HEADER TRANSFERASE 06-JAN-15 4XIF
TITLE HUMAN OGT IN COMPLEX WITH UDP-5S-GLCNAC AND SUBSTRATE PEPTIDE
TITLE 2 (KERATIN-7)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-
COMPND 3 ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: UNP RESIDUES 323-1041;
COMPND 6 SYNONYM: O-GLCNAC TRANSFERASE SUBUNIT P110,O-LINKED N-
COMPND 7 ACETYLGLUCOSAMINE TRANSFERASE 110 KDA SUBUNIT,OGT;
COMPND 8 EC: 2.4.1.255;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: KERATIN, TYPE II CYTOSKELETAL 7;
COMPND 12 CHAIN: E, F, G, H;
COMPND 13 FRAGMENT: UNP RESIDUES 8-16;
COMPND 14 SYNONYM: CYTOKERATIN-7,CK-7,KERATIN-7,K7,SARCOLECTIN,TYPE-II KERATIN
COMPND 15 KB7;
COMPND 16 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: OGT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS O-GLCNAC TRANSFERASE INVERTING GT-B SUBSTRATE COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SCHIMPL,D.M.F.VAN AALTEN
REVDAT 3 16-SEP-15 4XIF 1 JRNL
REVDAT 2 12-AUG-15 4XIF 1 JRNL
REVDAT 1 05-AUG-15 4XIF 0
JRNL AUTH S.PATHAK,J.ALONSO,M.SCHIMPL,K.RAFIE,D.E.BLAIR,V.S.BORODKIN,
JRNL AUTH 2 A.W.SCHUTTELKOPF,O.ALBARBARAWI,D.M.VAN AALTEN
JRNL TITL THE ACTIVE SITE OF O-GLCNAC TRANSFERASE IMPOSES CONSTRAINTS
JRNL TITL 2 ON SUBSTRATE SEQUENCE.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 22 744 2015
JRNL REFN ESSN 1545-9985
JRNL PMID 26237509
JRNL DOI 10.1038/NSMB.3063
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 100304
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1015
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7227
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.3310
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.3850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22432
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 176
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.46000
REMARK 3 B22 (A**2) : 1.46000
REMARK 3 B33 (A**2) : -2.18000
REMARK 3 B12 (A**2) : 0.73000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.052
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.365
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.290
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.745
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.913
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.884
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23124 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 31384 ; 1.356 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2836 ; 5.608 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1052 ;38.660 ;24.487
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3940 ;17.733 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 124 ;19.269 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3484 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17484 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 14264 ; 0.688 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23040 ; 1.413 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8860 ; 1.910 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8344 ; 3.496 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 312 A 1031 1
REMARK 3 1 B 312 B 1031 1
REMARK 3 1 C 312 C 1031 1
REMARK 3 1 D 312 D 1031 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 5535 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 5535 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 5535 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 D (A): 5535 ; 0.05 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 5535 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 5535 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 5535 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 1 D (A**2): 5535 ; 0.08 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2007 A 2017 1
REMARK 3 1 B 2007 B 2017 1
REMARK 3 1 C 2007 C 2017 1
REMARK 3 1 D 2007 D 2017 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 73 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 B (A): 73 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 C (A): 73 ; 0.03 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 D (A): 73 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 2 A (A**2): 73 ; 0.06 ; 0.50
REMARK 3 TIGHT THERMAL 2 B (A**2): 73 ; 0.04 ; 0.50
REMARK 3 TIGHT THERMAL 2 C (A**2): 73 ; 0.05 ; 0.50
REMARK 3 TIGHT THERMAL 2 D (A**2): 73 ; 0.05 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4XIF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000205715.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.873
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105151
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 1.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 1.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.45 M POTASSIUM PHOSPHATE, 10 MM
REMARK 280 EDTA, 1% (W/V) XYLITOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 309
