP P52789 EXPRESSION TAG
SEQADV 5HEX GLU A 9 UNP P52789 EXPRESSION TAG
SEQADV 5HEX ASN A 10 UNP P52789 EXPRESSION TAG
SEQADV 5HEX LEU A 11 UNP P52789 EXPRESSION TAG
SEQADV 5HEX TYR A 12 UNP P52789 EXPRESSION TAG
SEQADV 5HEX PHE A 13 UNP P52789 EXPRESSION TAG
SEQADV 5HEX GLN A 14 UNP P52789 EXPRESSION TAG
SEQADV 5HEX GLY A 15 UNP P52789 EXPRESSION TAG
SEQADV 5HEX SER A 16 UNP P52789 EXPRESSION TAG
SEQADV 5HEX MET B -5 UNP P52789 INITIATING METHIONINE
SEQADV 5HEX GLY B -4 UNP P52789 EXPRESSION TAG
SEQADV 5HEX SER B -3 UNP P52789 EXPRESSION TAG
SEQADV 5HEX SER B -2 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS B -1 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS B 0 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS B 1 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS B 2 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS B 3 UNP P52789 EXPRESSION TAG
SEQADV 5HEX HIS B 4 UNP P52789 EXPRESSION TAG
SEQADV 5HEX SER B 5 UNP P52789 EXPRESSION TAG
SEQADV 5HEX SER B 6 UNP P52789 EXPRESSION TAG
SEQADV 5HEX GLY B 7 UNP P52789 EXPRESSION TAG
SEQADV 5HEX LEU B 8 UNP P52789 EXPRESSION TAG
SEQADV 5HEX GLU B 9 UNP P52789 EXPRESSION TAG
SEQADV 5HEX ASN B 10 UNP P52789 EXPRESSION TAG
SEQADV 5HEX LEU B 11 UNP P52789 EXPRESSION TAG
SEQADV 5HEX TYR B 12 UNP P52789 EXPRESSION TAG
SEQADV 5HEX PHE B 13 UNP P52789 EXPRESSION TAG
SEQADV 5HEX GLN B 14 UNP P52789 EXPRESSION TAG
SEQADV 5HEX GLY B 15 UNP P52789 EXPRESSION TAG
SEQADV 5HEX SER B 16 UNP P52789 EXPRESSION TAG
SEQRES 1 A 923 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 923 LEU GLU ASN LEU TYR PHE GLN GLY SER ASP GLN VAL GLN
SEQRES 3 A 923 LYS VAL ASP GLN TYR LEU TYR HIS MET ARG LEU SER ASP
SEQRES 4 A 923 GLU THR LEU LEU GLU ILE SER LYS ARG PHE ARG LYS GLU
SEQRES 5 A 923 MET GLU LYS GLY LEU GLY ALA THR THR HIS PRO THR ALA
SEQRES 6 A 923 ALA VAL LYS MET LEU PRO THR PHE VAL ARG SER THR PRO
SEQRES 7 A 923 ASP GLY THR GLU HIS GLY GLU PHE LEU ALA LEU ASP LEU
SEQRES 8 A 923 GLY GLY THR ASN PHE ARG VAL LEU TRP VAL LYS VAL THR
SEQRES 9 A 923 ASP ASN GLY LEU GLN LYS VAL GLU MET GLU ASN GLN ILE
SEQRES 10 A 923 TYR ALA ILE PRO GLU ASP ILE MET ARG GLY SER GLY THR
SEQRES 11 A 923 GLN LEU PHE ASP HIS ILE ALA GLU CYS LEU ALA ASN PHE
