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HEADER HYDROLASE 01-OCT-19 6SYR
TITLE THE WILD TYPE GLUCURONOYL ESTERASE OTCE15A FROM OPITUTUS TERRAE IN
TITLE 2 COMPLEX WITH D-GLUCURONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCURONOYL ESTERASE OTCE15A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OPITUTUS TERRAE PB90-1;
SOURCE 3 ORGANISM_TAXID: 452637;
SOURCE 4 GENE: OTER_0116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS ESTERASE, COMPLEX, BIOMASS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
REVDAT 1 27-NOV-19 6SYR 0
JRNL AUTH S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
JRNL TITL THE WILD TYPE GLUCURONOYL ESTERASE OTCE15A FROM OPITUTUS
JRNL TITL 2 TERRAE IN COMPLEX WITH D-GLUCURONATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 47109
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.470
REMARK 3 FREE R VALUE TEST SET COUNT : 3520
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 32.6900 - 4.3500 0.98 1882 151 0.1422 0.1864
REMARK 3 2 4.3500 - 3.4600 0.97 1866 150 0.1262 0.1604
REMARK 3 3 3.4600 - 3.0200 0.98 1868 148 0.1470 0.1907
REMARK 3 4 3.0200 - 2.7400 0.98 1865 152 0.1541 0.1910
REMARK 3 5 2.7400 - 2.5500 0.96 1826 145 0.1568 0.1775
REMARK 3 6 2.5500 - 2.4000 0.71 1373 116 0.1559 0.1894
REMARK 3 7 2.4000 - 2.2800 0.82 1556 128 0.1577 0.2038
REMARK 3 8 2.2800 - 2.1800 0.87 1676 135 0.1688 0.2280
REMARK 3 9 2.1800 - 2.0900 0.89 1693 129 0.1670 0.2476
REMARK 3 10 2.0900 - 2.0200 0.90 1716 138 0.1881 0.2557
REMARK 3 11 2.0200 - 1.9600 0.90 1730 140 0.1839 0.2094
REMARK 3 12 1.9600 - 1.9000 0.91 1765 132 0.1913 0.2478
REMARK 3 13 1.9000 - 1.8500 0.92 1730 147 0.1982 0.2816
REMARK 3 14 1.8500 - 1.8100 0.92 1746 142 0.2166 0.2626
REMARK 3 15 1.8100 - 1.7700 0.92 1771 142 0.2499 0.2825
REMARK 3 16 1.7700 - 1.7300 0.92 1746 137 0.2832 0.3166
REMARK 3 17 1.7300 - 1.6900 0.91 1755 146 0.2938 0.3424
REMARK 3 18 1.6900 - 1.6600 0.92 1764 151 0.3403 0.3842
REMARK 3 19 1.6600 - 1.6300 0.92 1738 139 0.3626 0.4019
REMARK 3 20 1.6300 - 1.6100 0.92 1786 146 0.3772 0.3597
REMARK 3 21 1.6100 - 1.5800 0.92 1741 135 0.4034 0.4996
REMARK 3 22 1.5800 - 1.5500 0.92 1770 147 0.4233 0.4493
REMARK 3 23 1.5500 - 1.5300 0.91 1749 132 0.4634 0.4636
REMARK 3 24 1.5300 - 1.5100 0.91 1762 150 0.5087 0.5013
REMARK 3 25 1.5100 - 1.4900 0.92 1715 142 0.5713 0.5672
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) : 0.232
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.996
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.11
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 3252
REMARK 3 ANGLE : 1.050 4445
REMARK 3 CHIRALITY : 0.076 469
REMARK 3 PLANARITY : 0.008 595
REMARK 3 DIHEDRAL : 18.475 1177
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 6SYR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-OCT-19.
