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HEADER HYDROLASE 02-OCT-18 6HSW
TITLE A CE15 GLUCURONOYL ESTERASE FROM TEREDINIBACTER TURNERAE T7901
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOHYDRATE ESTERASE FAMILY 15 DOMAIN PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TEREDINIBACTER TURNERAE T7901;
SOURCE 3 ORGANISM_TAXID: 377629;
SOURCE 4 GENE: TERTU_0517;
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: MODIFIED PET28-A
KEYWDS CE15, CARBOHYDRATE ESTERASE, GLUCURONOYL ESTERASE, XYLAN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAZURKEWICH,L.LO LEGGIO,J.C.NAVARRO POULSEN,J.LARSBRINK
REVDAT 1 20-MAR-19 6HSW 0
JRNL AUTH J.ARNLING BAATH,S.MAZURKEWICH,J.C.NAVARRO POULSEN,L.OLSSON,
JRNL AUTH 2 L.LO LEGGIO,J.LARSBRINK
JRNL TITL STRUCTURAL ENZYMOLOGY OF THE GLUCURONOYL ESTERASE TTCE15B
JRNL TITL 2 FROM TEREDINIBACTER TURNERAE REVEALS BINDING TO A VARIETY OF
JRNL TITL 3 LIGNIN- AND CARBOHYDRATE-DERIVED COMPOUNDS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.344
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 92233
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.051
REMARK 3 FREE R VALUE TEST SET COUNT : 969
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.3819 - 4.1069 1.00 13508 144 0.1453 0.2046
REMARK 3 2 4.1069 - 3.2600 1.00 13096 139 0.1436 0.1798
REMARK 3 3 3.2600 - 2.8480 1.00 13039 138 0.1695 0.2257
REMARK 3 4 2.8480 - 2.5876 1.00 12957 138 0.1808 0.2131
REMARK 3 5 2.5876 - 2.4022 1.00 12952 137 0.1901 0.2474
REMARK 3 6 2.4022 - 2.2606 1.00 12889 137 0.2131 0.2631
REMARK 3 7 2.2606 - 2.1473 0.99 12823 136 0.2458 0.2743
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.255
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.125
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.85
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 10137
REMARK 3 ANGLE : 1.055 13757
REMARK 3 CHIRALITY : 0.058 1446
REMARK 3 PLANARITY : 0.008 1819
REMARK 3 DIHEDRAL : 13.120 5871
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6HSW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1200012104.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 300
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979500
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 92246
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.147
REMARK 200 RESOLUTION RANGE LOW (A) : 44.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 20.30
REMARK 200 R MERGE (I) : 0.19780
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.8600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 19.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.370
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME MIXED 50/50 WITH RESERVOIR
REMARK 280 SOLUTION CONTAINING MORPHEUS SCREEN SOLUTION WITH 0.09 M
REMARK 280 HALOGENS (0.3M SODIUM FLUORIDE; 0.3M SODIUM BROMIDE; 0.3M SODIUM
REMARK 280 IODIDE), 0.1 M BUFFER SYSTEM 1 (IMIDAZOLE; MES) , AND 50% V/V
REMARK 280 PRECIPITANT MIX 2 (40% V/V ETHYLENE GLYCOL; 20 % W/V PEG8000),
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 66.06767
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 132.13533
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 132.13533
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 66.06767