SEQRES 12 A 923 MET ASP LYS LEU GLN ILE LYS ASP LYS LYS LEU PRO LEU
SEQRES 13 A 923 GLY PHE THR PHE SER PHE PRO CYS HIS GLN THR LYS LEU
SEQRES 14 A 923 ASP GLU SER PHE LEU VAL SER TRP THR LYS GLY PHE LYS
SEQRES 15 A 923 SER SER GLY VAL GLU GLY ARG ASP VAL VAL ALA LEU ILE
SEQRES 16 A 923 ARG LYS ALA ILE GLN ARG ARG GLY ASP PHE ASP ILE ASP
SEQRES 17 A 923 ILE VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET
SEQRES 18 A 923 THR CYS GLY TYR ASP ASP HIS ASN CYS GLU ILE GLY LEU
SEQRES 19 A 923 ILE VAL GLY THR GLY SER ASN ALA CYS TYR MET GLU GLU
SEQRES 20 A 923 MET ARG HIS ILE ASP MET VAL GLU GLY ASP GLU GLY ARG
SEQRES 21 A 923 MET CYS ILE ASN MET GLU TRP GLY ALA PHE GLY ASP ASP
SEQRES 22 A 923 GLY SER LEU ASN ASP ILE ARG THR GLU PHE ASP GLN GLU
SEQRES 23 A 923 ILE ASP MET GLY SER LEU ASN PRO GLY LYS GLN LEU PHE
SEQRES 24 A 923 GLU LYS MET ILE SER GLY MET TYR MET GLY GLU LEU VAL
SEQRES 25 A 923 ARG LEU ILE LEU VAL LYS MET ALA LYS GLU GLU LEU LEU
SEQRES 26 A 923 PHE GLY GLY LYS LEU SER PRO GLU LEU LEU ASN THR GLY
SEQRES 27 A 923 ARG PHE GLU THR LYS ASP ILE SER ASP ILE GLU GLY GLU
SEQRES 28 A 923 LYS ASP GLY ILE ARG LYS ALA ARG GLU VAL LEU MET ARG
SEQRES 29 A 923 LEU GLY LEU ASP PRO THR GLN GLU ASP CYS VAL ALA THR
SEQRES 30 A 923 HIS ARG ILE CYS GLN ILE VAL SER THR ARG SER ALA SER
SEQRES 31 A 923 LEU CYS ALA ALA THR LEU ALA ALA VAL LEU GLN ARG ILE
SEQRES 32 A 923 LYS GLU ASN LYS GLY GLU GLU ARG LEU ARG SER THR ILE
SEQRES 33 A 923 GLY VAL ASP GLY SER VAL TYR LYS LYS HIS PRO HIS PHE
SEQRES 34 A 923 ALA LYS ARG LEU HIS LYS THR VAL ARG ARG LEU VAL PRO
SEQRES 35 A 923 GLY CYS ASP VAL ARG PHE LEU ARG SER GLU ASP GLY SER
SEQRES 36 A 923 GLY LYS GLY ALA ALA MET VAL THR ALA VAL ALA TYR ARG
SEQRES 37 A 923 LEU ALA ASP GLN HIS ARG ALA ARG GLN LYS THR LEU GLU
SEQRES 38 A 923 HIS LEU GLN LEU SER HIS ASP GLN LEU LEU GLU VAL LYS
SEQRES 39 A 923 ARG ARG MET LYS VAL GLU MET GLU ARG GLY LEU SER LYS
SEQRES 40 A 923 GLU THR HIS ALA SER ALA PRO VAL LYS MET LEU PRO THR
SEQRES 41 A 923 TYR VAL CYS ALA THR PRO ASP GLY THR GLU LYS GLY ASP
SEQRES 42 A 923 PHE LEU ALA LEU ASP LEU GLY GLY THR ASN PHE ARG VAL
SEQRES 43 A 923 LEU LEU VAL ARG VAL ARG ASN GLY LYS TRP GLY GLY VAL
SEQRES 44 A 923 GLU MET HIS ASN LYS ILE TYR ALA ILE PRO GLN GLU VAL