REMARK 465 PRO A 310
REMARK 465 GLY A 311
REMARK 465 SER A 715
REMARK 465 ASN A 716
REMARK 465 GLY A 717
REMARK 465 PRO A 749
REMARK 465 ASP A 750
REMARK 465 GLY A 751
REMARK 465 GLY A 752
REMARK 465 ASP A 753
REMARK 465 ASN A 754
REMARK 465 ALA A 755
REMARK 465 ASP A 756
REMARK 465 SER A 757
REMARK 465 SER A 758
REMARK 465 ASN A 759
REMARK 465 THR A 760
REMARK 465 PRO A 1029
REMARK 465 VAL A 1030
REMARK 465 GLU A 1031
REMARK 465 GLY B 309
REMARK 465 PRO B 310
REMARK 465 GLY B 311
REMARK 465 SER B 715
REMARK 465 ASN B 716
REMARK 465 GLY B 717
REMARK 465 PRO B 749
REMARK 465 ASP B 750
REMARK 465 GLY B 751
REMARK 465 GLY B 752
REMARK 465 ASP B 753
REMARK 465 ASN B 754
REMARK 465 ALA B 755
REMARK 465 ASP B 756
REMARK 465 SER B 757
REMARK 465 SER B 758
REMARK 465 ASN B 759
REMARK 465 THR B 760
REMARK 465 PRO B 1029
REMARK 465 VAL B 1030
REMARK 465 GLU B 1031
REMARK 465 GLY C 309
REMARK 465 PRO C 310
REMARK 465 GLY C 311
REMARK 465 SER C 715
REMARK 465 ASN C 716
REMARK 465 GLY C 717
REMARK 465 PRO C 749
REMARK 465 ASP C 750
REMARK 465 GLY C 751
REMARK 465 GLY C 752
REMARK 465 ASP C 753
REMARK 465 ASN C 754
REMARK 465 ALA C 755
REMARK 465 ASP C 756
REMARK 465 SER C 757
REMARK 465 SER C 758
REMARK 465 ASN C 759
REMARK 465 THR C 760
REMARK 465 PRO C 1029
REMARK 465 VAL C 1030
REMARK 465 GLU C 1031
REMARK 465 GLY D 309
REMARK 465 PRO D 310
REMARK 465 GLY D 311
REMARK 465 SER D 715
REMARK 465 ASN D 716
REMARK 465 GLY D 717
REMARK 465 PRO D 749
REMARK 465 ASP D 750
REMARK 465 GLY D 751
REMARK 465 GLY D 752
REMARK 465 ASP D 753
REMARK 465 ASN D 754
REMARK 465 ALA D 755
REMARK 465 ASP D 756
REMARK 465 SER D 757
REMARK 465 SER D 758
REMARK 465 ASN D 759
REMARK 465 THR D 760
REMARK 465 PRO D 1029
REMARK 465 VAL D 1030
REMARK 465 GLU D 1031
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 LYS A 714 CG CD CE NZ
REMARK 470 HIS A 718 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 714 CG CD CE NZ
REMARK 470 HIS B 718 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 714 CG CD CE NZ
REMARK 470 HIS C 718 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 714 CG CD CE NZ
REMARK 470 HIS D 718 CG ND1 CD2 CE1 NE2
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 B 580 CB CYS B 580 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 ARG A 963 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG B 963 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG C 963 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG D 963 NE - CZ - NH1 ANGL. DEV. = 4.6 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 GLN A 330 4.02 -69.65
REMARK 500 GLU A 349 36.20 -92.81
REMARK 500 LYS A 366 48.27 -92.61
REMARK 500 ASP A 400 77.60 -105.24
REMARK 500 LYS A 489 -5.09 -55.40
REMARK 500 ASP A 543 40.97 72.58
REMARK 500 TYR A 632 52.84 -109.26
REMARK 500 LEU A 653 -48.00 67.48
REMARK 500 PRO A 656 55.53 -92.47
REMARK 500 THR A 669 -152.71 -149.82
REMARK 500 HIS A 691 -78.57 -123.81
REMARK 500 ILE A 719 84.05 81.71
REMARK 500 ASN A 722 42.18 -153.35
REMARK 500 ASN A 763 166.34 176.86
REMARK 500 ASN A 804 98.44 -165.48
REMARK 500 ASN A 860 64.62 -103.44
REMARK 500 ASN A 888 -33.13 -27.92
REMARK 500 HIS A 920 -75.00 -103.00
REMARK 500 GLN B 330 7.70 -69.81
REMARK 500 ASN B 332 83.32 -68.65
REMARK 500 GLU B 349 33.82 -91.74
REMARK 500 LYS B 366 43.68 -91.91
REMARK 500 ASP B 400 75.03 -101.38
REMARK 500 LYS B 489 -3.56 -56.14
REMARK 500 TYR B 632 54.75 -111.58
REMARK 500 LEU B 653 -44.44 63.31
REMARK 500 PRO B 656 55.68 -93.02
REMARK 500 THR B 669 -152.61 -149.10
REMARK 500 HIS B 691 -76.74 -127.06
REMARK 500 ILE B 719 86.14 83.30
REMARK 500 ASN B 722 42.42 -157.68
REMARK 500 ASN B 763 165.92 174.31
REMARK 500 ASN B 804 97.80 -164.13
REMARK 500 ASN B 860 64.41 -103.69
REMARK 500 ARG B 867 78.70 -68.81
REMARK 500 ASN B 888 -38.66 -30.49
REMARK 500 HIS B 920 -75.29 -104.98
REMARK 500 GLN C 330 6.41 -68.85
REMARK 500 ASN C 332 81.36 -67.59
REMARK 500 GLU C 349 34.95 -92.84
REMARK 500 LYS C 366 44.66 -92.08
REMARK 500 ASP C 400 78.50 -103.64
REMARK 500 PHE C 452 89.70 -151.88
REMARK 500 LYS C 489 -4.65 -55.86
REMARK 500 TYR C 632 54.72 -110.63
REMARK 500 LEU C 653 -49.00 68.41
REMARK 500 PRO C 656 52.40 -93.65
REMARK 500 THR C 669 -148.71 -148.40
REMARK 500 HIS C 691 -78.40 -127.53
REMARK 500 ILE C 719 84.82 82.00
REMARK 500
REMARK 500 THIS ENTRY HAS 74 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 12V A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 12V B 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 12V C 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 12V D 1200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 2101
DBREF 4XIF A 313 1031 UNP O15294 OGT1_HUMAN 323 1041
DBREF 4XIF B 313 1031 UNP O15294 OGT1_HUMAN 323 1041
DBREF 4XIF C 313 1031 UNP O15294 OGT1_HUMAN 323 1041
DBREF 4XIF D 313 1031 UNP O15294 OGT1_HUMAN 323 1041
DBREF 4XIF E 2008 2016 UNP P08729 K2C7_HUMAN 8 16