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 856 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 880 LIES ON A SPECIAL POSITION.
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 MSE A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 MSE B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 GLY B -2
REMARK 465 HIS B -1
REMARK 465 MSE C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 SER C -10
REMARK 465 SER C -9
REMARK 465 GLU C -8
REMARK 465 ASN C -7
REMARK 465 LEU C -6
REMARK 465 TYR C -5
REMARK 465 PHE C -4
REMARK 465 GLN C -3
REMARK 465 GLY C -2
REMARK 465 HIS C -1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 H GLU C 41 O HOH C 608 1.50
REMARK 500 HD22 ASN A 50 OD1 ASP A 52 1.52
REMARK 500 H ALA B 27 OD1 ASP B 226 1.52
REMARK 500 HG1 THR C 76 O HOH C 607 1.53
REMARK 500 HH12 ARG A 45 O HOH A 606 1.59
REMARK 500 OE2 GLU C 424 O HOH C 601 2.02
REMARK 500 OE2 GLU C 90 O HOH C 602 2.05
REMARK 500 OE2 GLU A 90 O HOH A 601 2.08
REMARK 500 OD2 ASP C 69 O HOH C 603 2.10
REMARK 500 ND2 ASN A 163 O HOH A 602 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASP A 127 OG SER C 121 5565 2.09
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 ALA A 188 -50.53 80.02
REMARK 500 SER A 224 143.32 -170.07
REMARK 500 GLN A 230 -169.88 -128.70
REMARK 500 SER A 281 -124.14 62.01
REMARK 500 PHE A 317 117.23 -166.54
REMARK 500 ASP A 378 75.05 58.43
REMARK 500 PRO A 407 -179.76 -67.34
REMARK 500 VAL A 409 138.70 -39.52
REMARK 500 ASP B 52 22.42 -76.85
REMARK 500 ASP B 126 -155.90 -99.19
REMARK 500 SER B 131 143.62 -27.66
REMARK 500 ASP B 223 55.52 -90.50
REMARK 500 SER B 281 -124.30 59.35
REMARK 500 PHE B 317 113.58 -167.05
REMARK 500 ASP B 378 76.29 55.15
REMARK 500 ASP C 52 50.57 -117.48
REMARK 500 ILE C 104 -71.60 -110.71
REMARK 500 PHE C 182 -73.23 -88.21
REMARK 500 ARG C 183 -74.62 48.50
REMARK 500 SER C 281 -128.21 68.89
REMARK 500 PHE C 317 109.12 -165.37
REMARK 500 ASP C 378 76.23 57.69
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 1PE A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BR C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 509
DBREF 6HSW A 27 445 UNP C5BN23 C5BN23_TERTT 27 445
DBREF 6HSW B 27 445 UNP C5BN23 C5BN23_TERTT 27 445
DBREF 6HSW C 27 445 UNP C5BN23 C5BN23_TERTT 27 445
SEQADV 6HSW MSE A -20 UNP C5BN23 INITIATING METHIONINE
SEQADV 6HSW GLY A -19 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER A -18 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER A -17 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS A -16 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS A -15 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS A -14 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS A -13 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS A -12 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS A -11 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER A -10 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER A -9 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW GLU A -8 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW ASN A -7 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW LEU A -6 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW TYR A -5 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW PHE A -4 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW GLN A -3 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW GLY A -2 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS A -1 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW MSE B -20 UNP C5BN23 INITIATING METHIONINE
