HEADER TRANSFERASE/TRANSFERASE INHIBITOR 18-NOV-11 3UPF
TITLE CRYSTAL STRUCTURE OF MURINE NOROVIRUS RNA-DEPENDENT RNA POLYMERASE
TITLE 2 BOUND TO NF023
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA-DEPENDENT RNA POLYMERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 1174-1684;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MURINE NOROVIRUS 1;
SOURCE 3 ORGANISM_TAXID: 223997;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MURINE NOROVIRUS, RNA-DEPENDENT RNA POLYMERASE, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MILANI,E.MASTRANGELO,M.BOLOGNESI
REVDAT 3 28-FEB-24 3UPF 1 REMARK SEQADV
REVDAT 2 23-MAY-12 3UPF 1 JRNL
REVDAT 1 02-MAY-12 3UPF 0
JRNL AUTH E.MASTRANGELO,M.PEZZULLO,D.TARANTINO,R.PETAZZI,F.GERMANI,
JRNL AUTH 2 D.KRAMER,I.ROBEL,J.ROHAYEM,M.BOLOGNESI,M.MILANI
JRNL TITL STRUCTURE-BASED INHIBITION OF NOROVIRUS RNA-DEPENDENT RNA
JRNL TITL 2 POLYMERASES.
JRNL REF J.MOL.BIOL. V. 419 198 2012
JRNL REFN ISSN 0022-2836
JRNL PMID 22446684
JRNL DOI 10.1016/J.JMB.2012.03.008
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 67276
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3578
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4954
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE SET COUNT : 256
REMARK 3 BIN FREE R VALUE : 0.3770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11376
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 233
REMARK 3 SOLVENT ATOMS : 625
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.44000
REMARK 3 B22 (A**2) : 0.50000
REMARK 3 B33 (A**2) : -1.61000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.82000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.294
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.222
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.969
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11900 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16165 ; 1.267 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1419 ; 5.513 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 539 ;35.095 ;23.117
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2011 ;18.158 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 108 ;19.754 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1697 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9099 ; 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): 7141 ; 1.178 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11507 ; 2.246 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4759 ; 3.599 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4657 ; 5.624 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 488
REMARK 3 RESIDUE RANGE : A 600 A 600
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9100 -49.9540 33.1490
REMARK 3 T TENSOR
REMARK 3 T11: 0.0821 T22: 0.0902
REMARK 3 T33: 0.0119 T12: 0.0497
REMARK 3 T13: -0.0225 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 0.5418 L22: 0.2834
REMARK 3 L33: 0.4068 L12: 0.0665
REMARK 3 L13: -0.1111 L23: 0.3392
REMARK 3 S TENSOR
REMARK 3 S11: 0.0898 S12: 0.0235 S13: -0.0247
REMARK 3 S21: 0.0381 S22: -0.0401 S23: -0.0593
REMARK 3 S31: 0.0108 S32: -0.0615 S33: -0.0497
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 488
REMARK 3 RESIDUE RANGE : B 600 B 600
