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HEADER HYDROLASE 10-FEB-17 5N4E
TITLE PROLYL OLIGOPEPTIDASE B FROM GALERINA MARGINATA BOUND TO 35MER
TITLE 2 HYDROLYSIS AND MACROCYCLIZATION SUBSTRATE - H698A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLYL OLIGOPEPTIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ALPHA-AMANITIN PROPROTEIN;
COMPND 8 CHAIN: C, D;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;
SOURCE 3 ORGANISM_TAXID: 109633;
SOURCE 4 GENE: POPB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PJ411;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;
SOURCE 12 ORGANISM_TAXID: 109633
KEYWDS AMANITIN BIOSYNTHESIS, PROLYL OLIGOPEPTIDASE, HYDROLASE,
KEYWDS 2 MACROCYCLASE, PEPTIDASE, BETA-PROPELLER, CLOSED FORM
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.CZEKSTER,S.A.MCMAHON,H.LUDEWIG,J.H.NAISMITH
REVDAT 1 01-NOV-17 5N4E 0
JRNL AUTH C.M.CZEKSTER,H.LUDEWIG,S.A.MCMAHON,J.H.NAISMITH
JRNL TITL CHARACTERIZATION OF A DUAL FUNCTION MACROCYCLASE ENABLES
JRNL TITL 2 DESIGN AND USE OF EFFICIENT MACROCYCLIZATION SUBSTRATES
JRNL REF NAT COMMUN 2017
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-017-00862-4
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 89.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 32664
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) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1690
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2247
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.3560
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.4830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11750
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 939
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.18000
REMARK 3 B22 (A**2) : -2.87000
REMARK 3 B33 (A**2) : 5.05000
REMARK 3 B12 (A**2) : 0.00000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.555
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.380
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.150
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.867
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12085 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10806 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16418 ; 1.101 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25114 ; 0.865 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1474 ; 5.890 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 581 ;34.109 ;24.337
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1916 ;12.341 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;12.376 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1739 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13582 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2581 ; 0.001 ; 0.020
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): 5923 ; 1.541 ; 3.248
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5922 ; 1.534 ; 3.248
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7388 ; 2.639 ; 4.864
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7389 ; 2.640 ; 4.864
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6162 ; 1.349 ; 3.344
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6162 ; 1.348 ; 3.344
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 9031 ; 2.313 ; 4.973
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 13745 ; 5.235 ;37.367
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 13745 ; 5.234 ;37.366
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 6 727 B 6 727 45368 0.09 0.05
REMARK 3 2 C 2 35 D 2 35 1462 0.11 0.05
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 : 1.00
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 5N4E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003502.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91770
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 31.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 2.8100
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 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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEGMME2000, 90 MM BICINE PH 8.7,
