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HEADER HYDROLASE 12-JUN-18 6GRW
TITLE GLUCURONOYL ESTERASE FROM OPITUTUS TERRAE (AU DERIVATIVE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ACETYL XYLAN ESTERASE;
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CARBOHYDRATE ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.LO LEGGIO,J.LARSBRINK,R.MELAND KNUDSEN,S.MAZURKEWICH,J.C.NAVARRO
AUTHOR 2 POULSEN
REVDAT 1 15-AUG-18 6GRW 0
JRNL AUTH J.ARNLING BAATH,S.MAZURKEWICH,R.M.KNUDSEN,J.N.POULSEN,
JRNL AUTH 2 L.OLSSON,L.LO LEGGIO,J.LARSBRINK
JRNL TITL BIOCHEMICAL AND STRUCTURAL FEATURES OF DIVERSE BACTERIAL
JRNL TITL 2 GLUCURONOYL ESTERASES FACILITATING RECALCITRANT BIOMASS
JRNL TITL 3 CONVERSION.
JRNL REF BIOTECHNOL BIOFUELS V. 11 213 2018
JRNL REFN ESSN 1754-6834
JRNL PMID 30083226
JRNL DOI 10.1186/S13068-018-1213-X
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 50799
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.136
REMARK 3 R VALUE (WORKING SET) : 0.135
REMARK 3 FREE R VALUE : 0.159
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.140
REMARK 3 FREE R VALUE TEST SET COUNT : 2101
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 46.2900 - 3.7000 0.98 3324 144 0.1319 0.1405
REMARK 3 2 3.7000 - 2.9300 0.98 3309 142 0.1244 0.1503
REMARK 3 3 2.9300 - 2.5600 0.98 3311 143 0.1260 0.1439
REMARK 3 4 2.5600 - 2.3300 0.97 3291 142 0.1245 0.1570
REMARK 3 5 2.3300 - 2.1600 0.98 3321 143 0.1267 0.1410
REMARK 3 6 2.1600 - 2.0300 0.97 3258 141 0.1307 0.1590
REMARK 3 7 2.0300 - 1.9300 0.96 3266 141 0.1346 0.1777
REMARK 3 8 1.9300 - 1.8500 0.96 3246 140 0.1411 0.1838
REMARK 3 9 1.8500 - 1.7800 0.96 3242 140 0.1394 0.1660
REMARK 3 10 1.7800 - 1.7200 0.96 3223 139 0.1419 0.1657
REMARK 3 11 1.7200 - 1.6600 0.95 3228 139 0.1501 0.1786
REMARK 3 12 1.6600 - 1.6100 0.95 3217 139 0.1556 0.2002
REMARK 3 13 1.6100 - 1.5700 0.95 3205 138 0.1655 0.1797
REMARK 3 14 1.5700 - 1.5300 0.95 3162 136 0.1747 0.2246
REMARK 3 15 1.5300 - 1.5000 0.92 3095 134 0.1980 0.2402
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.074
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.16
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 : 0.008 3293
REMARK 3 ANGLE : 1.093 4504
REMARK 3 CHIRALITY : 0.076 471
REMARK 3 PLANARITY : 0.009 603
REMARK 3 DIHEDRAL : 17.594 1208
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 6GRW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1200010018.
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) : 100
REMARK 200 PH : 8.0
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) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS BUILT=20180126
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50802
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 46.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 3.550
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.31400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.13_2998
REMARK 200 STARTING MODEL: STRUCTURE UNDER DEPOSITION
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR COMPOSITION FOR CRYSTAL
REMARK 280 GROWTH: 0.03M MAGNESIUM CHLORIDE, 0.03 M CALCIUM CHLORIDE, 0.05M
REMARK 280 IMIDAZOLE, 0.05M MES, 10% V/V MPD, 10% W/V PEG 1000, 10% V/W PEG
REMARK 280 3500P. HEAVY ATOM DERIVATIZATION: 1.2UL CRYSTALLIZATION MOTHER
REMARK 280 LIQUOR CONTAINING 0.5MM KAU(CN)2 ADDED TO DROP CONTAINING
REMARK 280 CRYSTALS. DROP SIZE AND COMPOSITION: SITTING DROPS OF 0.4UL WERE
REMARK 280 MIXED IN A PROTEIN:RESERVOIR VOLUME RATIO OF 1:1 USING 45 MG/ML
REMARK 280 OF OTCE15A IN 20 MM TRIS PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.15K