DBREF 4XIF F 2008 2016 UNP P08729 K2C7_HUMAN 8 16
DBREF 4XIF G 2008 2016 UNP P08729 K2C7_HUMAN 8 16
DBREF 4XIF H 2008 2016 UNP P08729 K2C7_HUMAN 8 16
SEQADV 4XIF GLY A 309 UNP O15294 EXPRESSION TAG
SEQADV 4XIF PRO A 310 UNP O15294 EXPRESSION TAG
SEQADV 4XIF GLY A 311 UNP O15294 EXPRESSION TAG
SEQADV 4XIF SER A 312 UNP O15294 EXPRESSION TAG
SEQADV 4XIF GLY B 309 UNP O15294 EXPRESSION TAG
SEQADV 4XIF PRO B 310 UNP O15294 EXPRESSION TAG
SEQADV 4XIF GLY B 311 UNP O15294 EXPRESSION TAG
SEQADV 4XIF SER B 312 UNP O15294 EXPRESSION TAG
SEQADV 4XIF GLY C 309 UNP O15294 EXPRESSION TAG
SEQADV 4XIF PRO C 310 UNP O15294 EXPRESSION TAG
SEQADV 4XIF GLY C 311 UNP O15294 EXPRESSION TAG
SEQADV 4XIF SER C 312 UNP O15294 EXPRESSION TAG
SEQADV 4XIF GLY D 309 UNP O15294 EXPRESSION TAG
SEQADV 4XIF PRO D 310 UNP O15294 EXPRESSION TAG
SEQADV 4XIF GLY D 311 UNP O15294 EXPRESSION TAG
SEQADV 4XIF SER D 312 UNP O15294 EXPRESSION TAG
SEQADV 4XIF GLY E 2007 UNP P08729 EXPRESSION TAG
SEQADV 4XIF GLY E 2017 UNP P08729 EXPRESSION TAG
SEQADV 4XIF GLY F 2007 UNP P08729 EXPRESSION TAG
SEQADV 4XIF GLY F 2017 UNP P08729 EXPRESSION TAG
SEQADV 4XIF GLY G 2007 UNP P08729 EXPRESSION TAG
SEQADV 4XIF GLY G 2017 UNP P08729 EXPRESSION TAG
SEQADV 4XIF GLY H 2007 UNP P08729 EXPRESSION TAG
SEQADV 4XIF GLY H 2017 UNP P08729 EXPRESSION TAG
SEQRES 1 A 723 GLY PRO GLY SER CYS PRO THR HIS ALA ASP SER LEU ASN
SEQRES 2 A 723 ASN LEU ALA ASN ILE LYS ARG GLU GLN GLY ASN ILE GLU
SEQRES 3 A 723 GLU ALA VAL ARG LEU TYR ARG LYS ALA LEU GLU VAL PHE
SEQRES 4 A 723 PRO GLU PHE ALA ALA ALA HIS SER ASN LEU ALA SER VAL
SEQRES 5 A 723 LEU GLN GLN GLN GLY LYS LEU GLN GLU ALA LEU MET HIS
SEQRES 6 A 723 TYR LYS GLU ALA ILE ARG ILE SER PRO THR PHE ALA ASP
SEQRES 7 A 723 ALA TYR SER ASN MET GLY ASN THR LEU LYS GLU MET GLN
SEQRES 8 A 723 ASP VAL GLN GLY ALA LEU GLN CYS TYR THR ARG ALA ILE
SEQRES 9 A 723 GLN ILE ASN PRO ALA PHE ALA ASP ALA HIS SER ASN LEU
SEQRES 10 A 723 ALA SER ILE HIS LYS ASP SER GLY ASN ILE PRO GLU ALA
SEQRES 11 A 723 ILE ALA SER TYR ARG THR ALA LEU LYS LEU LYS PRO ASP
SEQRES 12 A 723 PHE PRO ASP ALA TYR CYS ASN LEU ALA HIS CYS LEU GLN
SEQRES 13 A 723 ILE VAL CYS ASP TRP THR ASP TYR ASP GLU ARG MET LYS
SEQRES 14 A 723 LYS LEU VAL SER ILE VAL ALA ASP GLN LEU GLU LYS ASN
SEQRES 15 A 723 ARG LEU PRO SER VAL HIS PRO HIS HIS SER MET LEU TYR
SEQRES 16 A 723 PRO LEU SER HIS GLY PHE ARG LYS ALA ILE ALA GLU ARG
SEQRES 17 A 723 HIS GLY ASN LEU CYS LEU ASP LYS ILE ASN VAL LEU HIS
SEQRES 18 A 723 LYS PRO PRO TYR GLU HIS PRO LYS ASP LEU LYS LEU SER
SEQRES 19 A 723 ASP GLY ARG LEU ARG VAL GLY TYR VAL SER SER ASP PHE
SEQRES 20 A 723 GLY ASN HIS PRO THR SER HIS LEU MET GLN SER ILE PRO
SEQRES 21 A 723 GLY MET HIS ASN PRO ASP LYS PHE GLU VAL PHE CYS TYR
SEQRES 22 A 723 ALA LEU SER PRO ASP ASP GLY THR ASN PHE ARG VAL LYS
SEQRES 23 A 723 VAL MET ALA GLU ALA ASN HIS PHE ILE ASP LEU SER GLN
SEQRES 24 A 723 ILE PRO CYS ASN GLY LYS ALA ALA ASP ARG ILE HIS GLN
SEQRES 25 A 723 ASP GLY ILE HIS ILE LEU VAL ASN MET ASN GLY TYR THR
SEQRES 26 A 723 LYS GLY ALA ARG ASN GLU LEU PHE ALA LEU ARG PRO ALA
SEQRES 27 A 723 PRO ILE GLN ALA MET TRP LEU GLY TYR PRO GLY THR SER
SEQRES 28 A 723 GLY ALA LEU PHE MET ASP TYR ILE ILE THR ASP GLN GLU
SEQRES 29 A 723 THR SER PRO ALA GLU VAL ALA GLU GLN TYR SER GLU LYS
SEQRES 30 A 723 LEU ALA TYR MET PRO HIS THR PHE PHE ILE GLY ASP HIS
SEQRES 31 A 723 ALA ASN MET PHE PRO HIS LEU LYS LYS LYS ALA VAL ILE
SEQRES 32 A 723 ASP PHE LYS SER ASN GLY HIS ILE TYR ASP ASN ARG ILE
SEQRES 33 A 723 VAL LEU ASN GLY ILE ASP LEU LYS ALA PHE LEU ASP SER
SEQRES 34 A 723 LEU PRO ASP VAL LYS ILE VAL LYS MET LYS CYS PRO ASP
SEQRES 35 A 723 GLY GLY ASP ASN ALA ASP SER SER ASN THR ALA LEU ASN
SEQRES 36 A 723 MET PRO VAL ILE PRO MET ASN THR ILE ALA GLU ALA VAL
SEQRES 37 A 723 ILE GLU MET ILE ASN ARG GLY GLN ILE GLN ILE THR ILE
SEQRES 38 A 723 ASN GLY PHE SER ILE SER ASN GLY LEU ALA THR THR GLN
SEQRES 39 A 723 ILE ASN ASN LYS ALA ALA THR GLY GLU GLU VAL PRO ARG
SEQRES 40 A 723 THR ILE ILE VAL THR THR ARG SER GLN TYR GLY LEU PRO
SEQRES 41 A 723 GLU ASP ALA ILE VAL TYR CYS ASN PHE ASN GLN LEU TYR
SEQRES 42 A 723 LYS ILE ASP PRO SER THR LEU GLN MET TRP ALA ASN ILE
SEQRES 43 A 723 LEU LYS ARG VAL PRO ASN SER VAL LEU TRP LEU LEU ARG
SEQRES 44 A 723 PHE PRO ALA VAL GLY GLU PRO ASN ILE GLN GLN TYR ALA
SEQRES 45 A 723 GLN ASN MET GLY LEU PRO GLN ASN ARG ILE ILE PHE SER
SEQRES 46 A 723 PRO VAL ALA PRO LYS GLU GLU HIS VAL ARG ARG GLY GLN
SEQRES 47 A 723 LEU ALA ASP VAL CYS LEU ASP THR PRO LEU CYS ASN GLY
SEQRES 48 A 723 HIS THR THR GLY MET ASP VAL LEU TRP ALA GLY THR PRO
SEQRES 49 A 723 MET VAL THR MET PRO GLY GLU THR LEU ALA SER ARG VAL
SEQRES 50 A 723 ALA ALA SER GLN LEU THR CYS LEU GLY CYS LEU GLU LEU
SEQRES 51 A 723 ILE ALA LYS ASN ARG GLN GLU TYR GLU ASP ILE ALA VAL
SEQRES 52 A 723 LYS LEU GLY THR ASP LEU GLU TYR LEU LYS LYS VAL ARG