REMARK 280 100 MM POTASSIUM THIOCYANATE, AND 12.5MM HEXAMMINE COBALT
REMARK 280 CHLORIDE. CRYSTALS WERE CRYOPROTECTED WITH 13% GLYCEROL., VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 49.59000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.72500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.72500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.59000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.50000
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
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 THR A 5
REMARK 465 ARG A 222
REMARK 465 GLU A 223
REMARK 465 ARG A 224
REMARK 465 HIS A 225
REMARK 465 GLU A 226
REMARK 465 GLY A 227
REMARK 465 THR A 228
REMARK 465 ARG A 229
REMARK 465 THR A 728
REMARK 465 VAL A 729
REMARK 465 GLU A 730
REMARK 465 MET A 731
REMARK 465 PHE A 732
REMARK 465 ASP A 733
REMARK 465 THR A 734
REMARK 465 ASN A 735
REMARK 465 ALA A 736
REMARK 465 THR A 737
REMARK 465 ARG A 738
REMARK 465 LEU A 739
REMARK 465 PRO A 740
REMARK 465 ILE A 741
REMARK 465 TRP A 742
REMARK 465 GLY A 743
REMARK 465 ILE A 744
REMARK 465 GLY A 745
REMARK 465 CYS A 746
REMARK 465 ASN A 747
REMARK 465 PRO A 748
REMARK 465 TRP A 749
REMARK 465 THR A 750
REMARK 465 ALA A 751
REMARK 465 GLU A 752
REMARK 465 HIS A 753
REMARK 465 VAL A 754
REMARK 465 ASP A 755
REMARK 465 GLN A 756
REMARK 465 THR A 757
REMARK 465 LEU A 758
REMARK 465 ALA A 759
REMARK 465 SER A 760
REMARK 465 GLY A 761
REMARK 465 ASN A 762
REMARK 465 ASP A 763
REMARK 465 ILE A 764
REMARK 465 CYS A 765
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 SER B 3
REMARK 465 VAL B 4
REMARK 465 THR B 5
REMARK 465 HIS B 163
REMARK 465 LEU B 164
REMARK 465 GLY B 165
REMARK 465 GLY B 166
REMARK 465 ASP B 167
REMARK 465 GLU B 223
REMARK 465 ARG B 224
REMARK 465 HIS B 225
REMARK 465 GLU B 226
REMARK 465 GLY B 227
REMARK 465 THR B 228
REMARK 465 ARG B 229
REMARK 465 SER B 230
REMARK 465 GLY B 699
REMARK 465 MET B 700
REMARK 465 THR B 728
REMARK 465 VAL B 729
REMARK 465 GLU B 730
REMARK 465 MET B 731
REMARK 465 PHE B 732
REMARK 465 ASP B 733
REMARK 465 THR B 734
REMARK 465 ASN B 735
REMARK 465 ALA B 736
REMARK 465 THR B 737
REMARK 465 ARG B 738
REMARK 465 LEU B 739
REMARK 465 PRO B 740
REMARK 465 ILE B 741
REMARK 465 TRP B 742
REMARK 465 GLY B 743
REMARK 465 ILE B 744
REMARK 465 GLY B 745
REMARK 465 CYS B 746
REMARK 465 ASN B 747
REMARK 465 PRO B 748
REMARK 465 TRP B 749
REMARK 465 THR B 750
REMARK 465 ALA B 751
REMARK 465 GLU B 752
REMARK 465 HIS B 753
REMARK 465 VAL B 754
REMARK 465 ASP B 755
REMARK 465 GLN B 756
REMARK 465 THR B 757
REMARK 465 LEU B 758
REMARK 465 ALA B 759
REMARK 465 SER B 760
REMARK 465 GLY B 761
REMARK 465 ASN B 762
REMARK 465 ASP B 763
REMARK 465 ILE B 764
REMARK 465 CYS B 765
REMARK 465 MET C 1
REMARK 465 GLY C 15
REMARK 465 CYS C 16
REMARK 465 ASN C 17
REMARK 465 PRO C 18
REMARK 465 MET D 1
REMARK 465 ILE D 14
REMARK 465 GLY D 15
REMARK 465 CYS D 16
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 190 -45.50 -27.89
REMARK 500 ALA A 311 -48.81 -145.29
REMARK 500 ALA A 332 75.21 -159.58
REMARK 500 TYR A 335 160.76 68.01
REMARK 500 GLU A 369 -50.31 67.21
REMARK 500 GLU A 452 -57.56 69.43
REMARK 500 TYR A 496 -63.52 -121.65
REMARK 500 ARG A 543 -113.28 56.90
REMARK 500 SER A 577 -96.44 67.92
REMARK 500 ALA A 605 -43.52 -158.30
REMARK 500 THR A 614 -121.75 36.82
REMARK 500 MET A 667 -53.12 -26.96
REMARK 500 TRP A 695 87.22 -67.67
REMARK 500 ALA A 698 99.49 -69.54
REMARK 500 ALA B 311 -48.82 -144.95
REMARK 500 ALA B 332 75.22 -159.61
REMARK 500 TYR B 335 160.46 68.33
REMARK 500 GLU B 369 -50.10 66.82
REMARK 500 GLU B 452 -57.23 69.28
REMARK 500 TYR B 496 -63.62 -121.93
REMARK 500 ARG B 543 -112.78 57.08
REMARK 500 SER B 577 -96.60 68.04
REMARK 500 ALA B 605 -43.08 -158.18
REMARK 500 THR B 614 -123.40 38.86
REMARK 500 MET B 667 -53.19 -26.99
REMARK 500 TRP B 695 90.78 -65.81
REMARK 500 VAL C 24 -48.65 -25.25
REMARK 500 VAL D 24 -49.01 -26.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1257 DISTANCE = 5.99 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 801