SEQRES 45 A 923 MET HIS GLY THR GLY ASP GLU LEU PHE ASP HIS ILE VAL
SEQRES 46 A 923 GLN CYS ILE ALA ASP PHE LEU GLU TYR MET GLY MET LYS
SEQRES 47 A 923 GLY VAL SER LEU PRO LEU GLY PHE THR PHE SER PHE PRO
SEQRES 48 A 923 CYS GLN GLN ASN SER LEU ASP GLU SER ILE LEU LEU LYS
SEQRES 49 A 923 TRP THR LYS GLY PHE LYS ALA SER GLY CYS GLU GLY GLU
SEQRES 50 A 923 ASP VAL VAL THR LEU LEU LYS GLU ALA ILE HIS ARG ARG
SEQRES 51 A 923 GLU GLU PHE ASP LEU ASP VAL VAL ALA VAL VAL ASN ASP
SEQRES 52 A 923 THR VAL GLY THR MET MET THR CYS GLY PHE GLU ASP PRO
SEQRES 53 A 923 HIS CYS GLU VAL GLY LEU ILE VAL GLY THR GLY SER ASN
SEQRES 54 A 923 ALA CYS TYR MET GLU GLU MET ARG ASN VAL GLU LEU VAL
SEQRES 55 A 923 GLU GLY GLU GLU GLY ARG MET CYS VAL ASN MET GLU TRP
SEQRES 56 A 923 GLY ALA PHE GLY ASP ASN GLY CYS LEU ASP ASP PHE ARG
SEQRES 57 A 923 THR GLU PHE ASP VAL ALA VAL ASP GLU LEU SER LEU ASN
SEQRES 58 A 923 PRO GLY LYS GLN ARG PHE GLU LYS MET ILE SER GLY MET
SEQRES 59 A 923 TYR LEU GLY GLU ILE VAL ARG ASN ILE LEU ILE ASP PHE
SEQRES 60 A 923 THR LYS ARG GLY LEU LEU PHE ARG GLY ARG ILE SER GLU
SEQRES 61 A 923 ARG LEU LYS THR ARG GLY ILE PHE GLU THR LYS PHE LEU
SEQRES 62 A 923 SER GLN ILE GLU SER ASP CYS LEU ALA LEU LEU GLN VAL
SEQRES 63 A 923 ARG ALA ILE LEU GLN HIS LEU GLY LEU GLU SER THR CYS
SEQRES 64 A 923 ASP ASP SER ILE ILE VAL LYS GLU VAL CYS THR VAL VAL
SEQRES 65 A 923 ALA ARG ARG ALA ALA GLN LEU CYS GLY ALA GLY MET ALA
SEQRES 66 A 923 ALA VAL VAL ASP ARG ILE ARG GLU ASN ARG GLY LEU ASP
SEQRES 67 A 923 ALA LEU LYS VAL THR VAL GLY VAL ASP GLY THR LEU TYR
SEQRES 68 A 923 LYS LEU HIS PRO HIS PHE ALA LYS VAL MET HIS GLU THR
SEQRES 69 A 923 VAL LYS ASP LEU ALA PRO LYS CYS ASP VAL SER PHE LEU
SEQRES 70 A 923 GLN SER GLU ASP GLY SER GLY LYS GLY ALA ALA LEU ILE
SEQRES 71 A 923 THR ALA VAL ALA CYS ARG ILE ARG GLU ALA GLY GLN ARG
SEQRES 1 B 923 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 923 LEU GLU ASN LEU TYR PHE GLN GLY SER ASP GLN VAL GLN
SEQRES 3 B 923 LYS VAL ASP GLN TYR LEU TYR HIS MET ARG LEU SER ASP
SEQRES 4 B 923 GLU THR LEU LEU GLU ILE SER LYS ARG PHE ARG LYS GLU
SEQRES 5 B 923 MET GLU LYS GLY LEU GLY ALA THR THR HIS PRO THR ALA