SEQRES 53 A 723 GLY LYS VAL TRP LYS GLN ARG ILE SER SER PRO LEU PHE
SEQRES 54 A 723 ASN THR LYS GLN TYR THR MET GLU LEU GLU ARG LEU TYR
SEQRES 55 A 723 LEU GLN MET TRP GLU HIS TYR ALA ALA GLY ASN LYS PRO
SEQRES 56 A 723 ASP HIS MET ILE LYS PRO VAL GLU
SEQRES 1 B 723 GLY PRO GLY SER CYS PRO THR HIS ALA ASP SER LEU ASN
SEQRES 2 B 723 ASN LEU ALA ASN ILE LYS ARG GLU GLN GLY ASN ILE GLU
SEQRES 3 B 723 GLU ALA VAL ARG LEU TYR ARG LYS ALA LEU GLU VAL PHE
SEQRES 4 B 723 PRO GLU PHE ALA ALA ALA HIS SER ASN LEU ALA SER VAL
SEQRES 5 B 723 LEU GLN GLN GLN GLY LYS LEU GLN GLU ALA LEU MET HIS
SEQRES 6 B 723 TYR LYS GLU ALA ILE ARG ILE SER PRO THR PHE ALA ASP
SEQRES 7 B 723 ALA TYR SER ASN MET GLY ASN THR LEU LYS GLU MET GLN
SEQRES 8 B 723 ASP VAL GLN GLY ALA LEU GLN CYS TYR THR ARG ALA ILE
SEQRES 9 B 723 GLN ILE ASN PRO ALA PHE ALA ASP ALA HIS SER ASN LEU
SEQRES 10 B 723 ALA SER ILE HIS LYS ASP SER GLY ASN ILE PRO GLU ALA
SEQRES 11 B 723 ILE ALA SER TYR ARG THR ALA LEU LYS LEU LYS PRO ASP
SEQRES 12 B 723 PHE PRO ASP ALA TYR CYS ASN LEU ALA HIS CYS LEU GLN
SEQRES 13 B 723 ILE VAL CYS ASP TRP THR ASP TYR ASP GLU ARG MET LYS
SEQRES 14 B 723 LYS LEU VAL SER ILE VAL ALA ASP GLN LEU GLU LYS ASN
SEQRES 15 B 723 ARG LEU PRO SER VAL HIS PRO HIS HIS SER MET LEU TYR
SEQRES 16 B 723 PRO LEU SER HIS GLY PHE ARG LYS ALA ILE ALA GLU ARG
SEQRES 17 B 723 HIS GLY ASN LEU CYS LEU ASP LYS ILE ASN VAL LEU HIS
SEQRES 18 B 723 LYS PRO PRO TYR GLU HIS PRO LYS ASP LEU LYS LEU SER
SEQRES 19 B 723 ASP GLY ARG LEU ARG VAL GLY TYR VAL SER SER ASP PHE
SEQRES 20 B 723 GLY ASN HIS PRO THR SER HIS LEU MET GLN SER ILE PRO
SEQRES 21 B 723 GLY MET HIS ASN PRO ASP LYS PHE GLU VAL PHE CYS TYR
SEQRES 22 B 723 ALA LEU SER PRO ASP ASP GLY THR ASN PHE ARG VAL LYS
SEQRES 23 B 723 VAL MET ALA GLU ALA ASN HIS PHE ILE ASP LEU SER GLN
SEQRES 24 B 723 ILE PRO CYS ASN GLY LYS ALA ALA ASP ARG ILE HIS GLN
SEQRES 25 B 723 ASP GLY ILE HIS ILE LEU VAL ASN MET ASN GLY TYR THR
SEQRES 26 B 723 LYS GLY ALA ARG ASN GLU LEU PHE ALA LEU ARG PRO ALA
SEQRES 27 B 723 PRO ILE GLN ALA MET TRP LEU GLY TYR PRO GLY THR SER
SEQRES 28 B 723 GLY ALA LEU PHE MET ASP TYR ILE ILE THR ASP GLN GLU
SEQRES 29 B 723 THR SER PRO ALA GLU VAL ALA GLU GLN TYR SER GLU LYS
SEQRES 30 B 723 LEU ALA TYR MET PRO HIS THR PHE PHE ILE GLY ASP HIS
SEQRES 31 B 723 ALA ASN MET PHE PRO HIS LEU LYS LYS LYS ALA VAL ILE
SEQRES 32 B 723 ASP PHE LYS SER ASN GLY HIS ILE TYR ASP ASN ARG ILE
SEQRES 33 B 723 VAL LEU ASN GLY ILE ASP LEU LYS ALA PHE LEU ASP SER
SEQRES 34 B 723 LEU PRO ASP VAL LYS ILE VAL LYS MET LYS CYS PRO ASP
SEQRES 35 B 723 GLY GLY ASP ASN ALA ASP SER SER ASN THR ALA LEU ASN
SEQRES 36 B 723 MET PRO VAL ILE PRO MET ASN THR ILE ALA GLU ALA VAL
SEQRES 37 B 723 ILE GLU MET ILE ASN ARG GLY GLN ILE GLN ILE THR ILE
SEQRES 38 B 723 ASN GLY PHE SER ILE SER ASN GLY LEU ALA THR THR GLN
SEQRES 39 B 723 ILE ASN ASN LYS ALA ALA THR GLY GLU GLU VAL PRO ARG
SEQRES 40 B 723 THR ILE ILE VAL THR THR ARG SER GLN TYR GLY LEU PRO
SEQRES 41 B 723 GLU ASP ALA ILE VAL TYR CYS ASN PHE ASN GLN LEU TYR
SEQRES 42 B 723 LYS ILE ASP PRO SER THR LEU GLN MET TRP ALA ASN ILE
SEQRES 43 B 723 LEU LYS ARG VAL PRO ASN SER VAL LEU TRP LEU LEU ARG
SEQRES 44 B 723 PHE PRO ALA VAL GLY GLU PRO ASN ILE GLN GLN TYR ALA
SEQRES 45 B 723 GLN ASN MET GLY LEU PRO GLN ASN ARG ILE ILE PHE SER
SEQRES 46 B 723 PRO VAL ALA PRO LYS GLU GLU HIS VAL ARG ARG GLY GLN
SEQRES 47 B 723 LEU ALA ASP VAL CYS LEU ASP THR PRO LEU CYS ASN GLY
SEQRES 48 B 723 HIS THR THR GLY MET ASP VAL LEU TRP ALA GLY THR PRO
SEQRES 49 B 723 MET VAL THR MET PRO GLY GLU THR LEU ALA SER ARG VAL
SEQRES 50 B 723 ALA ALA SER GLN LEU THR CYS LEU GLY CYS LEU GLU LEU
SEQRES 51 B 723 ILE ALA LYS ASN ARG GLN GLU TYR GLU ASP ILE ALA VAL
SEQRES 52 B 723 LYS LEU GLY THR ASP LEU GLU TYR LEU LYS LYS VAL ARG
SEQRES 53 B 723 GLY LYS VAL TRP LYS GLN ARG ILE SER SER PRO LEU PHE
SEQRES 54 B 723 ASN THR LYS GLN TYR THR MET GLU LEU GLU ARG LEU TYR
SEQRES 55 B 723 LEU GLN MET TRP GLU HIS TYR ALA ALA GLY ASN LYS PRO
SEQRES 56 B 723 ASP HIS MET ILE LYS PRO VAL GLU
SEQRES 1 C 723 GLY PRO GLY SER CYS PRO THR HIS ALA ASP SER LEU ASN
SEQRES 2 C 723 ASN LEU ALA ASN ILE LYS ARG GLU GLN GLY ASN ILE GLU
SEQRES 3 C 723 GLU ALA VAL ARG LEU TYR ARG LYS ALA LEU GLU VAL PHE
SEQRES 4 C 723 PRO GLU PHE ALA ALA ALA HIS SER ASN LEU ALA SER VAL
SEQRES 5 C 723 LEU GLN GLN GLN GLY LYS LEU GLN GLU ALA LEU MET HIS
SEQRES 6 C 723 TYR LYS GLU ALA ILE ARG ILE SER PRO THR PHE ALA ASP
SEQRES 7 C 723 ALA TYR SER ASN MET GLY ASN THR LEU LYS GLU MET GLN
SEQRES 8 C 723 ASP VAL GLN GLY ALA LEU GLN CYS TYR THR ARG ALA ILE
SEQRES 9 C 723 GLN ILE ASN PRO ALA PHE ALA ASP ALA HIS SER ASN LEU
SEQRES 10 C 723 ALA SER ILE HIS LYS ASP SER GLY ASN ILE PRO GLU ALA
SEQRES 11 C 723 ILE ALA SER TYR ARG THR ALA LEU LYS LEU LYS PRO ASP
SEQRES 12 C 723 PHE PRO ASP ALA TYR CYS ASN LEU ALA HIS CYS LEU GLN
SEQRES 13 C 723 ILE VAL CYS ASP TRP THR ASP TYR ASP GLU ARG MET LYS