REMARK 100 THE DEPOSITION ID IS D_1292104569.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918374
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47249
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 32.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06132
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 1.41600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.820
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.15.2_3472
REMARK 200 STARTING MODEL: 6GS0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: BASED ON THE MORPHEUS SCREEN FROM
REMARK 280 MOLECULAR DIMENSIONS: G12 - 0.1 M CARBOXYLIC ACIDS, 0.1 M BUFFER
REMARK 280 SYSTEM 3, PH 8.5, 50 % V/V PRECIPITANT MIX 4, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 TOTAL BURIED SURFACE AREA: 1230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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 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 ARG A 2
REMARK 465 ASN A 3
REMARK 465 VAL A 4
REMARK 465 LEU A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 7
REMARK 465 LEU A 8
REMARK 465 SER A 9
REMARK 465 LEU A 10
REMARK 465 LEU A 11
REMARK 465 PHE A 12
REMARK 465 THR A 13
REMARK 465 LEU A 14
REMARK 465 THR A 15
REMARK 465 SER A 16
REMARK 465 MET A 17
REMARK 465 GLN A 18
REMARK 465 ALA A 19
REMARK 465 THR A 20
REMARK 465 SER A 21
REMARK 465 ARG A 22
REMARK 465 PRO A 23
REMARK 465 ALA A 24
REMARK 465 ARG A 25
REMARK 465 LEU A 26
REMARK 465 ASP A 27
REMARK 465 ASP A 28
REMARK 465 THR A 29
REMARK 465 PRO A 30
REMARK 465 PRO A 31
REMARK 465 PRO A 32
REMARK 465 ALA A 33
REMARK 465 TYR A 34
REMARK 465 ALA A 432
REMARK 465 ARG A 433
REMARK 465 GLU A 434
REMARK 465 PRO A 435
REMARK 465 GLN A 436
REMARK 465 ARG A 437
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 HH12 ARG A 51 OD2 ASP A 110 1654 1.56
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 VAL A 70 -71.11 -121.73
REMARK 500 ASP A 150 110.84 -35.78
REMARK 500 LEU A 220 31.57 -89.09
REMARK 500 ASP A 221 -118.54 147.34
REMARK 500 ALA A 222 -39.75 58.79
REMARK 500 ALA A 223 -148.83 54.40
REMARK 500 SER A 267 -127.73 57.59
REMARK 500 HIS A 328 37.49 -147.59
REMARK 500 ASP A 360 72.31 58.89
REMARK 500 LYS A 427 151.20 -44.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 507 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 250 O
REMARK 620 2 ASP A 253 O 93.8
REMARK 620 3 VAL A 256 O 114.6 79.9
REMARK 620 4 HOH A 750 O 109.0 156.3 84.5
REMARK 620 5 HOH A 778 O 133.5 86.6 111.2 82.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 303 O
REMARK 620 2 GLU A 305 O 93.7
REMARK 620 3 HOH A 727 O 100.8 94.5
REMARK 620 4 HOH A 605 O 89.2 89.5 169.0
REMARK 620 5 HOH A 802 O 163.6 88.9 95.1 74.7