SEQADV 6HSW GLY B -19 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER B -18 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER B -17 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS B -16 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS B -15 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS B -14 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS B -13 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS B -12 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS B -11 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER B -10 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER B -9 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW GLU B -8 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW ASN B -7 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW LEU B -6 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW TYR B -5 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW PHE B -4 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW GLN B -3 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW GLY B -2 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS B -1 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW MSE C -20 UNP C5BN23 INITIATING METHIONINE
SEQADV 6HSW GLY C -19 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER C -18 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER C -17 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS C -16 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS C -15 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS C -14 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS C -13 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS C -12 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS C -11 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER C -10 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW SER C -9 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW GLU C -8 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW ASN C -7 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW LEU C -6 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW TYR C -5 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW PHE C -4 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW GLN C -3 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW GLY C -2 UNP C5BN23 EXPRESSION TAG
SEQADV 6HSW HIS C -1 UNP C5BN23 EXPRESSION TAG
SEQRES 1 A 440 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 440 ASN LEU TYR PHE GLN GLY HIS MSE ALA ASP GLN ASP HIS
SEQRES 3 A 440 ALA GLN LEU LEU HIS VAL LEU GLY ILE GLU ASN LEU ARG
SEQRES 4 A 440 ARG GLY ALA ASP GLY ASN THR ASP SER PRO PHE ALA ALA
SEQRES 5 A 440 ASN THR ASP GLU ALA LYS ALA ASN THR ALA LEU ASP SER
SEQRES 6 A 440 LEU PRO PRO LEU LEU THR SER VAL SER GLY GLN ALA ILE
SEQRES 7 A 440 ALA SER ALA THR ASP TRP GLU ALA ASN ARG PRO ALA LEU
SEQRES 8 A 440 LEU ASN THR PHE SER GLN GLU ILE TYR GLY TYR VAL PRO
SEQRES 9 A 440 GLY GLY ALA PRO GLU LEU HIS TRP LYS ALA GLY SER THR
SEQRES 10 A 440 THR PRO ILE ASP ASP SER GLY THR SER ALA ILE ARG GLN
SEQRES 11 A 440 HIS PHE THR SER THR LEU VAL HIS PRO GLU ASN ALA ALA