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1810 -46.8830 -11.1160
REMARK 3 T TENSOR
REMARK 3 T11: 0.0955 T22: 0.0730
REMARK 3 T33: 0.0569 T12: 0.0373
REMARK 3 T13: 0.0217 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 0.0381 L22: 0.4056
REMARK 3 L33: 0.4930 L12: 0.0879
REMARK 3 L13: -0.0080 L23: -0.3476
REMARK 3 S TENSOR
REMARK 3 S11: 0.0012 S12: -0.0197 S13: -0.0009
REMARK 3 S21: -0.0171 S22: 0.0217 S23: -0.0226
REMARK 3 S31: -0.0080 S32: -0.0186 S33: -0.0229
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 5 C 488
REMARK 3 RESIDUE RANGE : C 600 C 600
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1430 0.3580 23.1430
REMARK 3 T TENSOR
REMARK 3 T11: 0.1295 T22: 0.0612
REMARK 3 T33: 0.0467 T12: 0.0200
REMARK 3 T13: 0.0301 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.1985 L22: 0.2665
REMARK 3 L33: 0.2321 L12: -0.0277
REMARK 3 L13: -0.0435 L23: -0.1856
REMARK 3 S TENSOR
REMARK 3 S11: -0.0065 S12: 0.0086 S13: 0.0239
REMARK 3 S21: 0.0085 S22: 0.0062 S23: -0.0100
REMARK 3 S31: 0.0156 S32: 0.0014 S33: 0.0003
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: NULL
REMARK 4
REMARK 4 3UPF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000069044.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70871
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULFATE, 11 % GLYCEROL,
REMARK 280 50 MM TRIS PH 8.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 60.43000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 97.97500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.43000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 97.97500
REMARK 290 SMTRY3 4 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 121470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -259.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 -9
REMARK 465 LYS A -8
REMARK 465 ALA A -7
REMARK 465 LEU A -6
REMARK 465 GLU A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 GLY A -2
REMARK 465 PRO A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 GLY A 301
REMARK 465 GLY A 377
REMARK 465 ALA A 434
REMARK 465 GLN A 435
REMARK 465 SER A 438
REMARK 465 GLN A 468
REMARK 465 SER A 469
REMARK 465 GLY A 470
REMARK 465 ILE A 471
REMARK 465 GLU A 472
REMARK 465 MET A 473
REMARK 465 THR A 489
REMARK 465 MET A 490
REMARK 465 ASP A 491
REMARK 465 ALA A 492
REMARK 465 GLU A 493
REMARK 465 THR A 494
REMARK 465 PRO A 495
REMARK 465 GLN A 496
REMARK 465 GLU A 497
REMARK 465 ARG A 498
REMARK 465 SER A 499
REMARK 465 ALA A 500
REMARK 465 VAL A 501
REMARK 465 PHE A 502
REMARK 465 VAL A 503
REMARK 465 ASN A 504
REMARK 465 GLU A 505
REMARK 465 ASP A 506
REMARK 465 GLU A 507
REMARK 465 LEU A 508
REMARK 465 GLU A 509
REMARK 465 HIS A 510
REMARK 465 HIS A 511
REMARK 465 HIS A 512
REMARK 465 HIS A 513
REMARK 465 HIS A 514
REMARK 465 HIS A 515
REMARK 465 MET B -9
REMARK 465 LYS B -8
REMARK 465 ALA B -7
REMARK 465 LEU B -6
REMARK 465 GLU B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 PRO B 303
REMARK 465 ILE B 471
REMARK 465 GLU B 472
REMARK 465 MET B 473
REMARK 465 THR B 489
REMARK 465 MET B 490
REMARK 465 ASP B 491
REMARK 465 ALA B 492
REMARK 465 GLU B 493
REMARK 465 THR B 494
REMARK 465 PRO B 495
REMARK 465 GLN B 496
REMARK 465 GLU B 497
REMARK 465 ARG B 498