SEQRES 6 B 923 ALA VAL LYS MET LEU PRO THR PHE VAL ARG SER THR PRO
SEQRES 7 B 923 ASP GLY THR GLU HIS GLY GLU PHE LEU ALA LEU ASP LEU
SEQRES 8 B 923 GLY GLY THR ASN PHE ARG VAL LEU TRP VAL LYS VAL THR
SEQRES 9 B 923 ASP ASN GLY LEU GLN LYS VAL GLU MET GLU ASN GLN ILE
SEQRES 10 B 923 TYR ALA ILE PRO GLU ASP ILE MET ARG GLY SER GLY THR
SEQRES 11 B 923 GLN LEU PHE ASP HIS ILE ALA GLU CYS LEU ALA ASN PHE
SEQRES 12 B 923 MET ASP LYS LEU GLN ILE LYS ASP LYS LYS LEU PRO LEU
SEQRES 13 B 923 GLY PHE THR PHE SER PHE PRO CYS HIS GLN THR LYS LEU
SEQRES 14 B 923 ASP GLU SER PHE LEU VAL SER TRP THR LYS GLY PHE LYS
SEQRES 15 B 923 SER SER GLY VAL GLU GLY ARG ASP VAL VAL ALA LEU ILE
SEQRES 16 B 923 ARG LYS ALA ILE GLN ARG ARG GLY ASP PHE ASP ILE ASP
SEQRES 17 B 923 ILE VAL ALA VAL VAL ASN ASP THR VAL GLY THR MET MET
SEQRES 18 B 923 THR CYS GLY TYR ASP ASP HIS ASN CYS GLU ILE GLY LEU
SEQRES 19 B 923 ILE VAL GLY THR GLY SER ASN ALA CYS TYR MET GLU GLU
SEQRES 20 B 923 MET ARG HIS ILE ASP MET VAL GLU GLY ASP GLU GLY ARG
SEQRES 21 B 923 MET CYS ILE ASN MET GLU TRP GLY ALA PHE GLY ASP ASP
SEQRES 22 B 923 GLY SER LEU ASN ASP ILE ARG THR GLU PHE ASP GLN GLU
SEQRES 23 B 923 ILE ASP MET GLY SER LEU ASN PRO GLY LYS GLN LEU PHE
SEQRES 24 B 923 GLU LYS MET ILE SER GLY MET TYR MET GLY GLU LEU VAL
SEQRES 25 B 923 ARG LEU ILE LEU VAL LYS MET ALA LYS GLU GLU LEU LEU
SEQRES 26 B 923 PHE GLY GLY LYS LEU SER PRO GLU LEU LEU ASN THR GLY
SEQRES 27 B 923 ARG PHE GLU THR LYS ASP ILE SER ASP ILE GLU GLY GLU
SEQRES 28 B 923 LYS ASP GLY ILE ARG LYS ALA ARG GLU VAL LEU MET ARG
SEQRES 29 B 923 LEU GLY LEU ASP PRO THR GLN GLU ASP CYS VAL ALA THR
SEQRES 30 B 923 HIS ARG ILE CYS GLN ILE VAL SER THR ARG SER ALA SER
SEQRES 31 B 923 LEU CYS ALA ALA THR LEU ALA ALA VAL LEU GLN ARG ILE
SEQRES 32 B 923 LYS GLU ASN LYS GLY GLU GLU ARG LEU ARG SER THR ILE
SEQRES 33 B 923 GLY VAL ASP GLY SER VAL TYR LYS LYS HIS PRO HIS PHE
SEQRES 34 B 923 ALA LYS ARG LEU HIS LYS THR VAL ARG ARG LEU VAL PRO
SEQRES 35 B 923 GLY CYS ASP VAL ARG PHE LEU ARG SER GLU ASP GLY SER
SEQRES 36 B 923 GLY LYS GLY ALA ALA MET VAL THR ALA VAL ALA TYR ARG
SEQRES 37 B 923 LEU ALA ASP GLN HIS ARG ALA ARG GLN LYS THR LEU GLU
SEQRES 38 B 923 HIS LEU GLN LEU SER HIS ASP GLN LEU LEU GLU VAL LYS