SEQRES 12 A 440 LEU ASN LEU SER LEU ASN PHE THR LEU VAL LEU PRO LYS
SEQRES 13 A 440 SER ASN LYS PRO VAL PRO VAL VAL VAL VAL MSE SER PHE
SEQRES 14 A 440 ASP PRO GLY ILE TRP GLU ARG PHE ARG ASP ARG MSE PRO
SEQRES 15 A 440 ALA GLU ARG TYR ALA GLN ILE GLN ALA ASP ASN ALA ARG
SEQRES 16 A 440 TRP ARG GLU GLN VAL VAL ASN ALA GLY TRP GLY TYR ALA
SEQRES 17 A 440 GLU ILE ILE PRO THR GLU PHE GLN ALA ASP SER GLY ASP
SEQRES 18 A 440 GLY LEU SER GLN GLY ILE ILE GLY PHE VAL ASN ASN GLY
SEQRES 19 A 440 LYS PRO ARG ASN PRO THR ASP TRP GLY ALA LEU ARG ALA
SEQRES 20 A 440 TRP ALA TRP SER ALA SER GLN VAL LEU THR TYR LEU GLN
SEQRES 21 A 440 THR ASP SER ARG VAL ALA ALA ASP ARG ILE SER VAL HIS
SEQRES 22 A 440 GLY HIS SER ARG PHE GLY LYS ALA ALA LEU VAL ALA MSE
SEQRES 23 A 440 ALA PHE ASP ASN ARG PHE ALA ALA GLY PHE ILE SER SER
SEQRES 24 A 440 SER GLY GLU GLY GLY ALA LYS LEU TRP ARG ARG ASN PHE
SEQRES 25 A 440 GLY GLU GLN VAL GLY ASN LEU ALA GLY ALA GLY GLU TYR
SEQRES 26 A 440 HIS TRP MSE ALA GLY ASN PHE VAL LYS TYR ALA GLY PRO
SEQRES 27 A 440 LYS LYS VAL ASN ASP ILE PRO VAL ASP ALA HIS GLN LEU
SEQRES 28 A 440 LEU ALA LEU CYS ALA PRO ARG PRO VAL LEU VAL SER VAL
SEQRES 29 A 440 GLY SER GLN GLY GLU SER TRP VAL ASP PRO LYS GLY MSE
SEQRES 30 A 440 LEU LEU ALA ALA TYR HIS ALA THR PRO ALA TYR ALA LEU
SEQRES 31 A 440 PHE GLY GLU GLN GLY VAL THR GLN ASN GLU LEU PRO ALA
SEQRES 32 A 440 VAL GLY ASN GLY LEU LEU ALA GLY LYS LEU ALA PHE ARG
SEQRES 33 A 440 GLN HIS GLU GLY GLY HIS THR PRO ALA PRO ASN TRP GLU
SEQRES 34 A 440 THR PHE ILE THR PHE ALA THR ARG GLN TRP ALA
SEQRES 1 B 440 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 B 440 ASN LEU TYR PHE GLN GLY HIS MSE ALA ASP GLN ASP HIS
SEQRES 3 B 440 ALA GLN LEU LEU HIS VAL LEU GLY ILE GLU ASN LEU ARG
SEQRES 4 B 440 ARG GLY ALA ASP GLY ASN THR ASP SER PRO PHE ALA ALA
SEQRES 5 B 440 ASN THR ASP GLU ALA LYS ALA ASN THR ALA LEU ASP SER
SEQRES 6 B 440 LEU PRO PRO LEU LEU THR SER VAL SER GLY GLN ALA ILE
SEQRES 7 B 440 ALA SER ALA THR ASP TRP GLU ALA ASN ARG PRO ALA LEU
SEQRES 8 B 440 LEU ASN THR PHE SER GLN GLU ILE TYR GLY TYR VAL PRO
SEQRES 9 B 440 GLY GLY ALA PRO GLU LEU HIS TRP LYS ALA GLY SER THR
SEQRES 10 B 440 THR PRO ILE ASP ASP SER GLY THR SER ALA ILE ARG GLN
SEQRES 11 B 440 HIS PHE THR SER THR LEU VAL HIS PRO GLU ASN ALA ALA
SEQRES 12 B 440 LEU ASN LEU SER LEU ASN PHE THR LEU VAL LEU PRO LYS
SEQRES 13 B 440 SER ASN LYS PRO VAL PRO VAL VAL VAL VAL MSE SER PHE
SEQRES 14 B 440 ASP PRO GLY ILE TRP GLU ARG PHE ARG ASP ARG MSE PRO
SEQRES 15 B 440 ALA GLU ARG TYR ALA GLN ILE GLN ALA ASP ASN ALA ARG
SEQRES 16 B 440 TRP ARG GLU GLN VAL VAL ASN ALA GLY TRP GLY TYR ALA
SEQRES 17 B 440 GLU ILE ILE PRO THR GLU PHE GLN ALA ASP SER GLY ASP
SEQRES 18 B 440 GLY LEU SER GLN GLY ILE ILE GLY PHE VAL ASN ASN GLY
SEQRES 19 B 440 LYS PRO ARG ASN PRO THR ASP TRP GLY ALA LEU ARG ALA
SEQRES 20 B 440 TRP ALA TRP SER ALA SER GLN VAL LEU THR TYR LEU GLN
SEQRES 21 B 440 THR ASP SER ARG VAL ALA ALA ASP ARG ILE SER VAL HIS
SEQRES 22 B 440 GLY HIS SER ARG PHE GLY LYS ALA ALA LEU VAL ALA MSE
SEQRES 23 B 440 ALA PHE ASP ASN ARG PHE ALA ALA GLY PHE ILE SER SER
SEQRES 24 B 440 SER GLY GLU GLY GLY ALA LYS LEU TRP ARG ARG ASN PHE
SEQRES 25 B 440 GLY GLU GLN VAL GLY ASN LEU ALA GLY ALA GLY GLU TYR
SEQRES 26 B 440 HIS TRP MSE ALA GLY ASN PHE VAL LYS TYR ALA GLY PRO
SEQRES 27 B 440 LYS LYS VAL ASN ASP ILE PRO VAL ASP ALA HIS GLN LEU