SEQRES 14 C 723 LYS LEU VAL SER ILE VAL ALA ASP GLN LEU GLU LYS ASN
SEQRES 15 C 723 ARG LEU PRO SER VAL HIS PRO HIS HIS SER MET LEU TYR
SEQRES 16 C 723 PRO LEU SER HIS GLY PHE ARG LYS ALA ILE ALA GLU ARG
SEQRES 17 C 723 HIS GLY ASN LEU CYS LEU ASP LYS ILE ASN VAL LEU HIS
SEQRES 18 C 723 LYS PRO PRO TYR GLU HIS PRO LYS ASP LEU LYS LEU SER
SEQRES 19 C 723 ASP GLY ARG LEU ARG VAL GLY TYR VAL SER SER ASP PHE
SEQRES 20 C 723 GLY ASN HIS PRO THR SER HIS LEU MET GLN SER ILE PRO
SEQRES 21 C 723 GLY MET HIS ASN PRO ASP LYS PHE GLU VAL PHE CYS TYR
SEQRES 22 C 723 ALA LEU SER PRO ASP ASP GLY THR ASN PHE ARG VAL LYS
SEQRES 23 C 723 VAL MET ALA GLU ALA ASN HIS PHE ILE ASP LEU SER GLN
SEQRES 24 C 723 ILE PRO CYS ASN GLY LYS ALA ALA ASP ARG ILE HIS GLN
SEQRES 25 C 723 ASP GLY ILE HIS ILE LEU VAL ASN MET ASN GLY TYR THR
SEQRES 26 C 723 LYS GLY ALA ARG ASN GLU LEU PHE ALA LEU ARG PRO ALA
SEQRES 27 C 723 PRO ILE GLN ALA MET TRP LEU GLY TYR PRO GLY THR SER
SEQRES 28 C 723 GLY ALA LEU PHE MET ASP TYR ILE ILE THR ASP GLN GLU
SEQRES 29 C 723 THR SER PRO ALA GLU VAL ALA GLU GLN TYR SER GLU LYS
SEQRES 30 C 723 LEU ALA TYR MET PRO HIS THR PHE PHE ILE GLY ASP HIS
SEQRES 31 C 723 ALA ASN MET PHE PRO HIS LEU LYS LYS LYS ALA VAL ILE
SEQRES 32 C 723 ASP PHE LYS SER ASN GLY HIS ILE TYR ASP ASN ARG ILE
SEQRES 33 C 723 VAL LEU ASN GLY ILE ASP LEU LYS ALA PHE LEU ASP SER
SEQRES 34 C 723 LEU PRO ASP VAL LYS ILE VAL LYS MET LYS CYS PRO ASP
SEQRES 35 C 723 GLY GLY ASP ASN ALA ASP SER SER ASN THR ALA LEU ASN
SEQRES 36 C 723 MET PRO VAL ILE PRO MET ASN THR ILE ALA GLU ALA VAL
SEQRES 37 C 723 ILE GLU MET ILE ASN ARG GLY GLN ILE GLN ILE THR ILE
SEQRES 38 C 723 ASN GLY PHE SER ILE SER ASN GLY LEU ALA THR THR GLN
SEQRES 39 C 723 ILE ASN ASN LYS ALA ALA THR GLY GLU GLU VAL PRO ARG
SEQRES 40 C 723 THR ILE ILE VAL THR THR ARG SER GLN TYR GLY LEU PRO
SEQRES 41 C 723 GLU ASP ALA ILE VAL TYR CYS ASN PHE ASN GLN LEU TYR
SEQRES 42 C 723 LYS ILE ASP PRO SER THR LEU GLN MET TRP ALA ASN ILE
SEQRES 43 C 723 LEU LYS ARG VAL PRO ASN SER VAL LEU TRP LEU LEU ARG
SEQRES 44 C 723 PHE PRO ALA VAL GLY GLU PRO ASN ILE GLN GLN TYR ALA
SEQRES 45 C 723 GLN ASN MET GLY LEU PRO GLN ASN ARG ILE ILE PHE SER
SEQRES 46 C 723 PRO VAL ALA PRO LYS GLU GLU HIS VAL ARG ARG GLY GLN
SEQRES 47 C 723 LEU ALA ASP VAL CYS LEU ASP THR PRO LEU CYS ASN GLY
SEQRES 48 C 723 HIS THR THR GLY MET ASP VAL LEU TRP ALA GLY THR PRO
SEQRES 49 C 723 MET VAL THR MET PRO GLY GLU THR LEU ALA SER ARG VAL
SEQRES 50 C 723 ALA ALA SER GLN LEU THR CYS LEU GLY CYS LEU GLU LEU
SEQRES 51 C 723 ILE ALA LYS ASN ARG GLN GLU TYR GLU ASP ILE ALA VAL
SEQRES 52 C 723 LYS LEU GLY THR ASP LEU GLU TYR LEU LYS LYS VAL ARG
SEQRES 53 C 723 GLY LYS VAL TRP LYS GLN ARG ILE SER SER PRO LEU PHE
SEQRES 54 C 723 ASN THR LYS GLN TYR THR MET GLU LEU GLU ARG LEU TYR
SEQRES 55 C 723 LEU GLN MET TRP GLU HIS TYR ALA ALA GLY ASN LYS PRO
SEQRES 56 C 723 ASP HIS MET ILE LYS PRO VAL GLU
SEQRES 1 D 723 GLY PRO GLY SER CYS PRO THR HIS ALA ASP SER LEU ASN
SEQRES 2 D 723 ASN LEU ALA ASN ILE LYS ARG GLU GLN GLY ASN ILE GLU
SEQRES 3 D 723 GLU ALA VAL ARG LEU TYR ARG LYS ALA LEU GLU VAL PHE
SEQRES 4 D 723 PRO GLU PHE ALA ALA ALA HIS SER ASN LEU ALA SER VAL
SEQRES 5 D 723 LEU GLN GLN GLN GLY LYS LEU GLN GLU ALA LEU MET HIS
SEQRES 6 D 723 TYR LYS GLU ALA ILE ARG ILE SER PRO THR PHE ALA ASP
SEQRES 7 D 723 ALA TYR SER ASN MET GLY ASN THR LEU LYS GLU MET GLN
SEQRES 8 D 723 ASP VAL GLN GLY ALA LEU GLN CYS TYR THR ARG ALA ILE
SEQRES 9 D 723 GLN ILE ASN PRO ALA PHE ALA ASP ALA HIS SER ASN LEU
SEQRES 10 D 723 ALA SER ILE HIS LYS ASP SER GLY ASN ILE PRO GLU ALA
SEQRES 11 D 723 ILE ALA SER TYR ARG THR ALA LEU LYS LEU LYS PRO ASP
SEQRES 12 D 723 PHE PRO ASP ALA TYR CYS ASN LEU ALA HIS CYS LEU GLN
SEQRES 13 D 723 ILE VAL CYS ASP TRP THR ASP TYR ASP GLU ARG MET LYS
SEQRES 14 D 723 LYS LEU VAL SER ILE VAL ALA ASP GLN LEU GLU LYS ASN
SEQRES 15 D 723 ARG LEU PRO SER VAL HIS PRO HIS HIS SER MET LEU TYR
SEQRES 16 D 723 PRO LEU SER HIS GLY PHE ARG LYS ALA ILE ALA GLU ARG
SEQRES 17 D 723 HIS GLY ASN LEU CYS LEU ASP LYS ILE ASN VAL LEU HIS
SEQRES 18 D 723 LYS PRO PRO TYR GLU HIS PRO LYS ASP LEU LYS LEU SER
SEQRES 19 D 723 ASP GLY ARG LEU ARG VAL GLY TYR VAL SER SER ASP PHE
SEQRES 20 D 723 GLY ASN HIS PRO THR SER HIS LEU MET GLN SER ILE PRO
SEQRES 21 D 723 GLY MET HIS ASN PRO ASP LYS PHE GLU VAL PHE CYS TYR
SEQRES 22 D 723 ALA LEU SER PRO ASP ASP GLY THR ASN PHE ARG VAL LYS
SEQRES 23 D 723 VAL MET ALA GLU ALA ASN HIS PHE ILE ASP LEU SER GLN
SEQRES 24 D 723 ILE PRO CYS ASN GLY LYS ALA ALA ASP ARG ILE HIS GLN
SEQRES 25 D 723 ASP GLY ILE HIS ILE LEU VAL ASN MET ASN GLY TYR THR
SEQRES 26 D 723 LYS GLY ALA ARG ASN GLU LEU PHE ALA LEU ARG PRO ALA
SEQRES 27 D 723 PRO ILE GLN ALA MET TRP LEU GLY TYR PRO GLY THR SER
SEQRES 28 D 723 GLY ALA LEU PHE MET ASP TYR ILE ILE THR ASP GLN GLU
SEQRES 29 D 723 THR SER PRO ALA GLU VAL ALA GLU GLN TYR SER GLU LYS