REMARK 465 SER B 499
REMARK 465 ALA B 500
REMARK 465 VAL B 501
REMARK 465 PHE B 502
REMARK 465 VAL B 503
REMARK 465 ASN B 504
REMARK 465 GLU B 505
REMARK 465 ASP B 506
REMARK 465 GLU B 507
REMARK 465 LEU B 508
REMARK 465 GLU B 509
REMARK 465 HIS B 510
REMARK 465 HIS B 511
REMARK 465 HIS B 512
REMARK 465 HIS B 513
REMARK 465 HIS B 514
REMARK 465 HIS B 515
REMARK 465 MET C -9
REMARK 465 LYS C -8
REMARK 465 ALA C -7
REMARK 465 LEU C -6
REMARK 465 GLU C -5
REMARK 465 PHE C -4
REMARK 465 GLN C -3
REMARK 465 GLY C -2
REMARK 465 PRO C -1
REMARK 465 PRO C 0
REMARK 465 MET C 1
REMARK 465 LEU C 2
REMARK 465 PRO C 3
REMARK 465 ARG C 4
REMARK 465 PRO C 303
REMARK 465 CYS C 304
REMARK 465 HIS C 433
REMARK 465 ALA C 434
REMARK 465 ALA C 466
REMARK 465 ALA C 467
REMARK 465 GLN C 468
REMARK 465 SER C 469
REMARK 465 GLY C 470
REMARK 465 ILE C 471
REMARK 465 GLU C 472
REMARK 465 MET C 473
REMARK 465 VAL C 474
REMARK 465 THR C 489
REMARK 465 MET C 490
REMARK 465 ASP C 491
REMARK 465 ALA C 492
REMARK 465 GLU C 493
REMARK 465 THR C 494
REMARK 465 PRO C 495
REMARK 465 GLN C 496
REMARK 465 GLU C 497
REMARK 465 ARG C 498
REMARK 465 SER C 499
REMARK 465 ALA C 500
REMARK 465 VAL C 501
REMARK 465 PHE C 502
REMARK 465 VAL C 503
REMARK 465 ASN C 504
REMARK 465 GLU C 505
REMARK 465 ASP C 506
REMARK 465 GLU C 507
REMARK 465 LEU C 508
REMARK 465 GLU C 509
REMARK 465 HIS C 510
REMARK 465 HIS C 511
REMARK 465 HIS C 512
REMARK 465 HIS C 513
REMARK 465 HIS C 514
REMARK 465 HIS C 515
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 HIS A 124 45.08 39.09
REMARK 500 CYS A 210 6.57 -64.39
REMARK 500 LEU A 265 30.81 -98.69
REMARK 500 PRO A 299 91.48 -59.45
REMARK 500 ASP A 354 92.22 -67.53
REMARK 500 LEU A 368 72.44 -113.87
REMARK 500 LYS A 374 -3.33 91.11
REMARK 500 LYS A 464 2.79 -66.18
REMARK 500 ALA B 45 156.74 -48.40
REMARK 500 ASP B 51 105.55 -49.55
REMARK 500 HIS B 124 45.40 36.79
REMARK 500 SER B 134 -12.10 -144.37
REMARK 500 ASP B 242 72.78 40.44
REMARK 500 SER B 300 -163.47 -65.65
REMARK 500 ALA B 434 88.58 -54.80
REMARK 500 SER B 469 -8.33 -140.16
REMARK 500 ILE C 137 -169.58 -113.86
REMARK 500 ASP C 242 76.64 45.29
REMARK 500 PRO C 282 123.83 -36.67
REMARK 500 SER C 300 2.24 -53.80
REMARK 500 PHE C 487 -87.09 -125.47
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 0BU A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0BU B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0BU C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 519
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NAH RELATED DB: PDB
REMARK 900 RELATED ID: 3NAI RELATED DB: PDB
REMARK 900 RELATED ID: 3UQS RELATED DB: PDB
REMARK 900 RELATED ID: 3UR0 RELATED DB: PDB
DBREF 3UPF A -6 507 UNP Q80J95 Q80J95_9CALI 1174 1687
DBREF 3UPF B -6 507 UNP Q80J95 Q80J95_9CALI 1174 1687
DBREF 3UPF C -6 507 UNP Q80J95 Q80J95_9CALI 1174 1687