SEQRES 28 B 440 LEU ALA LEU CYS ALA PRO ARG PRO VAL LEU VAL SER VAL
SEQRES 29 B 440 GLY SER GLN GLY GLU SER TRP VAL ASP PRO LYS GLY MSE
SEQRES 30 B 440 LEU LEU ALA ALA TYR HIS ALA THR PRO ALA TYR ALA LEU
SEQRES 31 B 440 PHE GLY GLU GLN GLY VAL THR GLN ASN GLU LEU PRO ALA
SEQRES 32 B 440 VAL GLY ASN GLY LEU LEU ALA GLY LYS LEU ALA PHE ARG
SEQRES 33 B 440 GLN HIS GLU GLY GLY HIS THR PRO ALA PRO ASN TRP GLU
SEQRES 34 B 440 THR PHE ILE THR PHE ALA THR ARG GLN TRP ALA
SEQRES 1 C 440 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 C 440 ASN LEU TYR PHE GLN GLY HIS MSE ALA ASP GLN ASP HIS
SEQRES 3 C 440 ALA GLN LEU LEU HIS VAL LEU GLY ILE GLU ASN LEU ARG
SEQRES 4 C 440 ARG GLY ALA ASP GLY ASN THR ASP SER PRO PHE ALA ALA
SEQRES 5 C 440 ASN THR ASP GLU ALA LYS ALA ASN THR ALA LEU ASP SER
SEQRES 6 C 440 LEU PRO PRO LEU LEU THR SER VAL SER GLY GLN ALA ILE
SEQRES 7 C 440 ALA SER ALA THR ASP TRP GLU ALA ASN ARG PRO ALA LEU
SEQRES 8 C 440 LEU ASN THR PHE SER GLN GLU ILE TYR GLY TYR VAL PRO
SEQRES 9 C 440 GLY GLY ALA PRO GLU LEU HIS TRP LYS ALA GLY SER THR
SEQRES 10 C 440 THR PRO ILE ASP ASP SER GLY THR SER ALA ILE ARG GLN
SEQRES 11 C 440 HIS PHE THR SER THR LEU VAL HIS PRO GLU ASN ALA ALA
SEQRES 12 C 440 LEU ASN LEU SER LEU ASN PHE THR LEU VAL LEU PRO LYS
SEQRES 13 C 440 SER ASN LYS PRO VAL PRO VAL VAL VAL VAL MSE SER PHE
SEQRES 14 C 440 ASP PRO GLY ILE TRP GLU ARG PHE ARG ASP ARG MSE PRO
SEQRES 15 C 440 ALA GLU ARG TYR ALA GLN ILE GLN ALA ASP ASN ALA ARG
SEQRES 16 C 440 TRP ARG GLU GLN VAL VAL ASN ALA GLY TRP GLY TYR ALA
SEQRES 17 C 440 GLU ILE ILE PRO THR GLU PHE GLN ALA ASP SER GLY ASP
SEQRES 18 C 440 GLY LEU SER GLN GLY ILE ILE GLY PHE VAL ASN ASN GLY
SEQRES 19 C 440 LYS PRO ARG ASN PRO THR ASP TRP GLY ALA LEU ARG ALA
SEQRES 20 C 440 TRP ALA TRP SER ALA SER GLN VAL LEU THR TYR LEU GLN
SEQRES 21 C 440 THR ASP SER ARG VAL ALA ALA ASP ARG ILE SER VAL HIS
SEQRES 22 C 440 GLY HIS SER ARG PHE GLY LYS ALA ALA LEU VAL ALA MSE
SEQRES 23 C 440 ALA PHE ASP ASN ARG PHE ALA ALA GLY PHE ILE SER SER
SEQRES 24 C 440 SER GLY GLU GLY GLY ALA LYS LEU TRP ARG ARG ASN PHE
SEQRES 25 C 440 GLY GLU GLN VAL GLY ASN LEU ALA GLY ALA GLY GLU TYR
SEQRES 26 C 440 HIS TRP MSE ALA GLY ASN PHE VAL LYS TYR ALA GLY PRO
SEQRES 27 C 440 LYS LYS VAL ASN ASP ILE PRO VAL ASP ALA HIS GLN LEU
SEQRES 28 C 440 LEU ALA LEU CYS ALA PRO ARG PRO VAL LEU VAL SER VAL
SEQRES 29 C 440 GLY SER GLN GLY GLU SER TRP VAL ASP PRO LYS GLY MSE
SEQRES 30 C 440 LEU LEU ALA ALA TYR HIS ALA THR PRO ALA TYR ALA LEU
SEQRES 31 C 440 PHE GLY GLU GLN GLY VAL THR GLN ASN GLU LEU PRO ALA
SEQRES 32 C 440 VAL GLY ASN GLY LEU LEU ALA GLY LYS LEU ALA PHE ARG
SEQRES 33 C 440 GLN HIS GLU GLY GLY HIS THR PRO ALA PRO ASN TRP GLU
SEQRES 34 C 440 THR PHE ILE THR PHE ALA THR ARG GLN TRP ALA
MODRES 6HSW MSE A 0 MODIFIED RESIDUE
MODRES 6HSW MSE A 172 MET MODIFIED RESIDUE
MODRES 6HSW MSE A 186 MET MODIFIED RESIDUE
MODRES 6HSW MSE A 291 MET MODIFIED RESIDUE
MODRES 6HSW MSE A 333 MET MODIFIED RESIDUE
MODRES 6HSW MSE A 382 MET MODIFIED RESIDUE
MODRES 6HSW MSE B 0 MODIFIED RESIDUE
MODRES 6HSW MSE B 172 MET MODIFIED RESIDUE
MODRES 6HSW MSE B 186 MET MODIFIED RESIDUE
MODRES 6HSW MSE B 291 MET MODIFIED RESIDUE
MODRES 6HSW MSE B 333 MET MODIFIED RESIDUE
MODRES 6HSW MSE B 382 MET MODIFIED RESIDUE
MODRES 6HSW MSE C 0 MODIFIED RESIDUE