REMARK 620 6 HOH A 722 O 92.1 162.0 101.2 73.5 80.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GCU A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 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 NA A 507
DBREF 6SYR A 1 437 UNP B1ZMF4 B1ZMF4_OPITP 1 437
SEQRES 1 A 437 MET ARG ASN VAL LEU ALA ALA LEU SER LEU LEU PHE THR
SEQRES 2 A 437 LEU THR SER MET GLN ALA THR SER ARG PRO ALA ARG LEU
SEQRES 3 A 437 ASP ASP THR PRO PRO PRO ALA TYR THR LEU PRO ASP PRO
SEQRES 4 A 437 LEU VAL GLY ALA ASP GLY THR ARG VAL HIS ASP ARG ALA
SEQRES 5 A 437 THR TRP GLN HIS ARG ARG ARG PRO GLU LEU LEU GLN LEU
SEQRES 6 A 437 PHE ALA ARG GLU VAL TYR GLY ARG THR PRO LEU GLY ARG
SEQRES 7 A 437 PRO GLU GLY MET VAL PHE LYS VAL THR THR MET GLU HIS
SEQRES 8 A 437 ALA ALA LEU GLY GLY ALA ALA THR ARG LYS GLU VAL THR
SEQRES 9 A 437 VAL ARG PHE GLY ARG ASP PRO ASN ALA PRO SER MET GLN
SEQRES 10 A 437 LEU LEU LEU TYR VAL PRO ASN ALA VAL ILE ALA ARG ALA
SEQRES 11 A 437 GLU ARG ALA PRO VAL PHE LEU GLY LEU ASN PHE TYR GLY
SEQRES 12 A 437 ASN HIS THR VAL HIS THR ASP PRO ALA ILE ALA LEU SER
SEQRES 13 A 437 ALA ARG TRP ILE PRO ALA GLU ALA PRO ASN GLY ALA ASN
SEQRES 14 A 437 HIS ARG ALA THR GLU ALA ALA ARG GLY SER ASP ALA GLN
SEQRES 15 A 437 LYS TRP PRO VAL GLU GLN ILE LEU ALA ARG GLY TYR ALA
SEQRES 16 A 437 VAL ALA THR VAL TYR CYS GLY ASP LEU CYS PRO ASP ARG
SEQRES 17 A 437 PRO ASP GLY LEU ASN ALA SER VAL ALA SER TRP LEU ASP
SEQRES 18 A 437 ALA ALA ALA GLY ASP GLN ARG ALA PRO ASP ALA TRP GLY
SEQRES 19 A 437 ALA ILE GLY VAL TRP ALA TRP GLY LEU SER ARG ALA LEU
SEQRES 20 A 437 ASP TYR LEU GLU THR ASP PRO LEU VAL ASP ALA SER ARG
SEQRES 21 A 437 VAL ALA VAL HIS GLY HIS SER ARG LEU GLY LYS ALA ALA
SEQRES 22 A 437 LEU TRP ALA GLY ALA GLN ASP ASP ARG PHE ALA LEU VAL
SEQRES 23 A 437 ILE SER ASN GLU SER GLY CYS GLY GLY ALA ALA LEU SER
SEQRES 24 A 437 LYS ARG ILE HIS GLY GLU THR VAL ALA ARG ILE ASN THR
SEQRES 25 A 437 VAL PHE PRO HIS TRP PHE ALA ARG ASN PHE ARG ARG TYR
SEQRES 26 A 437 ASP ASP HIS GLU GLU ALA LEU PRO VAL ASP GLN HIS GLU
SEQRES 27 A 437 LEU LEU ALA LEU VAL ALA PRO ARG PRO LEU TYR VAL ALA
SEQRES 28 A 437 SER ALA GLU ASP ASP ASP TRP ALA ASP PRO ARG GLY GLU
SEQRES 29 A 437 PHE LEU ALA VAL LYS ALA ALA GLU PRO VAL PHE ARG LEU
SEQRES 30 A 437 PHE GLY GLN THR GLY PRO SER GLY GLU ASP VAL PRO ARG
SEQRES 31 A 437 VAL ASN GLU PRO SER GLY GLY ALA LEU ARG TYR HIS ILE
SEQRES 32 A 437 ARG PRO GLY PRO HIS GLY MET THR ALA GLN ASP TRP ALA
SEQRES 33 A 437 PHE TYR LEU ALA PHE ALA ASP GLU TRP LEU LYS SER ALA
SEQRES 34 A 437 LEU PRO ALA ARG GLU PRO GLN ARG
HET GCU A 501 22
HET MG A 502 1
HET EDO A 503 10
HET EDO A 504 10
HET EDO A 505 10
HET EDO A 506 10
HET NA A 507 1
HETNAM GCU D-GLUCURONIC ACID