SEQADV 3UPF MET A -9 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF LYS A -8 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF ALA A -7 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF LEU A 508 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF GLU A 509 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS A 510 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS A 511 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS A 512 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS A 513 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS A 514 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS A 515 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF MET B -9 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF LYS B -8 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF ALA B -7 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF LEU B 508 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF GLU B 509 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS B 510 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS B 511 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS B 512 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS B 513 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS B 514 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS B 515 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF MET C -9 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF LYS C -8 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF ALA C -7 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF LEU C 508 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF GLU C 509 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS C 510 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS C 511 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS C 512 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS C 513 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS C 514 UNP Q80J95 EXPRESSION TAG
SEQADV 3UPF HIS C 515 UNP Q80J95 EXPRESSION TAG
SEQRES 1 A 525 MET LYS ALA LEU GLU PHE GLN GLY PRO PRO MET LEU PRO
SEQRES 2 A 525 ARG PRO SER GLY THR TYR ALA GLY LEU PRO ILE ALA ASP
SEQRES 3 A 525 TYR GLY ASP ALA PRO PRO LEU SER THR LYS THR MET PHE
SEQRES 4 A 525 TRP ARG THR SER PRO GLU LYS LEU PRO PRO GLY ALA TRP
SEQRES 5 A 525 GLU PRO ALA TYR LEU GLY SER LYS ASP GLU ARG VAL ASP
SEQRES 6 A 525 GLY PRO SER LEU GLN GLN VAL MET ARG ASP GLN LEU LYS
SEQRES 7 A 525 PRO TYR SER GLU PRO ARG GLY LEU LEU PRO PRO GLN GLU
SEQRES 8 A 525 ILE LEU ASP ALA VAL CYS ASP ALA ILE GLU ASN ARG LEU
SEQRES 9 A 525 GLU ASN THR LEU GLU PRO GLN LYS PRO TRP THR PHE LYS
SEQRES 10 A 525 LYS ALA CYS GLU SER LEU ASP LYS ASN THR SER SER GLY
SEQRES 11 A 525 TYR PRO TYR HIS LYS GLN LYS SER LYS ASP TRP THR GLY
SEQRES 12 A 525 SER ALA PHE ILE GLY ASP LEU GLY ASP GLN ALA THR HIS
SEQRES 13 A 525 ALA ASN ASN MET TYR GLU MET GLY LYS SER MET ARG PRO
SEQRES 14 A 525 ILE TYR THR ALA ALA LEU LYS ASP GLU LEU VAL LYS PRO
SEQRES 15 A 525 ASP LYS ILE TYR GLY LYS ILE LYS LYS ARG LEU LEU TRP
SEQRES 16 A 525 GLY SER ASP LEU GLY THR MET ILE ARG ALA ALA ARG ALA
SEQRES 17 A 525 PHE GLY PRO PHE CYS ASP ALA LEU LYS GLU THR CYS ILE
SEQRES 18 A 525 PHE ASN PRO ILE ARG VAL GLY MET SER MET ASN GLU ASP
SEQRES 19 A 525 GLY PRO PHE ILE PHE ALA ARG HIS ALA ASN PHE ARG TYR
SEQRES 20 A 525 HIS MET ASP ALA ASP TYR THR ARG TRP ASP SER THR GLN
SEQRES 21 A 525 GLN ARG ALA ILE LEU LYS ARG ALA GLY ASP ILE MET VAL
SEQRES 22 A 525 ARG LEU SER PRO GLU PRO ASP LEU ALA ARG VAL VAL MET
SEQRES 23 A 525 ASP ASP LEU LEU ALA PRO SER LEU LEU ASP VAL GLY ASP
SEQRES 24 A 525 TYR LYS ILE VAL VAL GLU GLU GLY LEU PRO SER GLY CYS