MODRES 6HSW MSE C 172 MET MODIFIED RESIDUE
MODRES 6HSW MSE C 186 MET MODIFIED RESIDUE
MODRES 6HSW MSE C 291 MET MODIFIED RESIDUE
MODRES 6HSW MSE C 333 MET MODIFIED RESIDUE
MODRES 6HSW MSE C 382 MET MODIFIED RESIDUE
HET MSE A 0 17
HET MSE A 172 17
HET MSE A 186 17
HET MSE A 291 17
HET MSE A 333 17
HET MSE A 382 17
HET MSE B 0 36
HET MSE B 172 17
HET MSE B 186 17
HET MSE B 291 17
HET MSE B 333 17
HET MSE B 382 17
HET MSE C 0 18
HET MSE C 172 17
HET MSE C 186 17
HET MSE C 291 17
HET MSE C 333 17
HET MSE C 382 17
HET 1PE A 501 38
HET EDO A 502 10
HET EDO A 503 10
HET EDO A 504 10
HET EDO A 505 10
HET EDO A 506 10
HET EDO A 507 10
HET EDO A 508 10
HET GOL A 509 14
HET GOL A 510 14
HET GOL A 511 14
HET BR B 501 1
HET 1PE B 502 38
HET EDO B 503 10
HET EDO B 504 10
HET EDO B 505 10
HET EDO B 506 10
HET EDO B 507 10
HET EDO B 508 10
HET EDO B 509 10
HET GOL B 510 14
HET GOL B 511 13
HET GOL B 512 12
HET GOL B 513 13
HET GOL B 514 13
HET GOL B 515 14
HET GOL B 516 14
HET GOL B 517 13
HET GOL B 518 13
HET BR C 501 1
HET PEG C 502 17
HET EDO C 503 10
HET EDO C 504 10
HET EDO C 505 10
HET EDO C 506 10
HET EDO C 507 10
HET EDO C 508 10
HET GOL C 509 14
HETNAM MSE SELENOMETHIONINE
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETNAM BR BROMIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN 1PE PEG400
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 4 1PE 2(C10 H22 O6)
FORMUL 5 EDO 20(C2 H6 O2)
FORMUL 12 GOL 13(C3 H8 O3)
FORMUL 15 BR 2(BR 1-)
FORMUL 34 PEG C4 H10 O3
FORMUL 42 HOH *821(H2 O)
HELIX 1 AA1 GLY A -2 GLY A 39 1 16
HELIX 2 AA2 ASP A 60 ALA A 64 5 5
HELIX 3 AA3 ASN A 65 LEU A 71 5 7
HELIX 4 AA4 SER A 85 ILE A 104 1 20
HELIX 5 AA5 ASN A 146 ASN A 150 5 5
HELIX 6 AA6 PRO A 176 PHE A 182 1 7
HELIX 7 AA7 ARG A 183 MSE A 186 5 4
HELIX 8 AA8 ALA A 188 ALA A 208 1 21
HELIX 9 AA9 ILE A 216 PHE A 220 5 5
HELIX 10 AB1 SER A 224 LEU A 228 5 5
HELIX 11 AB2 GLN A 230 ASN A 237 1 8
HELIX 12 AB3 GLY A 248 GLN A 265 1 18
HELIX 13 AB4 SER A 281 ASP A 294 1 14
HELIX 14 AB5 GLN A 320 ALA A 325 1 6
HELIX 15 AB6 GLU A 329 MSE A 333 5 5
HELIX 16 AB7 ALA A 334 GLY A 342 5 9
HELIX 17 AB8 LYS A 345 ILE A 349 5 5
HELIX 18 AB9 ASP A 352 LEU A 359 1 8
HELIX 19 AC1 GLU A 374 VAL A 377 5 4
HELIX 20 AC2 ASP A 378 PHE A 396 1 19
HELIX 21 AC3 PRO A 429 PRO A 431 5 3
HELIX 22 AC4 ASN A 432 ALA A 445 1 14
HELIX 23 AC5 ALA B 27 GLY B 39 1 13
HELIX 24 AC6 ASP B 60 ALA B 64 5 5
HELIX 25 AC7 ASN B 65 LEU B 71 5 7
HELIX 26 AC8 SER B 85 ILE B 104 1 20
HELIX 27 AC9 ASN B 146 ASN B 150 5 5
HELIX 28 AD1 PRO B 176 ARG B 181 1 6
HELIX 29 AD2 PHE B 182 MSE B 186 5 5
HELIX 30 AD3 PRO B 187 ALA B 208 1 22
HELIX 31 AD4 ILE B 216 GLN B 221 1 6
HELIX 32 AD5 SER B 224 LEU B 228 5 5
HELIX 33 AD6 GLN B 230 ASN B 237 1 8
HELIX 34 AD7 GLY B 248 GLN B 265 1 18
HELIX 35 AD8 SER B 281 ASP B 294 1 14
HELIX 36 AD9 GLN B 320 GLY B 326 1 7
HELIX 37 AE1 GLU B 329 MSE B 333 5 5
HELIX 38 AE2 ALA B 334 GLY B 342 5 9
HELIX 39 AE3 LYS B 345 ILE B 349 5 5
HELIX 40 AE4 ASP B 352 LEU B 359 1 8
HELIX 41 AE5 GLU B 374 VAL B 377 5 4
HELIX 42 AE6 ASP B 378 LEU B 395 1 18
HELIX 43 AE7 PRO B 429 PRO B 431 5 3
HELIX 44 AE8 ASN B 432 ALA B 445 1 14
HELIX 45 AE9 ALA C 27 LEU C 38 1 12
HELIX 46 AF1 ASP C 60 ALA C 64 5 5
HELIX 47 AF2 ASN C 65 LEU C 71 5 7
HELIX 48 AF3 SER C 85 ILE C 104 1 20
HELIX 49 AF4 ASN C 146 ASN C 150 5 5
HELIX 50 AF5 PRO C 187 ALA C 208 1 22