SEQRES 39 B 923 ARG ARG MET LYS VAL GLU MET GLU ARG GLY LEU SER LYS
SEQRES 40 B 923 GLU THR HIS ALA SER ALA PRO VAL LYS MET LEU PRO THR
SEQRES 41 B 923 TYR VAL CYS ALA THR PRO ASP GLY THR GLU LYS GLY ASP
SEQRES 42 B 923 PHE LEU ALA LEU ASP LEU GLY GLY THR ASN PHE ARG VAL
SEQRES 43 B 923 LEU LEU VAL ARG VAL ARG ASN GLY LYS TRP GLY GLY VAL
SEQRES 44 B 923 GLU MET HIS ASN LYS ILE TYR ALA ILE PRO GLN GLU VAL
SEQRES 45 B 923 MET HIS GLY THR GLY ASP GLU LEU PHE ASP HIS ILE VAL
SEQRES 46 B 923 GLN CYS ILE ALA ASP PHE LEU GLU TYR MET GLY MET LYS
SEQRES 47 B 923 GLY VAL SER LEU PRO LEU GLY PHE THR PHE SER PHE PRO
SEQRES 48 B 923 CYS GLN GLN ASN SER LEU ASP GLU SER ILE LEU LEU LYS
SEQRES 49 B 923 TRP THR LYS GLY PHE LYS ALA SER GLY CYS GLU GLY GLU
SEQRES 50 B 923 ASP VAL VAL THR LEU LEU LYS GLU ALA ILE HIS ARG ARG
SEQRES 51 B 923 GLU GLU PHE ASP LEU ASP VAL VAL ALA VAL VAL ASN ASP
SEQRES 52 B 923 THR VAL GLY THR MET MET THR CYS GLY PHE GLU ASP PRO
SEQRES 53 B 923 HIS CYS GLU VAL GLY LEU ILE VAL GLY THR GLY SER ASN
SEQRES 54 B 923 ALA CYS TYR MET GLU GLU MET ARG ASN VAL GLU LEU VAL
SEQRES 55 B 923 GLU GLY GLU GLU GLY ARG MET CYS VAL ASN MET GLU TRP
SEQRES 56 B 923 GLY ALA PHE GLY ASP ASN GLY CYS LEU ASP ASP PHE ARG
SEQRES 57 B 923 THR GLU PHE ASP VAL ALA VAL ASP GLU LEU SER LEU ASN
SEQRES 58 B 923 PRO GLY LYS GLN ARG PHE GLU LYS MET ILE SER GLY MET
SEQRES 59 B 923 TYR LEU GLY GLU ILE VAL ARG ASN ILE LEU ILE ASP PHE
SEQRES 60 B 923 THR LYS ARG GLY LEU LEU PHE ARG GLY ARG ILE SER GLU
SEQRES 61 B 923 ARG LEU LYS THR ARG GLY ILE PHE GLU THR LYS PHE LEU
SEQRES 62 B 923 SER GLN ILE GLU SER ASP CYS LEU ALA LEU LEU GLN VAL
SEQRES 63 B 923 ARG ALA ILE LEU GLN HIS LEU GLY LEU GLU SER THR CYS
SEQRES 64 B 923 ASP ASP SER ILE ILE VAL LYS GLU VAL CYS THR VAL VAL
SEQRES 65 B 923 ALA ARG ARG ALA ALA GLN LEU CYS GLY ALA GLY MET ALA
SEQRES 66 B 923 ALA VAL VAL ASP ARG ILE ARG GLU ASN ARG GLY LEU ASP
SEQRES 67 B 923 ALA LEU LYS VAL THR VAL GLY VAL ASP GLY THR LEU TYR
SEQRES 68 B 923 LYS LEU HIS PRO HIS PHE ALA LYS VAL MET HIS GLU THR
SEQRES 69 B 923 VAL LYS ASP LEU ALA PRO LYS CYS ASP VAL SER PHE LEU
SEQRES 70 B 923 GLN SER GLU ASP GLY SER GLY LYS GLY ALA ALA LEU ILE
SEQRES 71 B 923 THR ALA VAL ALA CYS ARG ILE ARG GLU ALA GLY GLN ARG