HETNAM MG MAGNESIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 GCU C6 H10 O7
FORMUL 3 MG MG 2+
FORMUL 4 EDO 4(C2 H6 O2)
FORMUL 8 NA NA 1+
FORMUL 9 HOH *227(H2 O)
HELIX 1 AA1 ASP A 50 ARG A 57 1 8
HELIX 2 AA2 ARG A 57 VAL A 70 1 14
HELIX 3 AA3 LEU A 94 GLY A 96 5 3
HELIX 4 AA4 ASN A 124 ALA A 128 1 5
HELIX 5 AA5 GLY A 143 VAL A 147 5 5
HELIX 6 AA6 THR A 173 ARG A 177 5 5
HELIX 7 AA7 ASP A 180 TRP A 184 5 5
HELIX 8 AA8 PRO A 185 ARG A 192 1 8
HELIX 9 AA9 GLY A 202 LEU A 204 5 3
HELIX 10 AB1 ASP A 210 ALA A 214 5 5
HELIX 11 AB2 SER A 215 LEU A 220 1 6
HELIX 12 AB3 GLY A 234 ASP A 253 1 20
HELIX 13 AB4 SER A 267 ASP A 280 1 14
HELIX 14 AB5 THR A 306 PHE A 314 1 9
HELIX 15 AB6 ALA A 319 ASP A 326 5 8
HELIX 16 AB7 HIS A 328 LEU A 332 5 5
HELIX 17 AB8 ASP A 335 LEU A 342 1 8
HELIX 18 AB9 ASP A 356 ALA A 359 5 4
HELIX 19 AC1 ASP A 360 PHE A 378 1 19
HELIX 20 AC2 THR A 411 LEU A 426 1 16
SHEET 1 AA1 9 VAL A 83 ALA A 93 0
SHEET 2 AA1 9 ALA A 98 ARG A 106 -1 O ARG A 106 N VAL A 83
SHEET 3 AA1 9 SER A 115 PRO A 123 -1 O LEU A 118 N VAL A 103
SHEET 4 AA1 9 ALA A 195 TYR A 200 -1 O VAL A 196 N TYR A 121
SHEET 5 AA1 9 ALA A 133 ASN A 140 1 N PHE A 136 O ALA A 197
SHEET 6 AA1 9 VAL A 256 HIS A 266 1 O ALA A 262 N LEU A 137
SHEET 7 AA1 9 LEU A 285 ASN A 289 1 O LEU A 285 N VAL A 263
SHEET 8 AA1 9 LEU A 348 ALA A 353 1 O TYR A 349 N SER A 288
SHEET 9 AA1 9 LEU A 399 ARG A 404 1 O ARG A 400 N VAL A 350
LINK O LEU A 250 NA NA A 507 1555 1555 2.46
LINK O ASP A 253 NA NA A 507 1555 1555 2.53
LINK O VAL A 256 NA NA A 507 1555 1555 2.65
LINK O HIS A 303 MG MG A 502 1555 1555 2.18
LINK O GLU A 305 MG MG A 502 1555 1555 2.25
LINK MG MG A 502 O HOH A 727 1555 1555 2.42
LINK MG MG A 502 O HOH A 605 1555 1555 2.63
LINK MG MG A 502 O HOH A 802 1555 1555 2.52
LINK MG MG A 502 O HOH A 722 1555 1555 2.18
LINK NA NA A 507 O HOH A 750 1555 1555 2.26
LINK NA NA A 507 O HOH A 778 1555 1555 2.49
CISPEP 1 ALA A 344 PRO A 345 0 0.68
SITE 1 AC1 12 SER A 267 ARG A 268 LYS A 271 GLU A 305
SITE 2 AC1 12 ILE A 310 PHE A 314 TRP A 358 HIS A 408
SITE 3 AC1 12 HOH A 655 HOH A 726 HOH A 768 HOH A 775
SITE 1 AC2 6 HIS A 303 GLU A 305 HOH A 605 HOH A 722
SITE 2 AC2 6 HOH A 727 HOH A 802
SITE 1 AC3 1 HOH A 606
SITE 1 AC4 3 GLU A 131 ASP A 226 PRO A 254
SITE 1 AC5 6 PRO A 75 LEU A 76 ALA A 92 LEU A 94
SITE 2 AC5 6 GLY A 95 HOH A 640
SITE 1 AC6 6 LEU A 250 GLU A 251 ASP A 253 VAL A 256
SITE 2 AC6 6 HOH A 750 HOH A 778
CRYST1 43.215 44.189 50.172 75.78 65.43 70.85 P 1 1
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 0.023140 -0.008037 -0.009638 0.00000
SCALE2 0.000000 0.023956 -0.003072 0.00000
SCALE3 0.000000 0.000000 0.022096 0.00000
TER 6102 PRO A 431
MASTER 349 0 7 20 9 0 11 6 3326 1 77 34
END |