HELIX 51 AF6 ILE C 216 PHE C 220 5 5
HELIX 52 AF7 SER C 224 LEU C 228 5 5
HELIX 53 AF8 GLN C 230 ASN C 237 1 8
HELIX 54 AF9 GLY C 248 GLN C 265 1 18
HELIX 55 AG1 SER C 281 ASP C 294 1 14
HELIX 56 AG2 GLN C 320 GLY C 326 1 7
HELIX 57 AG3 GLU C 329 MSE C 333 5 5
HELIX 58 AG4 ALA C 334 GLY C 342 5 9
HELIX 59 AG5 LYS C 345 ILE C 349 5 5
HELIX 60 AG6 ASP C 352 LEU C 359 1 8
HELIX 61 AG7 GLU C 374 VAL C 377 5 4
HELIX 62 AG8 ASP C 378 PHE C 396 1 19
HELIX 63 AG9 PRO C 429 PRO C 431 5 3
HELIX 64 AH1 ASN C 432 ALA C 445 1 14
SHEET 1 AA1 3 LYS A 118 ALA A 119 0
SHEET 2 AA1 3 ILE A 133 LEU A 141 -1 O THR A 138 N LYS A 118
SHEET 3 AA1 3 THR A 123 PRO A 124 -1 N THR A 123 O ARG A 134
SHEET 1 AA2 9 LYS A 118 ALA A 119 0
SHEET 2 AA2 9 ILE A 133 LEU A 141 -1 O THR A 138 N LYS A 118
SHEET 3 AA2 9 LEU A 151 LEU A 159 -1 O LEU A 157 N GLN A 135
SHEET 4 AA2 9 GLY A 211 ILE A 215 -1 O TYR A 212 N VAL A 158
SHEET 5 AA2 9 VAL A 166 MSE A 172 1 N PRO A 167 O GLY A 211
SHEET 6 AA2 9 VAL A 270 HIS A 280 1 O SER A 276 N VAL A 170
SHEET 7 AA2 9 ALA A 299 SER A 303 1 O PHE A 301 N VAL A 277
SHEET 8 AA2 9 VAL A 365 VAL A 369 1 O LEU A 366 N GLY A 300
SHEET 9 AA2 9 LEU A 418 GLN A 422 1 O ALA A 419 N VAL A 365
SHEET 1 AA3 3 LYS B 118 ALA B 119 0
SHEET 2 AA3 3 ILE B 133 LEU B 141 -1 O THR B 138 N LYS B 118
SHEET 3 AA3 3 THR B 123 PRO B 124 -1 N THR B 123 O ARG B 134
SHEET 1 AA4 9 LYS B 118 ALA B 119 0
SHEET 2 AA4 9 ILE B 133 LEU B 141 -1 O THR B 138 N LYS B 118
SHEET 3 AA4 9 LEU B 151 LEU B 159 -1 O LEU B 153 N SER B 139
SHEET 4 AA4 9 GLY B 211 ILE B 215 -1 O TYR B 212 N VAL B 158
SHEET 5 AA4 9 VAL B 166 MSE B 172 1 N PRO B 167 O GLY B 211
SHEET 6 AA4 9 VAL B 270 HIS B 280 1 O SER B 276 N VAL B 170
SHEET 7 AA4 9 ALA B 299 SER B 303 1 O PHE B 301 N VAL B 277
SHEET 8 AA4 9 VAL B 365 VAL B 369 1 O LEU B 366 N GLY B 300
SHEET 9 AA4 9 LEU B 418 GLN B 422 1 O ALA B 419 N VAL B 367
SHEET 1 AA5 3 TRP C 117 ALA C 119 0
SHEET 2 AA5 3 ILE C 133 LEU C 141 -1 O THR C 138 N LYS C 118
SHEET 3 AA5 3 THR C 123 PRO C 124 -1 N THR C 123 O ARG C 134
SHEET 1 AA6 9 TRP C 117 ALA C 119 0
SHEET 2 AA6 9 ILE C 133 LEU C 141 -1 O THR C 138 N LYS C 118
SHEET 3 AA6 9 LEU C 151 LEU C 159 -1 O LEU C 157 N GLN C 135
SHEET 4 AA6 9 GLY C 211 ILE C 215 -1 O GLU C 214 N THR C 156
SHEET 5 AA6 9 VAL C 166 MSE C 172 1 N PRO C 167 O GLY C 211
SHEET 6 AA6 9 VAL C 270 HIS C 280 1 O SER C 276 N VAL C 170
SHEET 7 AA6 9 GLY C 300 SER C 303 1 O PHE C 301 N VAL C 277
SHEET 8 AA6 9 VAL C 365 VAL C 369 1 O LEU C 366 N GLY C 300
SHEET 9 AA6 9 LEU C 418 GLN C 422 1 O ALA C 419 N VAL C 365
LINK C HIS A -1 N MSE A 0 1555 1555 1.33
LINK C MSE A 0 N ALA A 27 1555 1555 1.33
LINK C VAL A 171 N MSE A 172 1555 1555 1.33
LINK C MSE A 172 N SER A 173 1555 1555 1.32
LINK C ARG A 185 N MSE A 186 1555 1555 1.33
LINK C MSE A 186 N PRO A 187 1555 1555 1.33
LINK C ALA A 290 N MSE A 291 1555 1555 1.33
LINK C MSE A 291 N ALA A 292 1555 1555 1.33
LINK C TRP A 332 N MSE A 333 1555 1555 1.32
LINK C MSE A 333 N ALA A 334 1555 1555 1.32
LINK C GLY A 381 N MSE A 382 1555 1555 1.32
LINK C MSE A 382 N LEU A 383 1555 1555 1.34
LINK C AMSE B 0 N ALA B 27 1555 1555 1.34
LINK C BMSE B 0 N ALA B 27 1555 1555 1.34
LINK C VAL B 171 N MSE B 172 1555 1555 1.32
LINK C MSE B 172 N SER B 173 1555 1555 1.33
LINK C ARG B 185 N MSE B 186 1555 1555 1.32
LINK C MSE B 186 N PRO B 187 1555 1555 1.33