HET 604 A1001 33
HET 604 A1002 33
HET 604 B1001 30
HET 604 B1002 33
HETNAM 604 2-[(3-BROMOBENZENE-1-CARBONYL)AMINO]-6-{[(4-CARBOXY-5-
HETNAM 2 604 METHYLFURAN-2-YL)SULFONYL]AMINO}-2,6-DIDEOXY-ALPHA-D-
HETNAM 3 604 GLUCOPYRANOS E
HETSYN 604 5-[[(2~{R},3~{S},4~{R},5~{R},6~{S})-5-[(3-BROMOPHENYL)
HETSYN 2 604 CARBONYLAMINO]-3,4,6-TRIS(OXIDANYL)OXAN-2-
HETSYN 3 604 YL]METHYLSULFAMOYL]-2-M ETHYL-FURAN-3-CARBOXYLIC ACID;
HETSYN 4 604 2-[(3-BROMOBENZENE-1-CARBONYL)AMINO]-6-{[(4-CARBOXY-5-
HETSYN 5 604 METHYLFURAN-2-YL)SULFONYL]AMINO}-2,6-DIDEOXY-ALPHA-D-
HETSYN 6 604 GLUCOSE; 2-[(3-BROMOBENZENE-1-CARBONYL)AMINO]-6-{[(4-
HETSYN 7 604 CARBOXY-5-METHYLFURAN-2-YL)SULFONYL]AMINO}-2,6-
HETSYN 8 604 DIDEOXY-D-GLUCOSE; 2-[(3-BROMOBENZENE-1-CARBONYL)
HETSYN 9 604 AMINO]-6-{[(4-CARBOXY-5-METHYLFURAN-2-YL)
HETSYN 10 604 SULFONYL]AMINO}-2,6-DIDEOXY-GLUCOSE
FORMUL 3 604 4(C19 H21 BR N2 O10 S)
FORMUL 7 HOH *83(H2 O)
HELIX 1 AA1 ASP A 17 LEU A 26 1 10
HELIX 2 AA2 TYR A 27 ARG A 30 5 4
HELIX 3 AA3 SER A 32 GLY A 52 1 21
HELIX 4 AA4 GLY A 123 LEU A 141 1 19
HELIX 5 AA5 ASP A 184 GLY A 197 1 14
HELIX 6 AA6 ASP A 209 ASP A 221 1 13
HELIX 7 AA7 ARG A 243 ILE A 245 5 3
HELIX 8 AA8 GLU A 260 PHE A 264 5 5
HELIX 9 AA9 THR A 275 GLY A 284 1 10
HELIX 10 AB1 PHE A 293 SER A 298 1 6
HELIX 11 AB2 TYR A 301 GLU A 316 1 16
HELIX 12 AB3 LEU A 319 LYS A 323 5 5
HELIX 13 AB4 GLU A 335 GLU A 345 1 11
HELIX 14 AB5 ASP A 347 LEU A 359 1 13
HELIX 15 AB6 THR A 364 GLY A 402 1 39
HELIX 16 AB7 GLY A 414 HIS A 420 1 7
HELIX 17 AB8 HIS A 422 VAL A 435 1 14
HELIX 18 AB9 GLY A 448 GLU A 475 1 28
HELIX 19 AC1 HIS A 476 GLN A 478 5 3
HELIX 20 AC2 SER A 480 SER A 500 1 21
HELIX 21 AC3 PRO A 563 GLY A 569 1 7
HELIX 22 AC4 THR A 570 MET A 589 1 20
HELIX 23 AC5 ASP A 632 ARG A 643 1 12
HELIX 24 AC6 ASN A 656 PHE A 667 1 12
HELIX 25 AC7 GLU A 708 PHE A 712 5 5
HELIX 26 AC8 THR A 723 SER A 733 1 11
HELIX 27 AC9 GLN A 739 SER A 746 1 8
HELIX 28 AD1 MET A 748 ARG A 764 1 17
HELIX 29 AD2 LEU A 767 ARG A 771 5 5
HELIX 30 AD3 GLU A 783 ASP A 793 1 11
HELIX 31 AD4 LEU A 797 LEU A 807 1 11
HELIX 32 AD5 THR A 812 GLY A 850 1 39
HELIX 33 AD6 GLY A 862 HIS A 868 1 7
HELIX 34 AD7 HIS A 870 ALA A 883 1 14
HELIX 35 AD8 LYS A 899 CYS A 909 1 11