DBREF 5N4E A 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
DBREF 5N4E B 1 730 UNP H2E7Q8 H2E7Q8_9AGAR 1 730
DBREF 5N4E C 1 35 UNP H2E7Q5 H2E7Q5_9AGAR 1 35
DBREF 5N4E D 1 35 UNP H2E7Q5 H2E7Q5_9AGAR 1 35
SEQADV 5N4E ALA A 698 UNP H2E7Q8 HIS 698 ENGINEERED MUTATION
SEQADV 5N4E MET A 731 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E PHE A 732 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASP A 733 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E THR A 734 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASN A 735 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ALA A 736 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E THR A 737 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ARG A 738 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E LEU A 739 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E PRO A 740 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ILE A 741 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E TRP A 742 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E GLY A 743 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ILE A 744 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E GLY A 745 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E CYS A 746 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASN A 747 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E PRO A 748 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E TRP A 749 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E THR A 750 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ALA A 751 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E GLU A 752 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E HIS A 753 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E VAL A 754 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASP A 755 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E GLN A 756 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E THR A 757 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E LEU A 758 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ALA A 759 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E SER A 760 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E GLY A 761 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASN A 762 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASP A 763 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ILE A 764 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E CYS A 765 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ALA B 698 UNP H2E7Q8 HIS 698 ENGINEERED MUTATION
SEQADV 5N4E MET B 731 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E PHE B 732 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASP B 733 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E THR B 734 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASN B 735 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ALA B 736 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E THR B 737 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ARG B 738 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E LEU B 739 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E PRO B 740 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ILE B 741 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E TRP B 742 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E GLY B 743 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ILE B 744 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E GLY B 745 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E CYS B 746 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASN B 747 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E PRO B 748 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E TRP B 749 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E THR B 750 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ALA B 751 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E GLU B 752 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E HIS B 753 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E VAL B 754 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASP B 755 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E GLN B 756 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E THR B 757 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E LEU B 758 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ALA B 759 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E SER B 760 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E GLY B 761 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASN B 762 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ASP B 763 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E ILE B 764 UNP H2E7Q8 EXPRESSION TAG
SEQADV 5N4E CYS B 765 UNP H2E7Q8 EXPRESSION TAG
SEQRES 1 A 765 MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER
SEQRES 2 A 765 THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA
SEQRES 3 A 765 SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP
SEQRES 4 A 765 LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR
SEQRES 5 A 765 ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN
SEQRES 6 A 765 ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER
SEQRES 7 A 765 ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP
SEQRES 8 A 765 ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN
SEQRES 9 A 765 SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU
SEQRES 10 A 765 PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL
SEQRES 11 A 765 PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA
SEQRES 12 A 765 GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE
SEQRES 13 A 765 PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER
SEQRES 14 A 765 THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN
SEQRES 15 A 765 ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP
SEQRES 16 A 765 GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR
SEQRES 17 A 765 LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA
SEQRES 18 A 765 ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA
SEQRES 19 A 765 MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU
SEQRES 20 A 765 ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP
SEQRES 21 A 765 ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU
SEQRES 22 A 765 TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU
SEQRES 23 A 765 LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER
SEQRES 24 A 765 GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA
SEQRES 25 A 765 ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR
SEQRES 26 A 765 ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE
SEQRES 27 A 765 THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP
SEQRES 28 A 765 PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL
SEQRES 29 A 765 ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS
SEQRES 30 A 765 ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA
SEQRES 31 A 765 GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY
SEQRES 32 A 765 ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE
SEQRES 33 A 765 PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE
SEQRES 34 A 765 ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE
SEQRES 35 A 765 SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO
SEQRES 36 A 765 ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS
SEQRES 37 A 765 ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS
SEQRES 38 A 765 SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR
SEQRES 39 A 765 GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE
SEQRES 40 A 765 SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA
SEQRES 41 A 765 ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE
SEQRES 42 A 765 GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS
SEQRES 43 A 765 VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE
SEQRES 44 A 765 LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA
SEQRES 45 A 765 ILE ASN GLY ALA SER ASN GLY GLY LEU LEU VAL MET GLY
SEQRES 46 A 765 SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA
SEQRES 47 A 765 VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS
SEQRES 48 A 765 LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY
SEQRES 49 A 765 ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO
SEQRES 50 A 765 LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET
SEQRES 51 A 765 PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY ARG
SEQRES 52 A 765 VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU
SEQRES 53 A 765 GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE
SEQRES 54 A 765 LYS ILE ASP LYS SER TRP LEU GLY ALA GLY MET GLY LYS
SEQRES 55 A 765 PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP
SEQRES 56 A 765 GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR
SEQRES 57 A 765 VAL GLU MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE
SEQRES 58 A 765 TRP GLY ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL
SEQRES 59 A 765 ASP GLN THR LEU ALA SER GLY ASN ASP ILE CYS
SEQRES 1 B 765 MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO SER
SEQRES 2 B 765 THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER ALA
SEQRES 3 B 765 SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN TRP
SEQRES 4 B 765 LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR THR
SEQRES 5 B 765 ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN ASN
SEQRES 6 B 765 ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA SER
SEQRES 7 B 765 ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU ASP
SEQRES 8 B 765 ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU GLN
SEQRES 9 B 765 SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA LEU
SEQRES 10 B 765 PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP VAL
SEQRES 11 B 765 PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER ALA
SEQRES 12 B 765 GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS PHE
SEQRES 13 B 765 PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR SER
SEQRES 14 B 765 THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER GLN
SEQRES 15 B 765 ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER ASP
SEQRES 16 B 765 GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP THR
SEQRES 17 B 765 LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO ALA
SEQRES 18 B 765 ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN ALA
SEQRES 19 B 765 MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU GLU
SEQRES 20 B 765 ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU TRP
SEQRES 21 B 765 ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR LEU
SEQRES 22 B 765 TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN LEU
SEQRES 23 B 765 LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS SER
SEQRES 24 B 765 GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA ALA
SEQRES 25 B 765 ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL TYR
SEQRES 26 B 765 ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL ILE
SEQRES 27 B 765 THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG ASP
SEQRES 28 B 765 PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN VAL
SEQRES 29 B 765 ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR LYS
SEQRES 30 B 765 ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS ALA
SEQRES 31 B 765 GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL GLY
SEQRES 32 B 765 ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS PHE
SEQRES 33 B 765 PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR ILE
SEQRES 34 B 765 ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG PHE
SEQRES 35 B 765 SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP PRO
SEQRES 36 B 765 ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER LYS
SEQRES 37 B 765 ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS LYS
SEQRES 38 B 765 SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN TYR
SEQRES 39 B 765 GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE PHE
SEQRES 40 B 765 SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY ALA
SEQRES 41 B 765 ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU PHE
SEQRES 42 B 765 GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR LYS
SEQRES 43 B 765 VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN PHE
SEQRES 44 B 765 LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL ALA