SEQRES 30 D 723 LEU ALA TYR MET PRO HIS THR PHE PHE ILE GLY ASP HIS
SEQRES 31 D 723 ALA ASN MET PHE PRO HIS LEU LYS LYS LYS ALA VAL ILE
SEQRES 32 D 723 ASP PHE LYS SER ASN GLY HIS ILE TYR ASP ASN ARG ILE
SEQRES 33 D 723 VAL LEU ASN GLY ILE ASP LEU LYS ALA PHE LEU ASP SER
SEQRES 34 D 723 LEU PRO ASP VAL LYS ILE VAL LYS MET LYS CYS PRO ASP
SEQRES 35 D 723 GLY GLY ASP ASN ALA ASP SER SER ASN THR ALA LEU ASN
SEQRES 36 D 723 MET PRO VAL ILE PRO MET ASN THR ILE ALA GLU ALA VAL
SEQRES 37 D 723 ILE GLU MET ILE ASN ARG GLY GLN ILE GLN ILE THR ILE
SEQRES 38 D 723 ASN GLY PHE SER ILE SER ASN GLY LEU ALA THR THR GLN
SEQRES 39 D 723 ILE ASN ASN LYS ALA ALA THR GLY GLU GLU VAL PRO ARG
SEQRES 40 D 723 THR ILE ILE VAL THR THR ARG SER GLN TYR GLY LEU PRO
SEQRES 41 D 723 GLU ASP ALA ILE VAL TYR CYS ASN PHE ASN GLN LEU TYR
SEQRES 42 D 723 LYS ILE ASP PRO SER THR LEU GLN MET TRP ALA ASN ILE
SEQRES 43 D 723 LEU LYS ARG VAL PRO ASN SER VAL LEU TRP LEU LEU ARG
SEQRES 44 D 723 PHE PRO ALA VAL GLY GLU PRO ASN ILE GLN GLN TYR ALA
SEQRES 45 D 723 GLN ASN MET GLY LEU PRO GLN ASN ARG ILE ILE PHE SER
SEQRES 46 D 723 PRO VAL ALA PRO LYS GLU GLU HIS VAL ARG ARG GLY GLN
SEQRES 47 D 723 LEU ALA ASP VAL CYS LEU ASP THR PRO LEU CYS ASN GLY
SEQRES 48 D 723 HIS THR THR GLY MET ASP VAL LEU TRP ALA GLY THR PRO
SEQRES 49 D 723 MET VAL THR MET PRO GLY GLU THR LEU ALA SER ARG VAL
SEQRES 50 D 723 ALA ALA SER GLN LEU THR CYS LEU GLY CYS LEU GLU LEU
SEQRES 51 D 723 ILE ALA LYS ASN ARG GLN GLU TYR GLU ASP ILE ALA VAL
SEQRES 52 D 723 LYS LEU GLY THR ASP LEU GLU TYR LEU LYS LYS VAL ARG
SEQRES 53 D 723 GLY LYS VAL TRP LYS GLN ARG ILE SER SER PRO LEU PHE
SEQRES 54 D 723 ASN THR LYS GLN TYR THR MET GLU LEU GLU ARG LEU TYR
SEQRES 55 D 723 LEU GLN MET TRP GLU HIS TYR ALA ALA GLY ASN LYS PRO
SEQRES 56 D 723 ASP HIS MET ILE LYS PRO VAL GLU
SEQRES 1 E 11 GLY PRO VAL PHE THR SER ARG SER ALA ALA GLY
SEQRES 1 F 11 GLY PRO VAL PHE THR SER ARG SER ALA ALA GLY
SEQRES 1 G 11 GLY PRO VAL PHE THR SER ARG SER ALA ALA GLY
SEQRES 1 H 11 GLY PRO VAL PHE THR SER ARG SER ALA ALA GLY
HET SO4 A1101 5
HET 12V A1102 39
HET SO4 B1101 5
HET 12V B1102 39
HET SO4 C1101 5
HET 12V C1102 39
HET 12V D1200 39
HET SO4 H2101 5
HETNAM SO4 SULFATE ION
HETNAM 12V (2S,3R,4R,5S,6R)-3-(ACETYLAMINO)-4,5-DIHYDROXY-6-
HETNAM 2 12V (HYDROXYMETHYL)TETRAHYDRO-2H-THIOPYRAN-2-YL [(2R,3S,
HETNAM 3 12V 4R,5R)-5-(2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL)-3,
HETNAM 4 12V 4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN
HETNAM 5 12V DIPHOSPHATE
HETSYN 12V URIDINE DIPHOSPHO-5-THIO-N-ACETYLGLUCOSAMINE
FORMUL 9 SO4 4(O4 S 2-)
FORMUL 10 12V 4(C17 H27 N3 O16 P2 S)
HELIX 1 AA1 CYS A 313 GLN A 330 1 18
HELIX 2 AA2 ASN A 332 PHE A 347 1 16
HELIX 3 AA3 PHE A 350 GLN A 364 1 15
HELIX 4 AA4 LYS A 366 SER A 381 1 16
HELIX 5 AA5 PHE A 384 MET A 398 1 15
HELIX 6 AA6 ASP A 400 ASN A 415 1 16
HELIX 7 AA7 PHE A 418 SER A 432 1 15
HELIX 8 AA8 ASN A 434 LYS A 449 1 16
HELIX 9 AA9 PHE A 452 CYS A 467 1 16
HELIX 10 AB1 ASP A 471 LYS A 489 1 19
HELIX 11 AB2 HIS A 499 TYR A 503 5 5
HELIX 12 AB3 SER A 506 VAL A 527 1 22
HELIX 13 AB4 HIS A 558 GLN A 565 1 8
HELIX 14 AB5 SER A 566 HIS A 571 1 6
HELIX 15 AB6 THR A 589 ALA A 599 1 11
HELIX 16 AB7 SER A 606 ILE A 608 5 3
HELIX 17 AB8 CYS A 610 GLY A 622 1 13
HELIX 18 AB9 ASN A 638 LEU A 643 1 6
HELIX 19 AC1 PRO A 675 TYR A 682 5 8
HELIX 20 AC2 ASP A 697 PHE A 702 1 6
HELIX 21 AC3 PRO A 703 LYS A 707 5 5
HELIX 22 AC4 ASP A 730 ASP A 736 1 7
HELIX 23 AC5 ASN A 770 GLY A 783 1 14
HELIX 24 AC6 ALA A 799 ASN A 804 1 6
HELIX 25 AC7 ASN A 804 THR A 809 1 6
HELIX 26 AC8 SER A 823 GLY A 826 5 4
HELIX 27 AC9 GLN A 839 ILE A 843 5 5
HELIX 28 AD1 ASP A 844 VAL A 858 1 15
HELIX 29 AD2 VAL A 871 ASN A 882 1 12
HELIX 30 AD3 PRO A 886 ASN A 888 5 3
HELIX 31 AD4 PRO A 897 ARG A 904 1 8
HELIX 32 AD5 GLY A 905 ALA A 908 5 4
HELIX 33 AD6 HIS A 920 GLY A 930 1 11
HELIX 34 AD7 THR A 940 SER A 943 5 4
HELIX 35 AD8 ARG A 944 GLY A 954 1 11
HELIX 36 AD9 CYS A 955 ILE A 959 5 5
HELIX 37 AE1 ASN A 962 ASP A 976 1 15
HELIX 38 AE2 ASP A 976 SER A 994 1 19
HELIX 39 AE3 ASN A 998 ALA A 1019 1 22
HELIX 40 AE4 CYS B 313 GLN B 330 1 18
HELIX 41 AE5 ASN B 332 PHE B 347 1 16
HELIX 42 AE6 PHE B 350 GLN B 364 1 15
HELIX 43 AE7 LYS B 366 SER B 381 1 16
HELIX 44 AE8 PHE B 384 MET B 398 1 15
HELIX 45 AE9 ASP B 400 ASN B 415 1 16
HELIX 46 AF1 PHE B 418 SER B 432 1 15
HELIX 47 AF2 ASN B 434 LYS B 449 1 16
HELIX 48 AF3 PHE B 452 CYS B 467 1 16
HELIX 49 AF4 ASP B 471 LYS B 489 1 19
HELIX 50 AF5 HIS B 496 MET B 501 1 6
HELIX 51 AF6 SER B 506 VAL B 527 1 22
HELIX 52 AF7 HIS B 558 GLN B 565 1 8
HELIX 53 AF8 SER B 566 HIS B 571 1 6
HELIX 54 AF9 THR B 589 ALA B 599 1 11
HELIX 55 AG1 SER B 606 ILE B 608 5 3
HELIX 56 AG2 CYS B 610 GLY B 622 1 13
HELIX 57 AG3 ASN B 638 LEU B 643 1 6
HELIX 58 AG4 PRO B 675 TYR B 682 5 8
HELIX 59 AG5 ASP B 697 PHE B 702 1 6