SEQRES 25 A 525 PRO CYS THR THR GLN LEU ASN SER LEU ALA HIS TRP ILE
SEQRES 26 A 525 LEU THR LEU CYS ALA MET VAL GLU VAL THR ARG VAL ASP
SEQRES 27 A 525 PRO ASP ILE VAL MET GLN GLU SER GLU PHE SER PHE TYR
SEQRES 28 A 525 GLY ASP ASP GLU VAL VAL SER THR ASN LEU GLU LEU ASP
SEQRES 29 A 525 MET VAL LYS TYR THR MET ALA LEU ARG ARG TYR GLY LEU
SEQRES 30 A 525 LEU PRO THR ARG ALA ASP LYS GLU GLU GLY PRO LEU GLU
SEQRES 31 A 525 ARG ARG GLN THR LEU GLN GLY ILE SER PHE LEU ARG ARG
SEQRES 32 A 525 ALA ILE VAL GLY ASP GLN PHE GLY TRP TYR GLY ARG LEU
SEQRES 33 A 525 ASP ARG ALA SER ILE ASP ARG GLN LEU LEU TRP THR LYS
SEQRES 34 A 525 GLY PRO ASN HIS GLN ASN PRO PHE GLU THR LEU PRO GLY
SEQRES 35 A 525 HIS ALA GLN ARG PRO SER GLN LEU MET ALA LEU LEU GLY
SEQRES 36 A 525 GLU ALA ALA MET HIS GLY GLU LYS TYR TYR ARG THR VAL
SEQRES 37 A 525 ALA SER ARG VAL SER LYS GLU ALA ALA GLN SER GLY ILE
SEQRES 38 A 525 GLU MET VAL VAL PRO ARG HIS ARG SER VAL LEU ARG TRP
SEQRES 39 A 525 VAL ARG PHE GLY THR MET ASP ALA GLU THR PRO GLN GLU
SEQRES 40 A 525 ARG SER ALA VAL PHE VAL ASN GLU ASP GLU LEU GLU HIS
SEQRES 41 A 525 HIS HIS HIS HIS HIS
SEQRES 1 B 525 MET LYS ALA LEU GLU PHE GLN GLY PRO PRO MET LEU PRO
SEQRES 2 B 525 ARG PRO SER GLY THR TYR ALA GLY LEU PRO ILE ALA ASP
SEQRES 3 B 525 TYR GLY ASP ALA PRO PRO LEU SER THR LYS THR MET PHE
SEQRES 4 B 525 TRP ARG THR SER PRO GLU LYS LEU PRO PRO GLY ALA TRP
SEQRES 5 B 525 GLU PRO ALA TYR LEU GLY SER LYS ASP GLU ARG VAL ASP
SEQRES 6 B 525 GLY PRO SER LEU GLN GLN VAL MET ARG ASP GLN LEU LYS
SEQRES 7 B 525 PRO TYR SER GLU PRO ARG GLY LEU LEU PRO PRO GLN GLU
SEQRES 8 B 525 ILE LEU ASP ALA VAL CYS ASP ALA ILE GLU ASN ARG LEU
SEQRES 9 B 525 GLU ASN THR LEU GLU PRO GLN LYS PRO TRP THR PHE LYS
SEQRES 10 B 525 LYS ALA CYS GLU SER LEU ASP LYS ASN THR SER SER GLY
SEQRES 11 B 525 TYR PRO TYR HIS LYS GLN LYS SER LYS ASP TRP THR GLY
SEQRES 12 B 525 SER ALA PHE ILE GLY ASP LEU GLY ASP GLN ALA THR HIS
SEQRES 13 B 525 ALA ASN ASN MET TYR GLU MET GLY LYS SER MET ARG PRO
SEQRES 14 B 525 ILE TYR THR ALA ALA LEU LYS ASP GLU LEU VAL LYS PRO
SEQRES 15 B 525 ASP LYS ILE TYR GLY LYS ILE LYS LYS ARG LEU LEU TRP
SEQRES 16 B 525 GLY SER ASP LEU GLY THR MET ILE ARG ALA ALA ARG ALA
SEQRES 17 B 525 PHE GLY PRO PHE CYS ASP ALA LEU LYS GLU THR CYS ILE
SEQRES 18 B 525 PHE ASN PRO ILE ARG VAL GLY MET SER MET ASN GLU ASP
SEQRES 19 B 525 GLY PRO PHE ILE PHE ALA ARG HIS ALA ASN PHE ARG TYR
SEQRES 20 B 525 HIS MET ASP ALA ASP TYR THR ARG TRP ASP SER THR GLN
SEQRES 21 B 525 GLN ARG ALA ILE LEU LYS ARG ALA GLY ASP ILE MET VAL
SEQRES 22 B 525 ARG LEU SER PRO GLU PRO ASP LEU ALA ARG VAL VAL MET
SEQRES 23 B 525 ASP ASP LEU LEU ALA PRO SER LEU LEU ASP VAL GLY ASP
SEQRES 24 B 525 TYR LYS ILE VAL VAL GLU GLU GLY LEU PRO SER GLY CYS
SEQRES 25 B 525 PRO CYS THR THR GLN LEU ASN SER LEU ALA HIS TRP ILE
SEQRES 26 B 525 LEU THR LEU CYS ALA MET VAL GLU VAL THR ARG VAL ASP
SEQRES 27 B 525 PRO ASP ILE VAL MET GLN GLU SER GLU PHE SER PHE TYR
SEQRES 28 B 525 GLY ASP ASP GLU VAL VAL SER THR ASN LEU GLU LEU ASP
SEQRES 29 B 525 MET VAL LYS TYR THR MET ALA LEU ARG ARG TYR GLY LEU
SEQRES 30 B 525 LEU PRO THR ARG ALA ASP LYS GLU GLU GLY PRO LEU GLU
SEQRES 31 B 525 ARG ARG GLN THR LEU GLN GLY ILE SER PHE LEU ARG ARG