SEQRES 45 B 765 ILE ASN GLY ALA SER ASN GLY GLY LEU LEU VAL MET GLY
SEQRES 46 B 765 SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA ALA
SEQRES 47 B 765 VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE HIS
SEQRES 48 B 765 LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR GLY
SEQRES 49 B 765 ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR PRO
SEQRES 50 B 765 LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL MET
SEQRES 51 B 765 PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY ARG
SEQRES 52 B 765 VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR LEU
SEQRES 53 B 765 GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU ILE
SEQRES 54 B 765 LYS ILE ASP LYS SER TRP LEU GLY ALA GLY MET GLY LYS
SEQRES 55 B 765 PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS TRP
SEQRES 56 B 765 GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS THR
SEQRES 57 B 765 VAL GLU MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE
SEQRES 58 B 765 TRP GLY ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL
SEQRES 59 B 765 ASP GLN THR LEU ALA SER GLY ASN ASP ILE CYS
SEQRES 1 C 35 MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE TRP GLY
SEQRES 2 C 35 ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL ASP GLN
SEQRES 3 C 35 THR LEU ALA SER GLY ASN ASP ILE CYS
SEQRES 1 D 35 MET PHE ASP THR ASN ALA THR ARG LEU PRO ILE TRP GLY
SEQRES 2 D 35 ILE GLY CYS ASN PRO TRP THR ALA GLU HIS VAL ASP GLN
SEQRES 3 D 35 THR LEU ALA SER GLY ASN ASP ILE CYS
HET GOL B 801 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *939(H2 O)
HELIX 1 AA1 TYR A 37 GLU A 42 5 6
HELIX 2 AA2 THR A 44 GLN A 64 1 21
HELIX 3 AA3 ALA A 66 ASN A 80 1 15
HELIX 4 AA4 ASP A 119 LYS A 122 5 4
HELIX 5 AA5 GLY A 123 VAL A 127 1 5
HELIX 6 AA6 ASP A 133 LEU A 137 5 5
HELIX 7 AA7 SER A 181 GLY A 188 1 8
HELIX 8 AA8 THR A 244 ASP A 248 5 5
HELIX 9 AA9 PRO A 437 GLN A 440 5 4
HELIX 10 AB1 ASP A 454 ASP A 456 5 3
HELIX 11 AB2 SER A 508 GLY A 519 1 12
HELIX 12 AB3 GLY A 534 GLY A 540 1 7
HELIX 13 AB4 GLY A 541 THR A 545 5 5
HELIX 14 AB5 LYS A 546 ASN A 563 1 18
HELIX 15 AB6 SER A 577 ALA A 590 1 14
HELIX 16 AB7 LYS A 609 PHE A 613 5 5
HELIX 17 AB8 GLY A 615 ALA A 618 5 4
HELIX 18 AB9 TRP A 619 GLY A 624 1 6
HELIX 19 AC1 ILE A 628 TYR A 636 1 9
HELIX 20 AC2 SER A 639 ASN A 643 5 5
HELIX 21 AC3 PRO A 666 VAL A 680 1 15
HELIX 22 AC4 PRO A 703 LEU A 722 1 20
HELIX 23 AC5 TYR B 37 GLU B 42 5 6
HELIX 24 AC6 THR B 44 GLN B 64 1 21
HELIX 25 AC7 ALA B 66 ASN B 80 1 15
HELIX 26 AC8 ASP B 119 LYS B 122 5 4
HELIX 27 AC9 GLY B 123 VAL B 127 1 5
HELIX 28 AD1 ASP B 133 LEU B 137 5 5
HELIX 29 AD2 SER B 181 GLY B 188 1 8
HELIX 30 AD3 THR B 244 ASP B 248 5 5
HELIX 31 AD4 PRO B 437 GLN B 440 5 4
HELIX 32 AD5 ASP B 454 ASP B 456 5 3
HELIX 33 AD6 SER B 508 GLY B 519 1 12
HELIX 34 AD7 GLY B 534 GLY B 540 1 7
HELIX 35 AD8 GLY B 541 THR B 545 5 5
HELIX 36 AD9 LYS B 546 ASN B 563 1 18
HELIX 37 AE1 SER B 577 ALA B 590 1 14
HELIX 38 AE2 LYS B 609 PHE B 613 5 5
HELIX 39 AE3 GLY B 615 ALA B 618 5 4
HELIX 40 AE4 TRP B 619 GLY B 624 1 6
HELIX 41 AE5 ILE B 628 TYR B 636 1 9
HELIX 42 AE6 SER B 639 ASN B 643 5 5
HELIX 43 AE7 PRO B 666 VAL B 680 1 15
HELIX 44 AE8 PRO B 703 LEU B 722 1 20
HELIX 45 AE9 THR C 4 LEU C 9 5 6
HELIX 46 AF1 THR C 20 VAL C 24 5 5
HELIX 47 AF2 THR D 4 LEU D 9 5 6
HELIX 48 AF3 THR D 20 VAL D 24 5 5
SHEET 1 AA1 2 VAL A 20 SER A 25 0
SHEET 2 AA1 2 GLY A 29 PRO A 34 -1 O GLY A 29 N SER A 25
SHEET 1 AA2 3 LYS A 83 PHE A 84 0
SHEET 2 AA2 3 TRP A 95 ASN A 100 -1 O ASN A 100 N LYS A 83
SHEET 3 AA2 3 THR A 88 LEU A 89 -1 N THR A 88 O TYR A 96
SHEET 1 AA3 4 LYS A 83 PHE A 84 0
SHEET 2 AA3 4 TRP A 95 ASN A 100 -1 O ASN A 100 N LYS A 83
SHEET 3 AA3 4 VAL A 108 SER A 112 -1 O TYR A 110 N TRP A 97
SHEET 4 AA3 4 GLY A 128 PHE A 132 -1 O PHE A 132 N LEU A 109
SHEET 1 AA4 4 GLY A 144 PHE A 150 0
SHEET 2 AA4 4 PHE A 156 SER A 162 -1 O SER A 162 N GLY A 144
SHEET 3 AA4 4 SER A 169 SER A 175 -1 O THR A 170 N VAL A 161
SHEET 4 AA4 4 VAL A 197 PHE A 200 -1 O VAL A 197 N ILE A 171
SHEET 1 AA5 4 ILE A 206 TRP A 207 0
SHEET 2 AA5 4 GLY A 213 ARG A 218 -1 O LEU A 215 N ILE A 206