LINK C ALA B 290 N MSE B 291 1555 1555 1.32
LINK C MSE B 291 N ALA B 292 1555 1555 1.33
LINK C TRP B 332 N MSE B 333 1555 1555 1.32
LINK C MSE B 333 N ALA B 334 1555 1555 1.33
LINK C GLY B 381 N MSE B 382 1555 1555 1.31
LINK C MSE B 382 N LEU B 383 1555 1555 1.34
LINK C MSE C 0 N ALA C 27 1555 1555 1.34
LINK C VAL C 171 N MSE C 172 1555 1555 1.31
LINK C MSE C 172 N SER C 173 1555 1555 1.33
LINK C ARG C 185 N MSE C 186 1555 1555 1.33
LINK C MSE C 186 N PRO C 187 1555 1555 1.33
LINK C ALA C 290 N MSE C 291 1555 1555 1.32
LINK C MSE C 291 N ALA C 292 1555 1555 1.34
LINK C TRP C 332 N MSE C 333 1555 1555 1.32
LINK C MSE C 333 N ALA C 334 1555 1555 1.34
LINK C GLY C 381 N MSE C 382 1555 1555 1.33
LINK C MSE C 382 N LEU C 383 1555 1555 1.34
CISPEP 1 ALA A 361 PRO A 362 0 6.21
CISPEP 2 ALA B 361 PRO B 362 0 1.09
CISPEP 3 ALA C 361 PRO C 362 0 0.47
SITE 1 AC1 10 ARG A 44 PHE A 55 ALA A 56 LYS A 63
SITE 2 AC1 10 PRO A 187 GLU A 189 ARG A 190 ASN A 316
SITE 3 AC1 10 GLN A 320 HOH A 785
SITE 1 AC2 4 LEU A 151 SER A 152 HOH A 648 HOH A 753
SITE 1 AC3 1 HOH A 806
SITE 1 AC4 4 GLN A 204 GLU A 434 THR A 438 HOH A 717
SITE 1 AC5 3 LYS A 118 HIS A 136 THR A 138
SITE 1 AC6 3 ARG A 251 TRP A 255 SER A 258
SITE 1 AC7 6 GLN A 265 THR A 266 SER A 268 HOH A 681
SITE 2 AC7 6 HOH A 842 HOH B 787
SITE 1 AC8 2 ARG A 274 TRP A 444
SITE 1 AC9 7 LYS A 161 SER A 162 PRO A 165 SER A 268
SITE 2 AC9 7 HOH A 710 THR B 435 HOH B 601
SITE 1 AD1 2 ARG B 200 ASN B 207
SITE 1 AD2 9 ARG B 45 ALA B 56 LYS B 63 THR B 66
SITE 2 AD2 9 ASN B 316 GLN B 320 HOH B 842 GLU C 189
SITE 3 AD2 9 ARG C 190
SITE 1 AD3 5 PRO B 73 LEU B 74 LEU B 75 HOH B 611
SITE 2 AD3 5 HOH B 739
SITE 1 AD4 3 TRP B 444 ALA B 445 HOH B 667
SITE 1 AD5 3 THR B 438 THR B 441 ARG B 442
SITE 1 AD6 1 GLN B 33
SITE 1 AD7 3 SER B 268 HOH B 657 HOH B 832
SITE 1 AD8 6 GLU B 424 GLY B 425 PRO B 431 HOH B 618
SITE 2 AD8 6 HOH B 731 HOH C 643
SITE 1 AD9 4 GLN B 265 ALA B 272 ARG B 296 HOH B 758
SITE 1 AE1 4 GLY B 373 SER B 375 HOH B 685 HOH B 845
SITE 1 AE2 2 THR B 99 PRO B 350
SITE 1 AE3 4 TYR B 387 HIS B 388 PRO B 391 HOH B 686
SITE 1 AE4 4 HIS B 280 HOH B 613 HOH B 644 HOH B 808
SITE 1 AE5 8 PRO B 187 ALA B 188 GLU B 189 HOH B 615
SITE 2 AE5 8 HOH B 616 HOH B 654 ARG C 44 LYS C 345
SITE 1 AE6 4 SER B 162 ASN B 163 SER B 268 HOH B 791
SITE 1 AE7 5 THR B 218 GLU B 219 GLN B 230 HOH B 637
SITE 2 AE7 5 HOH B 757
SITE 1 AE8 2 ALA B 394 LEU B 395
SITE 1 AE9 11 GLU B 307 LYS B 311 TRP B 313 ARG B 315
SITE 2 AE9 11 ASN B 316 GLN B 320 VAL B 321 VAL B 346
SITE 3 AE9 11 HOH B 602 HOH B 736 HOH B 831
SITE 1 AF1 2 ARG C 200 ASN C 207
SITE 1 AF2 5 ARG C 251 ALA C 254 TRP C 255 SER C 258
SITE 2 AF2 5 PHE C 293
SITE 1 AF3 3 ARG B 45 ARG C 181 ARG C 185
SITE 1 AF4 7 ARG C 44 ARG C 45 GLY C 322 ALA C 325
SITE 2 AF4 7 GLY C 326 HOH C 673 HOH C 696
SITE 1 AF5 3 SER C 229 GLN C 230 GLY C 239
SITE 1 AF6 6 GLN C 204 GLU C 434 ILE C 437 THR C 438
SITE 2 AF6 6 HOH C 638 HOH C 644
SITE 1 AF7 2 ALA C 86 GLU C 90
CRYST1 121.173 121.173 198.203 90.00 90.00 120.00 P 31 2 1 18
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 0.008253 0.004765 0.000000 0.00000
SCALE2 0.000000 0.009529 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005045 0.00000
TER 6378 ALA A 445
TER 12726 ALA B 445
TER 19037 ALA C 445
MASTER 513 0 56 64 36 0 49 610664 3 822 102
END |