HELIX 36 AD9 GLN B 18 LEU B 26 1 9
HELIX 37 AE1 TYR B 27 ARG B 30 5 4
HELIX 38 AE2 SER B 32 GLY B 52 1 21
HELIX 39 AE3 THR B 55 ALA B 59 5 5
HELIX 40 AE4 PRO B 115 GLY B 121 1 7
HELIX 41 AE5 SER B 122 LEU B 141 1 20
HELIX 42 AE6 ASP B 184 GLY B 197 1 14
HELIX 43 AE7 ASP B 209 ASP B 221 1 13
HELIX 44 AE8 ARG B 243 ILE B 245 5 3
HELIX 45 AE9 GLU B 260 PHE B 264 5 5
HELIX 46 AF1 THR B 275 GLY B 284 1 10
HELIX 47 AF2 GLN B 291 SER B 298 1 8
HELIX 48 AF3 TYR B 301 GLU B 316 1 16
HELIX 49 AF4 LEU B 319 LYS B 323 5 5
HELIX 50 AF5 GLU B 335 GLU B 343 1 9
HELIX 51 AF6 GLY B 348 LEU B 359 1 12
HELIX 52 AF7 THR B 364 GLY B 402 1 39
HELIX 53 AF8 GLY B 414 HIS B 420 1 7
HELIX 54 AF9 HIS B 422 VAL B 435 1 14
HELIX 55 AG1 GLY B 448 HIS B 476 1 29
HELIX 56 AG2 SER B 480 SER B 500 1 21
HELIX 57 AG3 THR B 503 ALA B 507 5 5
HELIX 58 AG4 PRO B 563 HIS B 568 1 6
HELIX 59 AG5 THR B 570 TYR B 588 1 19
HELIX 60 AG6 ASP B 632 ARG B 644 1 13
HELIX 61 AG7 ASN B 656 ASP B 669 1 14
HELIX 62 AG8 GLU B 708 PHE B 712 5 5
HELIX 63 AG9 LEU B 718 ARG B 722 5 5
HELIX 64 AH1 THR B 723 LEU B 732 1 10
HELIX 65 AH2 GLN B 739 SER B 746 1 8
HELIX 66 AH3 MET B 748 ARG B 764 1 17
HELIX 67 AH4 LEU B 767 ARG B 771 5 5
HELIX 68 AH5 GLU B 774 THR B 778 5 5
HELIX 69 AH6 GLU B 783 ASP B 793 1 11
HELIX 70 AH7 LEU B 797 LEU B 807 1 11
HELIX 71 AH8 THR B 812 ARG B 849 1 38
HELIX 72 AH9 GLY B 862 HIS B 868 1 7
HELIX 73 AI1 HIS B 870 ALA B 883 1 14
HELIX 74 AI2 GLY B 898 GLU B 913 1 16
SHEET 1 AA1 6 LEU A 64 PRO A 65 0
SHEET 2 AA1 6 ARG A 254 ASN A 258 -1 O ASN A 258 N LEU A 64
SHEET 3 AA1 6 SER A 234 GLU A 241 -1 N TYR A 238 O ILE A 257
SHEET 4 AA1 6 CYS A 224 VAL A 230 -1 N ILE A 229 O ASN A 235
SHEET 5 AA1 6 LEU A 406 ASP A 413 1 O GLY A 411 N ILE A 226
SHEET 6 AA1 6 CYS A 438 ARG A 444 1 O ASP A 439 N LEU A 406
SHEET 1 AA2 5 GLU A 106 TYR A 112 0
SHEET 2 AA2 5 PHE A 90 VAL A 97 -1 N LYS A 96 O GLU A 106
SHEET 3 AA2 5 GLY A 78 LEU A 85 -1 N GLY A 78 O VAL A 97
SHEET 4 AA2 5 LEU A 150 PHE A 154 1 O GLY A 151 N LEU A 81
SHEET 5 AA2 5 VAL A 204 ASN A 208 1 O ALA A 205 N PHE A 152
SHEET 1 AA3 6 LEU A 512 PRO A 513 0
SHEET 2 AA3 6 ARG A 702 ASN A 706 -1 O ASN A 706 N LEU A 512
SHEET 3 AA3 6 SER A 682 GLU A 689 -1 N TYR A 686 O VAL A 705