SEQRES 32 B 525 ALA ILE VAL GLY ASP GLN PHE GLY TRP TYR GLY ARG LEU
SEQRES 33 B 525 ASP ARG ALA SER ILE ASP ARG GLN LEU LEU TRP THR LYS
SEQRES 34 B 525 GLY PRO ASN HIS GLN ASN PRO PHE GLU THR LEU PRO GLY
SEQRES 35 B 525 HIS ALA GLN ARG PRO SER GLN LEU MET ALA LEU LEU GLY
SEQRES 36 B 525 GLU ALA ALA MET HIS GLY GLU LYS TYR TYR ARG THR VAL
SEQRES 37 B 525 ALA SER ARG VAL SER LYS GLU ALA ALA GLN SER GLY ILE
SEQRES 38 B 525 GLU MET VAL VAL PRO ARG HIS ARG SER VAL LEU ARG TRP
SEQRES 39 B 525 VAL ARG PHE GLY THR MET ASP ALA GLU THR PRO GLN GLU
SEQRES 40 B 525 ARG SER ALA VAL PHE VAL ASN GLU ASP GLU LEU GLU HIS
SEQRES 41 B 525 HIS HIS HIS HIS HIS
SEQRES 1 C 525 MET LYS ALA LEU GLU PHE GLN GLY PRO PRO MET LEU PRO
SEQRES 2 C 525 ARG PRO SER GLY THR TYR ALA GLY LEU PRO ILE ALA ASP
SEQRES 3 C 525 TYR GLY ASP ALA PRO PRO LEU SER THR LYS THR MET PHE
SEQRES 4 C 525 TRP ARG THR SER PRO GLU LYS LEU PRO PRO GLY ALA TRP
SEQRES 5 C 525 GLU PRO ALA TYR LEU GLY SER LYS ASP GLU ARG VAL ASP
SEQRES 6 C 525 GLY PRO SER LEU GLN GLN VAL MET ARG ASP GLN LEU LYS
SEQRES 7 C 525 PRO TYR SER GLU PRO ARG GLY LEU LEU PRO PRO GLN GLU
SEQRES 8 C 525 ILE LEU ASP ALA VAL CYS ASP ALA ILE GLU ASN ARG LEU
SEQRES 9 C 525 GLU ASN THR LEU GLU PRO GLN LYS PRO TRP THR PHE LYS
SEQRES 10 C 525 LYS ALA CYS GLU SER LEU ASP LYS ASN THR SER SER GLY
SEQRES 11 C 525 TYR PRO TYR HIS LYS GLN LYS SER LYS ASP TRP THR GLY
SEQRES 12 C 525 SER ALA PHE ILE GLY ASP LEU GLY ASP GLN ALA THR HIS
SEQRES 13 C 525 ALA ASN ASN MET TYR GLU MET GLY LYS SER MET ARG PRO
SEQRES 14 C 525 ILE TYR THR ALA ALA LEU LYS ASP GLU LEU VAL LYS PRO
SEQRES 15 C 525 ASP LYS ILE TYR GLY LYS ILE LYS LYS ARG LEU LEU TRP
SEQRES 16 C 525 GLY SER ASP LEU GLY THR MET ILE ARG ALA ALA ARG ALA
SEQRES 17 C 525 PHE GLY PRO PHE CYS ASP ALA LEU LYS GLU THR CYS ILE
SEQRES 18 C 525 PHE ASN PRO ILE ARG VAL GLY MET SER MET ASN GLU ASP
SEQRES 19 C 525 GLY PRO PHE ILE PHE ALA ARG HIS ALA ASN PHE ARG TYR
SEQRES 20 C 525 HIS MET ASP ALA ASP TYR THR ARG TRP ASP SER THR GLN
SEQRES 21 C 525 GLN ARG ALA ILE LEU LYS ARG ALA GLY ASP ILE MET VAL
SEQRES 22 C 525 ARG LEU SER PRO GLU PRO ASP LEU ALA ARG VAL VAL MET
SEQRES 23 C 525 ASP ASP LEU LEU ALA PRO SER LEU LEU ASP VAL GLY ASP
SEQRES 24 C 525 TYR LYS ILE VAL VAL GLU GLU GLY LEU PRO SER GLY CYS
SEQRES 25 C 525 PRO CYS THR THR GLN LEU ASN SER LEU ALA HIS TRP ILE
SEQRES 26 C 525 LEU THR LEU CYS ALA MET VAL GLU VAL THR ARG VAL ASP
SEQRES 27 C 525 PRO ASP ILE VAL MET GLN GLU SER GLU PHE SER PHE TYR
SEQRES 28 C 525 GLY ASP ASP GLU VAL VAL SER THR ASN LEU GLU LEU ASP
SEQRES 29 C 525 MET VAL LYS TYR THR MET ALA LEU ARG ARG TYR GLY LEU
SEQRES 30 C 525 LEU PRO THR ARG ALA ASP LYS GLU GLU GLY PRO LEU GLU
SEQRES 31 C 525 ARG ARG GLN THR LEU GLN GLY ILE SER PHE LEU ARG ARG
SEQRES 32 C 525 ALA ILE VAL GLY ASP GLN PHE GLY TRP TYR GLY ARG LEU
SEQRES 33 C 525 ASP ARG ALA SER ILE ASP ARG GLN LEU LEU TRP THR LYS
SEQRES 34 C 525 GLY PRO ASN HIS GLN ASN PRO PHE GLU THR LEU PRO GLY
SEQRES 35 C 525 HIS ALA GLN ARG PRO SER GLN LEU MET ALA LEU LEU GLY
SEQRES 36 C 525 GLU ALA ALA MET HIS GLY GLU LYS TYR TYR ARG THR VAL
SEQRES 37 C 525 ALA SER ARG VAL SER LYS GLU ALA ALA GLN SER GLY ILE
SEQRES 38 C 525 GLU MET VAL VAL PRO ARG HIS ARG SER VAL LEU ARG TRP