HELIX 60 AG6 PRO B 703 LYS B 707 5 5
HELIX 61 AG7 ASP B 730 ASP B 736 1 7
HELIX 62 AG8 ASN B 770 GLY B 783 1 14
HELIX 63 AG9 ALA B 799 ASN B 804 1 6
HELIX 64 AH1 ASN B 804 THR B 809 1 6
HELIX 65 AH2 SER B 823 GLY B 826 5 4
HELIX 66 AH3 GLN B 839 ILE B 843 5 5
HELIX 67 AH4 ASP B 844 VAL B 858 1 15
HELIX 68 AH5 VAL B 871 ASN B 882 1 12
HELIX 69 AH6 PRO B 886 ASN B 888 5 3
HELIX 70 AH7 PRO B 897 GLY B 905 1 9
HELIX 71 AH8 GLN B 906 ALA B 908 5 3
HELIX 72 AH9 HIS B 920 GLY B 930 1 11
HELIX 73 AI1 THR B 940 SER B 943 5 4
HELIX 74 AI2 ARG B 944 GLY B 954 1 11
HELIX 75 AI3 CYS B 955 ILE B 959 5 5
HELIX 76 AI4 ASN B 962 ASP B 976 1 15
HELIX 77 AI5 ASP B 976 SER B 994 1 19
HELIX 78 AI6 ASN B 998 ALA B 1019 1 22
HELIX 79 AI7 CYS C 313 GLN C 330 1 18
HELIX 80 AI8 ASN C 332 PHE C 347 1 16
HELIX 81 AI9 PHE C 350 GLN C 364 1 15
HELIX 82 AJ1 LYS C 366 SER C 381 1 16
HELIX 83 AJ2 PHE C 384 MET C 398 1 15
HELIX 84 AJ3 ASP C 400 ASN C 415 1 16
HELIX 85 AJ4 PHE C 418 SER C 432 1 15
HELIX 86 AJ5 ASN C 434 LYS C 449 1 16
HELIX 87 AJ6 PHE C 452 CYS C 467 1 16
HELIX 88 AJ7 ASP C 471 LYS C 489 1 19
HELIX 89 AJ8 HIS C 496 TYR C 503 5 8
HELIX 90 AJ9 SER C 506 VAL C 527 1 22
HELIX 91 AK1 HIS C 558 GLN C 565 1 8
HELIX 92 AK2 SER C 566 HIS C 571 1 6
HELIX 93 AK3 THR C 589 ALA C 599 1 11
HELIX 94 AK4 SER C 606 ILE C 608 5 3
HELIX 95 AK5 CYS C 610 GLY C 622 1 13
HELIX 96 AK6 ASN C 638 LEU C 643 1 6
HELIX 97 AK7 PRO C 675 TYR C 682 5 8
HELIX 98 AK8 ASP C 697 PHE C 702 1 6
HELIX 99 AK9 PRO C 703 LYS C 707 5 5
HELIX 100 AL1 ASP C 730 ASP C 736 1 7
HELIX 101 AL2 ASN C 770 GLY C 783 1 14
HELIX 102 AL3 ALA C 799 ASN C 804 1 6
HELIX 103 AL4 ASN C 804 THR C 809 1 6
HELIX 104 AL5 SER C 823 GLY C 826 5 4
HELIX 105 AL6 GLN C 839 ILE C 843 5 5
HELIX 106 AL7 ASP C 844 VAL C 858 1 15
HELIX 107 AL8 VAL C 871 ASN C 882 1 12
HELIX 108 AL9 PRO C 886 ASN C 888 5 3
HELIX 109 AM1 PRO C 897 GLY C 905 1 9
HELIX 110 AM2 GLN C 906 ALA C 908 5 3
HELIX 111 AM3 HIS C 920 ALA C 929 1 10
HELIX 112 AM4 THR C 940 GLY C 954 1 15
HELIX 113 AM5 CYS C 955 ILE C 959 5 5
HELIX 114 AM6 ASN C 962 ASP C 976 1 15
HELIX 115 AM7 ASP C 976 SER C 994 1 19
HELIX 116 AM8 ASN C 998 ALA C 1019 1 22
HELIX 117 AM9 CYS D 313 GLN D 330 1 18
HELIX 118 AN1 ASN D 332 PHE D 347 1 16
HELIX 119 AN2 PHE D 350 GLN D 364 1 15
HELIX 120 AN3 LYS D 366 SER D 381 1 16
HELIX 121 AN4 PHE D 384 MET D 398 1 15
HELIX 122 AN5 ASP D 400 ASN D 415 1 16
HELIX 123 AN6 PHE D 418 SER D 432 1 15
HELIX 124 AN7 ASN D 434 LYS D 449 1 16
HELIX 125 AN8 PHE D 452 CYS D 467 1 16
HELIX 126 AN9 ASP D 471 LYS D 489 1 19
HELIX 127 AO1 HIS D 496 TYR D 503 5 8
HELIX 128 AO2 SER D 506 VAL D 527 1 22
HELIX 129 AO3 HIS D 558 GLN D 565 1 8
HELIX 130 AO4 SER D 566 HIS D 571 1 6
HELIX 131 AO5 THR D 589 ALA D 599 1 11
HELIX 132 AO6 SER D 606 ILE D 608 5 3
HELIX 133 AO7 CYS D 610 GLY D 622 1 13
HELIX 134 AO8 ASN D 638 LEU D 643 1 6
HELIX 135 AO9 PRO D 675 TYR D 682 5 8
HELIX 136 AP1 ASP D 697 PHE D 702 1 6
HELIX 137 AP2 PRO D 703 LYS D 707 5 5
HELIX 138 AP3 ASP D 730 ASP D 736 1 7
HELIX 139 AP4 ASN D 770 GLY D 783 1 14
HELIX 140 AP5 ALA D 799 ASN D 804 1 6
HELIX 141 AP6 ASN D 804 THR D 809 1 6
HELIX 142 AP7 SER D 823 GLY D 826 5 4
HELIX 143 AP8 GLN D 839 ILE D 843 5 5
HELIX 144 AP9 ASP D 844 VAL D 858 1 15
HELIX 145 AQ1 VAL D 871 ASN D 882 1 12
HELIX 146 AQ2 PRO D 886 ASN D 888 5 3
HELIX 147 AQ3 PRO D 897 GLY D 905 1 9
HELIX 148 AQ4 GLN D 906 ALA D 908 5 3
HELIX 149 AQ5 HIS D 920 GLY D 930 1 11
HELIX 150 AQ6 THR D 940 SER D 943 5 4
HELIX 151 AQ7 ARG D 944 GLY D 954 1 11
HELIX 152 AQ8 CYS D 955 ILE D 959 5 5
HELIX 153 AQ9 ASN D 962 ASP D 976 1 15
HELIX 154 AR1 ASP D 976 SER D 994 1 19
HELIX 155 AR2 ASN D 998 ALA D 1019 1 22
SHEET 1 AA1 7 HIS A 601 ASP A 604 0
SHEET 2 AA1 7 PHE A 576 ALA A 582 1 N CYS A 580 O ILE A 603
SHEET 3 AA1 7 LEU A 546 SER A 552 1 N TYR A 550 O TYR A 581
SHEET 4 AA1 7 ILE A 625 ASN A 628 1 O VAL A 627 N GLY A 549
SHEET 5 AA1 7 ILE A 648 TRP A 652 1 O ALA A 650 N ASN A 628
SHEET 6 AA1 7 TYR A 666 ASP A 670 1 O ILE A 668 N MET A 651
SHEET 7 AA1 7 LYS A 685 MET A 689 1 O ALA A 687 N THR A 669
SHEET 1 AA2 7 LYS A 742 LYS A 745 0
SHEET 2 AA2 7 ASN A 763 ILE A 767 -1 O VAL A 766 N LYS A 742
SHEET 3 AA2 7 ALA A 709 ILE A 711 1 N VAL A 710 O ILE A 767
SHEET 4 AA2 7 ILE A 724 ASN A 727 -1 O LEU A 726 N ALA A 709
SHEET 5 AA2 7 ILE A 817 THR A 821 -1 O ILE A 818 N ASN A 727
SHEET 6 AA2 7 PHE A 792 ASN A 796 1 N SER A 795 O ILE A 817
SHEET 7 AA2 7 GLN A 786 ILE A 789 -1 N ILE A 787 O ILE A 794
SHEET 1 AA3 5 ILE A 890 SER A 893 0
SHEET 2 AA3 5 SER A 861 LEU A 866 1 N LEU A 863 O ILE A 891
SHEET 3 AA3 5 ILE A 832 CYS A 835 1 N TYR A 834 O TRP A 864
SHEET 4 AA3 5 VAL A 910 LEU A 912 1 O VAL A 910 N CYS A 835
SHEET 5 AA3 5 MET A 933 VAL A 934 1 O VAL A 934 N CYS A 911
SHEET 1 AA4 7 HIS B 601 ASP B 604 0
SHEET 2 AA4 7 PHE B 576 ALA B 582 1 N CYS B 580 O ILE B 603
SHEET 3 AA4 7 LEU B 546 SER B 552 1 N TYR B 550 O TYR B 581