SHEET 4 AA3 6 CYS A 672 VAL A 678 -1 N ILE A 677 O ASN A 683
SHEET 5 AA3 6 LEU A 854 ASP A 861 1 O GLY A 859 N VAL A 674
SHEET 6 AA3 6 CYS A 886 GLN A 892 1 O ASP A 887 N LEU A 854
SHEET 1 AA4 5 GLY A 552 ALA A 561 0
SHEET 2 AA4 5 ASN A 537 ARG A 546 -1 N LEU A 542 O HIS A 556
SHEET 3 AA4 5 GLY A 526 LEU A 533 -1 N PHE A 528 O VAL A 543
SHEET 4 AA4 5 PRO A 597 PHE A 602 1 O THR A 601 N LEU A 533
SHEET 5 AA4 5 ASP A 650 VAL A 655 1 O VAL A 655 N PHE A 600
SHEET 1 AA5 2 CYS A 606 SER A 610 0
SHEET 2 AA5 2 GLU A 613 LEU A 616 -1 O ILE A 615 N GLN A 607
SHEET 1 AA6 6 LEU B 64 PRO B 65 0
SHEET 2 AA6 6 ARG B 254 ASN B 258 -1 O ASN B 258 N LEU B 64
SHEET 3 AA6 6 SER B 234 GLU B 241 -1 N GLU B 240 O MET B 255
SHEET 4 AA6 6 CYS B 224 VAL B 230 -1 N GLY B 227 O CYS B 237
SHEET 5 AA6 6 LEU B 406 ASP B 413 1 O GLY B 411 N LEU B 228
SHEET 6 AA6 6 CYS B 438 ARG B 444 1 O ARG B 441 N ILE B 410
SHEET 1 AA7 5 VAL B 105 ALA B 113 0
SHEET 2 AA7 5 ASN B 89 VAL B 97 -1 N PHE B 90 O TYR B 112
SHEET 3 AA7 5 GLY B 78 GLY B 86 -1 N GLY B 78 O VAL B 97
SHEET 4 AA7 5 LEU B 150 PHE B 154 1 O GLY B 151 N LEU B 81
SHEET 5 AA7 5 VAL B 204 ASN B 208 1 O ALA B 205 N PHE B 152
SHEET 1 AA8 6 LEU B 512 PRO B 513 0
SHEET 2 AA8 6 ARG B 702 ASN B 706 -1 O ASN B 706 N LEU B 512
SHEET 3 AA8 6 SER B 682 GLU B 689 -1 N GLU B 688 O MET B 703
SHEET 4 AA8 6 CYS B 672 VAL B 678 -1 N GLY B 675 O CYS B 685
SHEET 5 AA8 6 LEU B 854 ASP B 861 1 O GLY B 859 N VAL B 674
SHEET 6 AA8 6 CYS B 886 GLN B 892 1 O ASP B 887 N LEU B 854
SHEET 1 AA9 5 VAL B 553 ALA B 561 0
SHEET 2 AA9 5 ASN B 537 VAL B 545 -1 N LEU B 542 O HIS B 556
SHEET 3 AA9 5 GLY B 526 LEU B 533 -1 N GLY B 526 O VAL B 545
SHEET 4 AA9 5 PRO B 597 PHE B 602 1 O PRO B 597 N LEU B 529
SHEET 5 AA9 5 ASP B 650 VAL B 655 1 O ASP B 650 N LEU B 598
SHEET 1 AB1 2 CYS B 606 SER B 610 0
SHEET 2 AB1 2 GLU B 613 LEU B 616 -1 O ILE B 615 N GLN B 607
CISPEP 1 GLY A 896 SER A 897 0 21.78
CISPEP 2 ASN B 547 GLY B 548 0 9.44
CRYST1 66.032 154.893 114.825 90.00 96.34 90.00 P 1 21 1 4
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 0.015144 0.000000 0.001682 0.00000
SCALE2 0.000000 0.006456 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008762 0.00000
(ATOM LINES ARE NOT SHOWN.)
END