SEQRES 39 C 525 VAL ARG PHE GLY THR MET ASP ALA GLU THR PRO GLN GLU
SEQRES 40 C 525 ARG SER ALA VAL PHE VAL ASN GLU ASP GLU LEU GLU HIS
SEQRES 41 C 525 HIS HIS HIS HIS HIS
HET 0BU A 600 66
HET SO4 A 516 5
HET 0BU B 600 66
HET SO4 B 516 5
HET SO4 B 517 5
HET 0BU C 600 66
HET SO4 C 516 5
HET SO4 C 517 5
HET SO4 C 518 5
HET SO4 C 519 5
HETNAM 0BU 8-({3-[({3-[(4,6,8-TRISULFONAPHTHALEN-1-YL)
HETNAM 2 0BU CARBAMOYL]PHENYL}CARBAMOYL)AMINO]BENZOYL}AMINO)
HETNAM 3 0BU NAPHTHALENE-1,3,5-TRISULFONIC ACID
HETNAM SO4 SULFATE ION
HETSYN 0BU NF023
FORMUL 4 0BU 3(C35 H26 N4 O21 S6)
FORMUL 5 SO4 7(O4 S 2-)
FORMUL 14 HOH *625(H2 O)
HELIX 1 1 SER A 58 LYS A 68 1 11
HELIX 2 2 PRO A 69 SER A 71 5 3
HELIX 3 3 PRO A 79 LEU A 98 1 20
HELIX 4 4 THR A 105 LEU A 113 1 9
HELIX 5 5 GLN A 126 TRP A 131 5 6
HELIX 6 6 ILE A 137 MET A 153 1 17
HELIX 7 7 LYS A 171 ILE A 175 5 5
HELIX 8 8 ASP A 188 THR A 209 1 22
HELIX 9 9 ASP A 224 ALA A 233 1 10
HELIX 10 10 GLN A 251 LEU A 265 1 15
HELIX 11 11 GLU A 268 ALA A 281 1 14
HELIX 12 12 CYS A 304 ARG A 326 1 23
HELIX 13 13 ASP A 328 GLU A 335 1 8
HELIX 14 14 ASP A 354 TYR A 365 1 12
HELIX 15 15 ASP A 407 LEU A 416 1 10
HELIX 16 16 LEU A 440 MET A 449 1 10
HELIX 17 17 GLY A 451 LYS A 464 1 14
HELIX 18 18 ARG A 477 GLY A 488 1 12
HELIX 19 19 SER B 58 LYS B 68 1 11
HELIX 20 20 PRO B 69 SER B 71 5 3
HELIX 21 21 PRO B 79 LEU B 98 1 20
HELIX 22 22 THR B 105 LEU B 113 1 9
HELIX 23 23 GLN B 126 TRP B 131 5 6
HELIX 24 24 ILE B 137 MET B 153 1 17
HELIX 25 25 PRO B 172 GLY B 177 1 6
HELIX 26 26 ASP B 188 THR B 209 1 22
HELIX 27 27 SER B 220 ALA B 233 1 14
HELIX 28 28 ARG B 245 GLN B 250 1 6
HELIX 29 29 GLN B 251 LEU B 265 1 15
HELIX 30 30 GLU B 268 ALA B 281 1 14
HELIX 31 31 THR B 305 ARG B 326 1 22
HELIX 32 32 ASP B 328 GLU B 335 1 8
HELIX 33 33 ASP B 354 TYR B 365 1 12
HELIX 34 34 ASP B 407 LEU B 416 1 10
HELIX 35 35 ARG B 436 MET B 449 1 14
HELIX 36 36 GLY B 451 ALA B 467 1 17
HELIX 37 37 ARG B 477 PHE B 487 1 11
HELIX 38 38 SER C 58 LYS C 68 1 11
HELIX 39 39 PRO C 69 GLU C 72 5 4
HELIX 40 40 PRO C 79 ASN C 96 1 18
HELIX 41 41 THR C 105 LEU C 113 1 9
HELIX 42 42 GLN C 126 TRP C 131 5 6
HELIX 43 43 ILE C 137 MET C 153 1 17
HELIX 44 44 PRO C 172 GLY C 177 1 6
HELIX 45 45 ASP C 188 GLU C 208 1 21
HELIX 46 46 SER C 220 ALA C 233 1 14
HELIX 47 47 TRP C 246 GLN C 250 5 5
HELIX 48 48 GLN C 251 LEU C 265 1 15
HELIX 49 49 GLU C 268 ALA C 281 1 14
HELIX 50 50 THR C 306 ARG C 326 1 21
HELIX 51 51 ASP C 328 GLU C 335 1 8
HELIX 52 52 ASP C 354 TYR C 365 1 12
HELIX 53 53 ASP C 407 LEU C 416 1 10
HELIX 54 54 ARG C 436 MET C 449 1 14
HELIX 55 55 GLY C 451 GLU C 465 1 15
HELIX 56 56 ARG C 477 PHE C 487 1 11
SHEET 1 A 6 THR A 8 TYR A 9 0
SHEET 2 A 6 LEU A 12 TYR A 17 -1 O LEU A 12 N TYR A 9
SHEET 3 A 6 TYR A 290 VAL A 294 -1 O LYS A 291 N ASP A 16
SHEET 4 A 6 SER A 283 ASP A 286 -1 N SER A 283 O VAL A 294
SHEET 5 A 6 ILE A 160 LEU A 165 1 N TYR A 161 O ASP A 286
SHEET 6 A 6 LEU A 183 GLY A 186 -1 O LEU A 184 N ALA A 164
SHEET 1 B 2 THR A 27 ARG A 31 0
SHEET 2 B 2 TRP A 417 HIS A 423 -1 O HIS A 423 N THR A 27
SHEET 1 C 2 GLU A 43 PRO A 44 0
SHEET 2 C 2 LEU A 169 VAL A 170 -1 O VAL A 170 N GLU A 43
SHEET 1 D 3 TYR A 237 MET A 239 0
SHEET 2 D 3 ASP A 344 THR A 349 -1 O THR A 349 N TYR A 237
SHEET 3 D 3 SER A 336 TYR A 341 -1 N GLU A 337 O SER A 348