SHEET 4 AA4 7 ILE B 625 ASN B 628 1 O VAL B 627 N GLY B 549
SHEET 5 AA4 7 ILE B 648 MET B 651 1 O ALA B 650 N ASN B 628
SHEET 6 AA4 7 TYR B 666 ASP B 670 1 O ILE B 668 N MET B 651
SHEET 7 AA4 7 LYS B 685 MET B 689 1 O ALA B 687 N THR B 669
SHEET 1 AA5 7 LYS B 742 LYS B 745 0
SHEET 2 AA5 7 ASN B 763 ILE B 767 -1 O VAL B 766 N LYS B 742
SHEET 3 AA5 7 ALA B 709 ILE B 711 1 N VAL B 710 O ILE B 767
SHEET 4 AA5 7 ILE B 724 ASN B 727 -1 O LEU B 726 N ALA B 709
SHEET 5 AA5 7 ILE B 817 THR B 821 -1 O ILE B 818 N ASN B 727
SHEET 6 AA5 7 PHE B 792 ASN B 796 1 N SER B 795 O ILE B 817
SHEET 7 AA5 7 GLN B 786 ILE B 789 -1 N ILE B 787 O ILE B 794
SHEET 1 AA6 5 ILE B 890 SER B 893 0
SHEET 2 AA6 5 SER B 861 LEU B 866 1 N LEU B 863 O ILE B 891
SHEET 3 AA6 5 ILE B 832 CYS B 835 1 N TYR B 834 O TRP B 864
SHEET 4 AA6 5 VAL B 910 LEU B 912 1 N VAL B 910 O VAL B 833
SHEET 5 AA6 5 MET B 933 VAL B 934 1 O VAL B 934 N CYS B 911
SHEET 1 AA7 7 HIS C 601 ASP C 604 0
SHEET 2 AA7 7 PHE C 576 ALA C 582 1 N CYS C 580 O ILE C 603
SHEET 3 AA7 7 LEU C 546 SER C 552 1 N TYR C 550 O TYR C 581
SHEET 4 AA7 7 ILE C 625 ASN C 628 1 O VAL C 627 N GLY C 549
SHEET 5 AA7 7 ILE C 648 MET C 651 1 O ALA C 650 N ASN C 628
SHEET 6 AA7 7 TYR C 666 ASP C 670 1 O ILE C 668 N MET C 651
SHEET 7 AA7 7 LYS C 685 MET C 689 1 O ALA C 687 N THR C 669
SHEET 1 AA8 7 LYS C 742 LYS C 745 0
SHEET 2 AA8 7 ASN C 763 ILE C 767 -1 O VAL C 766 N LYS C 742
SHEET 3 AA8 7 ALA C 709 ILE C 711 1 N VAL C 710 O ILE C 767
SHEET 4 AA8 7 ILE C 724 ASN C 727 -1 O LEU C 726 N ALA C 709
SHEET 5 AA8 7 ILE C 817 THR C 821 -1 O ILE C 818 N ASN C 727
SHEET 6 AA8 7 PHE C 792 ASN C 796 1 N SER C 795 O ILE C 817
SHEET 7 AA8 7 GLN C 786 ILE C 789 -1 N ILE C 787 O ILE C 794
SHEET 1 AA9 5 ILE C 890 SER C 893 0
SHEET 2 AA9 5 SER C 861 LEU C 866 1 N LEU C 863 O ILE C 891
SHEET 3 AA9 5 ILE C 832 ASN C 836 1 N TYR C 834 O TRP C 864
SHEET 4 AA9 5 VAL C 910 LEU C 912 1 O LEU C 912 N CYS C 835
SHEET 5 AA9 5 MET C 933 VAL C 934 1 O VAL C 934 N CYS C 911
SHEET 1 AB1 7 HIS D 601 ASP D 604 0
SHEET 2 AB1 7 PHE D 576 ALA D 582 1 N CYS D 580 O ILE D 603
SHEET 3 AB1 7 LEU D 546 SER D 552 1 N TYR D 550 O TYR D 581
SHEET 4 AB1 7 ILE D 625 ASN D 628 1 O VAL D 627 N GLY D 549
SHEET 5 AB1 7 ILE D 648 TRP D 652 1 O ALA D 650 N ASN D 628
SHEET 6 AB1 7 TYR D 666 ASP D 670 1 O ILE D 668 N MET D 651
SHEET 7 AB1 7 LYS D 685 MET D 689 1 O MET D 689 N THR D 669
SHEET 1 AB2 7 LYS D 742 LYS D 745 0
SHEET 2 AB2 7 ASN D 763 ILE D 767 -1 O VAL D 766 N LYS D 742
SHEET 3 AB2 7 ALA D 709 ILE D 711 1 N VAL D 710 O ILE D 767
SHEET 4 AB2 7 ILE D 724 ASN D 727 -1 O LEU D 726 N ALA D 709
SHEET 5 AB2 7 ILE D 817 THR D 821 -1 O ILE D 818 N ASN D 727
SHEET 6 AB2 7 PHE D 792 ASN D 796 1 N SER D 795 O ILE D 817
SHEET 7 AB2 7 GLN D 786 ILE D 789 -1 N ILE D 789 O PHE D 792
SHEET 1 AB3 5 ILE D 890 SER D 893 0
SHEET 2 AB3 5 SER D 861 LEU D 866 1 N LEU D 863 O ILE D 891
SHEET 3 AB3 5 ILE D 832 CYS D 835 1 N TYR D 834 O TRP D 864
SHEET 4 AB3 5 VAL D 910 LEU D 912 1 O VAL D 910 N CYS D 835
SHEET 5 AB3 5 MET D 933 VAL D 934 1 O VAL D 934 N CYS D 911
CISPEP 1 PHE A 868 PRO A 869 0 3.32
CISPEP 2 PHE B 868 PRO B 869 0 2.53
CISPEP 3 PHE C 868 PRO C 869 0 -1.72
CISPEP 4 PHE D 868 PRO D 869 0 2.77
SITE 1 AC1 4 THR A 633 LYS A 634 GLY A 635 ALA E2016
SITE 1 AC2 19 HIS A 498 PRO A 559 THR A 560 LEU A 563
SITE 2 AC2 19 LEU A 653 GLY A 654 PRO A 656 GLN A 839
SITE 3 AC2 19 LYS A 842 VAL A 895 ALA A 896 LYS A 898
SITE 4 AC2 19 HIS A 901 ARG A 904 HIS A 920 THR A 921
SITE 5 AC2 19 THR A 922 ASP A 925 SER E2012
SITE 1 AC3 4 LYS B 634 GLY B 635 ALA F2015 ALA F2016
SITE 1 AC4 21 HIS B 498 PRO B 559 THR B 560 LEU B 653
SITE 2 AC4 21 GLY B 654 PRO B 656 GLN B 839 TYR B 841
SITE 3 AC4 21 LYS B 842 LEU B 866 VAL B 895 ALA B 896
SITE 4 AC4 21 LYS B 898 HIS B 901 ARG B 904 HIS B 920
SITE 5 AC4 21 THR B 921 THR B 922 ASP B 925 VAL F2009
SITE 6 AC4 21 SER F2012
SITE 1 AC5 4 LYS C 634 GLY C 635 ALA G2015 ALA G2016
SITE 1 AC6 21 HIS C 498 PRO C 559 THR C 560 LEU C 653
SITE 2 AC6 21 GLY C 654 PRO C 656 GLN C 839 TYR C 841
SITE 3 AC6 21 LYS C 842 VAL C 895 ALA C 896 LYS C 898
SITE 4 AC6 21 HIS C 901 ARG C 904 CYS C 917 HIS C 920
SITE 5 AC6 21 THR C 921 THR C 922 ASP C 925 VAL G2009
SITE 6 AC6 21 SER G2012
SITE 1 AC7 22 HIS D 498 PRO D 559 THR D 560 LEU D 653
SITE 2 AC7 22 GLY D 654 PHE D 694 GLN D 839 LYS D 842
SITE 3 AC7 22 LEU D 866 VAL D 895 ALA D 896 LYS D 898
SITE 4 AC7 22 HIS D 901 ARG D 904 HIS D 920 THR D 921
SITE 5 AC7 22 THR D 922 ASP D 925 VAL H2009 PHE H2010
SITE 6 AC7 22 THR H2011 SER H2012
SITE 1 AC8 4 LYS D 634 GLY D 635 ALA H2015 ALA H2016
CRYST1 275.138 275.138 143.136 90.00 90.00 120.00 P 3 2 1 24
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 0.003635 0.002098 0.000000 0.00000
SCALE2 0.000000 0.004197 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006986 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