SHEET 3 AA5 4 MET A 235 LYS A 240 -1 O CYS A 237 N TYR A 216
SHEET 4 AA5 4 ILE A 249 TYR A 252 -1 O TYR A 252 N MET A 236
SHEET 1 AA6 4 ILE A 261 THR A 266 0
SHEET 2 AA6 4 TYR A 272 PHE A 278 -1 O TYR A 274 N ASP A 265
SHEET 3 AA6 4 ASN A 285 GLU A 291 -1 O ALA A 290 N LEU A 273
SHEET 4 AA6 4 ARG A 304 VAL A 307 -1 O ARG A 304 N VAL A 289
SHEET 1 AA7 4 TYR A 314 HIS A 320 0
SHEET 2 AA7 4 LEU A 323 THR A 328 -1 O TYR A 325 N ILE A 317
SHEET 3 AA7 4 LYS A 336 ASP A 341 -1 O LYS A 336 N THR A 328
SHEET 4 AA7 4 GLU A 348 ILE A 353 -1 O PHE A 352 N VAL A 337
SHEET 1 AA8 4 LYS A 360 ALA A 367 0
SHEET 2 AA8 4 TYR A 371 ARG A 378 -1 O VAL A 373 N ASN A 365
SHEET 3 AA8 4 LYS A 381 TYR A 387 -1 O TYR A 387 N PHE A 372
SHEET 4 AA8 4 GLN A 393 LEU A 397 -1 O LEU A 397 N ILE A 384
SHEET 1 AA9 4 ALA A 404 ALA A 408 0
SHEET 2 AA9 4 HIS A 415 GLY A 422 -1 O PHE A 417 N ALA A 408
SHEET 3 AA9 4 THR A 425 ASP A 433 -1 O THR A 428 N LEU A 420
SHEET 4 AA9 4 PHE A 442 THR A 447 -1 O ARG A 446 N ILE A 429
SHEET 1 AB1 8 PHE A 458 GLU A 466 0
SHEET 2 AB1 8 LYS A 472 HIS A 480 -1 O ILE A 473 N TYR A 465
SHEET 3 AB1 8 ILE A 521 PRO A 525 -1 O PHE A 522 N VAL A 478
SHEET 4 AB1 8 ALA A 491 TYR A 494 1 N ILE A 492 O ALA A 523
SHEET 5 AB1 8 VAL A 571 ALA A 576 1 O ALA A 572 N GLN A 493
SHEET 6 AB1 8 ALA A 597 GLU A 601 1 O GLU A 601 N GLY A 575
SHEET 7 AB1 8 ALA A 652 ASN A 658 1 O THR A 656 N PRO A 600
SHEET 8 AB1 8 LEU A 687 ASP A 692 1 O LYS A 690 N ILE A 655
SHEET 1 AB2 2 VAL B 20 SER B 25 0
SHEET 2 AB2 2 GLY B 29 PRO B 34 -1 O GLY B 29 N SER B 25
SHEET 1 AB3 3 LYS B 83 PHE B 84 0
SHEET 2 AB3 3 TRP B 95 ASN B 100 -1 O ASN B 100 N LYS B 83
SHEET 3 AB3 3 THR B 88 LEU B 89 -1 N THR B 88 O TYR B 96
SHEET 1 AB4 4 LYS B 83 PHE B 84 0
SHEET 2 AB4 4 TRP B 95 ASN B 100 -1 O ASN B 100 N LYS B 83
SHEET 3 AB4 4 VAL B 108 SER B 112 -1 O TYR B 110 N TRP B 97
SHEET 4 AB4 4 GLY B 128 PHE B 132 -1 O PHE B 132 N LEU B 109
SHEET 1 AB5 4 GLY B 144 PHE B 150 0
SHEET 2 AB5 4 PHE B 156 SER B 162 -1 O SER B 162 N GLY B 144
SHEET 3 AB5 4 SER B 169 SER B 175 -1 O THR B 170 N VAL B 161
SHEET 4 AB5 4 GLU B 196 PHE B 200 -1 O VAL B 197 N ILE B 171
SHEET 1 AB6 4 ILE B 206 TRP B 207 0
SHEET 2 AB6 4 GLY B 213 ARG B 218 -1 O LEU B 215 N ILE B 206
SHEET 3 AB6 4 MET B 235 LYS B 240 -1 O CYS B 237 N TYR B 216
SHEET 4 AB6 4 ILE B 249 TYR B 252 -1 O TYR B 252 N MET B 236
SHEET 1 AB7 4 ILE B 261 THR B 266 0
SHEET 2 AB7 4 TYR B 272 PHE B 278 -1 O TYR B 274 N ASP B 265
SHEET 3 AB7 4 LEU B 286 GLU B 291 -1 O ALA B 290 N LEU B 273
SHEET 4 AB7 4 ARG B 304 VAL B 307 -1 O ARG B 304 N VAL B 289
SHEET 1 AB8 4 TYR B 314 HIS B 320 0
SHEET 2 AB8 4 LEU B 323 THR B 328 -1 O TYR B 325 N ILE B 317
SHEET 3 AB8 4 LYS B 336 ASP B 341 -1 O LYS B 336 N THR B 328
SHEET 4 AB8 4 GLU B 348 ILE B 353 -1 O PHE B 352 N VAL B 337
SHEET 1 AB9 4 LYS B 360 ALA B 367 0
SHEET 2 AB9 4 TYR B 371 ARG B 378 -1 O VAL B 373 N ASN B 365
SHEET 3 AB9 4 LYS B 381 TYR B 387 -1 O TYR B 387 N PHE B 372
SHEET 4 AB9 4 GLN B 393 LEU B 397 -1 O LEU B 397 N ILE B 384
SHEET 1 AC1 4 ALA B 404 ALA B 408 0
SHEET 2 AC1 4 HIS B 415 GLY B 422 -1 O PHE B 417 N ALA B 408
SHEET 3 AC1 4 THR B 425 ASP B 433 -1 O THR B 428 N LEU B 420
SHEET 4 AC1 4 PHE B 442 THR B 447 -1 O ARG B 446 N ILE B 429
SHEET 1 AC2 8 PHE B 458 GLU B 466 0
SHEET 2 AC2 8 LYS B 472 HIS B 480 -1 O ILE B 473 N TYR B 465
SHEET 3 AC2 8 ILE B 521 PRO B 525 -1 O PHE B 522 N VAL B 478
SHEET 4 AC2 8 ALA B 491 TYR B 494 1 N ILE B 492 O ALA B 523
SHEET 5 AC2 8 VAL B 571 ALA B 576 1 O ALA B 572 N GLN B 493
SHEET 6 AC2 8 ALA B 597 GLU B 601 1 O GLU B 601 N GLY B 575
SHEET 7 AC2 8 ALA B 652 ASN B 658 1 O THR B 656 N PRO B 600
SHEET 8 AC2 8 LEU B 687 ASP B 692 1 O LYS B 690 N ILE B 655
SITE 1 AC1 4 GLU B 268 ASN B 315 ILE B 316 HOH B1153
CRYST1 99.180 115.000 141.450 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010083 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008696 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007070 0.00000
TER 5666 LYS A 727
TER 11282 LYS B 727
TER 11519 CYS C 35
TER 11763 CYS D 35
MASTER 444 0 1 48 82 0 1 612695 4 6 124
END |