SHEET 1 E 3 SER A 389 PHE A 390 0
SHEET 2 E 3 ARG A 393 ASP A 398 -1 O ARG A 393 N PHE A 390
SHEET 3 E 3 GLY A 401 ARG A 405 -1 O ARG A 405 N ALA A 394
SHEET 1 F 6 THR B 8 TYR B 9 0
SHEET 2 F 6 LEU B 12 TYR B 17 -1 O LEU B 12 N TYR B 9
SHEET 3 F 6 TYR B 290 VAL B 294 -1 O LYS B 291 N ASP B 16
SHEET 4 F 6 SER B 283 ASP B 286 -1 N LEU B 285 O ILE B 292
SHEET 5 F 6 ILE B 160 LEU B 165 1 N TYR B 161 O ASP B 286
SHEET 6 F 6 LEU B 183 GLY B 186 -1 O GLY B 186 N THR B 162
SHEET 1 G 2 THR B 27 ARG B 31 0
SHEET 2 G 2 TRP B 417 HIS B 423 -1 O THR B 418 N TRP B 30
SHEET 1 H 2 GLU B 43 PRO B 44 0
SHEET 2 H 2 LEU B 169 VAL B 170 -1 O VAL B 170 N GLU B 43
SHEET 1 I 3 TYR B 237 MET B 239 0
SHEET 2 I 3 ASP B 344 THR B 349 -1 O THR B 349 N TYR B 237
SHEET 3 I 3 SER B 336 TYR B 341 -1 N GLU B 337 O SER B 348
SHEET 1 J 3 SER B 389 PHE B 390 0
SHEET 2 J 3 ARG B 393 ASP B 398 -1 O ARG B 393 N PHE B 390
SHEET 3 J 3 GLY B 401 ARG B 405 -1 O ARG B 405 N ALA B 394
SHEET 1 K 6 THR C 8 TYR C 9 0
SHEET 2 K 6 LEU C 12 TYR C 17 -1 O LEU C 12 N TYR C 9
SHEET 3 K 6 TYR C 290 VAL C 294 -1 O LYS C 291 N ALA C 15
SHEET 4 K 6 SER C 283 ASP C 286 -1 N SER C 283 O VAL C 294
SHEET 5 K 6 TYR C 161 LEU C 165 1 N TYR C 161 O ASP C 286
SHEET 6 K 6 LEU C 183 GLY C 186 -1 O LEU C 184 N ALA C 164
SHEET 1 L 2 THR C 27 ARG C 31 0
SHEET 2 L 2 TRP C 417 HIS C 423 -1 O HIS C 423 N THR C 27
SHEET 1 M 2 GLU C 43 PRO C 44 0
SHEET 2 M 2 LEU C 169 VAL C 170 -1 O VAL C 170 N GLU C 43
SHEET 1 N 3 TYR C 237 MET C 239 0
SHEET 2 N 3 ASP C 344 THR C 349 -1 O THR C 349 N TYR C 237
SHEET 3 N 3 SER C 336 TYR C 341 -1 N GLU C 337 O SER C 348
SHEET 1 O 3 SER C 389 PHE C 390 0
SHEET 2 O 3 ARG C 393 ASP C 398 -1 O ARG C 393 N PHE C 390
SHEET 3 O 3 GLY C 401 ARG C 405 -1 O ARG C 405 N ALA C 394
CISPEP 1 TYR A 121 PRO A 122 0 0.01
CISPEP 2 TYR B 121 PRO B 122 0 2.64
CISPEP 3 TYR C 121 PRO C 122 0 -3.04
SITE 1 AC1 15 TRP A 42 ASP A 65 GLN A 66 PRO A 69
SITE 2 AC1 15 GLU A 168 VAL A 170 LYS A 171 LYS A 174
SITE 3 AC1 15 LYS A 180 ARG A 182 ARG A 245 ARG A 392
SITE 4 AC1 15 ARG A 413 SO4 A 516 HOH A 687
SITE 1 AC2 4 THR A 244 ARG A 245 HOH A 560 0BU A 600
SITE 1 AC3 17 TRP B 42 ASP B 65 GLN B 66 LYS B 68
SITE 2 AC3 17 PRO B 69 GLU B 168 VAL B 170 LYS B 171
SITE 3 AC3 17 LYS B 174 LYS B 178 LYS B 180 ARG B 182
SITE 4 AC3 17 ARG B 245 ARG B 392 ARG B 413 SO4 B 517
SITE 5 AC3 17 HOH B 608
SITE 1 AC4 3 VAL B 322 ARG B 326 ASP B 328
SITE 1 AC5 5 TYR B 243 THR B 244 ARG B 245 0BU B 600
SITE 2 AC5 5 HOH B 608
SITE 1 AC6 16 TRP C 42 ASP C 65 GLN C 66 LYS C 68
SITE 2 AC6 16 PRO C 69 GLU C 168 VAL C 170 LYS C 171
SITE 3 AC6 16 LYS C 174 LYS C 178 LYS C 180 ARG C 182
SITE 4 AC6 16 ARG C 245 ARG C 392 SO4 C 516 HOH C 743
SITE 1 AC7 5 TYR C 243 THR C 244 ARG C 245 HOH C 520
SITE 2 AC7 5 0BU C 600
SITE 1 AC8 4 GLY C 7 ALA C 10 ARG C 64 HOH C 633
SITE 1 AC9 2 VAL C 322 ARG C 326
SITE 1 BC1 7 THR C 25 GLY C 48 SER C 49 SER C 58
SITE 2 BC1 7 LEU C 59 HOH C 610 HOH C 695
CRYST1 120.860 195.950 109.240 90.00 114.38 90.00 C 1 2 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008274 0.000000 0.003750 0.00000
SCALE2 0.000000 0.005103 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010050 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