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: 1630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 GLY A -2
REMARK 465 HIS A -1
REMARK 465 ASP A 221
REMARK 465 ALA A 222
REMARK 465 ALA A 223
REMARK 465 ALA A 432
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 HD1 HIS A 148 H ASP A 150 1.31
REMARK 500 OE1 GLN A 64 HH12 ARG A 73 1.59
REMARK 500 O PRO A 431 O HOH A 601 1.65
REMARK 500 O HOH A 927 O HOH A 972 1.85
REMARK 500 O HOH A 604 O HOH A 927 2.09
REMARK 500 O HOH A 935 O HOH A 994 2.15
REMARK 500 O2 EDO A 508 O HOH A 602 2.19
REMARK 500 O PRO A 206 O HOH A 603 2.19
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 33 62.04 -103.99
REMARK 500 VAL A 70 -73.43 -120.99
REMARK 500 ASP A 150 108.21 -25.42
REMARK 500 SER A 267 -128.53 56.78
REMARK 500 HIS A 328 41.70 -144.44
REMARK 500 ASP A 360 73.94 67.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 430 PRO A 431 122.42
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 AU A 501 AU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 293 SG
REMARK 620 2 HOH A 902 O 100.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AU A 502 AU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 293 SG
REMARK 620 2 GLY A 294 N 89.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 303 O
REMARK 620 2 GLU A 305 O 95.0
REMARK 620 3 HOH A 829 O 100.1 91.9
REMARK 620 4 HOH A 616 O 86.8 85.6 172.8
REMARK 620 5 HOH A 636 O 89.8 160.8 105.5 76.1
REMARK 620 6 HOH A 902 O 167.7 95.5 85.9 87.6 78.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 505 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 953 O
REMARK 620 2 HOH A 614 O 164.3
REMARK 620 3 HOH A 676 O 73.1 96.2
REMARK 620 4 HOH A 717 O 102.5 85.1 165.9
REMARK 620 5 HOH A 916 O 82.0 87.2 92.8 73.2
REMARK 620 6 HOH A 964 O 94.2 98.6 97.4 96.3 167.6
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 AU A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AU A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 511
DBREF 6GRW A 33 432 UNP B1ZMF4 B1ZMF4_OPITP 33 432
SEQADV 6GRW GLY A -2 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6GRW HIS A -1 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6GRW SER A 0 UNP B1ZMF4 EXPRESSION TAG
SEQRES 1 A 403 GLY HIS SER ALA TYR THR LEU PRO ASP PRO LEU VAL GLY
SEQRES 2 A 403 ALA ASP GLY THR ARG VAL HIS ASP ARG ALA THR TRP GLN
SEQRES 3 A 403 HIS ARG ARG ARG PRO GLU LEU LEU GLN LEU PHE ALA ARG
SEQRES 4 A 403 GLU VAL TYR GLY ARG THR PRO LEU GLY ARG PRO GLU GLY
SEQRES 5 A 403 MET VAL PHE LYS VAL THR THR MET GLU HIS ALA ALA LEU
SEQRES 6 A 403 GLY GLY ALA ALA THR ARG LYS GLU VAL THR VAL ARG PHE
SEQRES 7 A 403 GLY ARG ASP PRO ASN ALA PRO SER MET GLN LEU LEU LEU
SEQRES 8 A 403 TYR VAL PRO ASN ALA VAL ILE ALA ARG ALA GLU ARG ALA
SEQRES 9 A 403 PRO VAL PHE LEU GLY LEU ASN PHE TYR GLY ASN HIS THR
SEQRES 10 A 403 VAL HIS THR ASP PRO ALA ILE ALA LEU SER ALA ARG TRP
SEQRES 11 A 403 ILE PRO ALA GLU ALA PRO ASN GLY ALA ASN HIS ARG ALA
SEQRES 12 A 403 THR GLU ALA ALA ARG GLY SER ASP ALA GLN LYS TRP PRO
SEQRES 13 A 403 VAL GLU GLN ILE LEU ALA ARG GLY TYR ALA VAL ALA THR
SEQRES 14 A 403 VAL TYR CYS GLY ASP LEU CYS PRO ASP ARG PRO ASP GLY
SEQRES 15 A 403 LEU ASN ALA SER VAL ALA SER TRP LEU ASP ALA ALA ALA
SEQRES 16 A 403 GLY ASP GLN ARG ALA PRO ASP ALA TRP GLY ALA ILE GLY
SEQRES 17 A 403 VAL TRP ALA TRP GLY LEU SER ARG ALA LEU ASP TYR LEU
SEQRES 18 A 403 GLU THR ASP PRO LEU VAL ASP ALA SER ARG VAL ALA VAL
SEQRES 19 A 403 HIS GLY HIS SER ARG LEU GLY LYS ALA ALA LEU TRP ALA
SEQRES 20 A 403 GLY ALA GLN ASP ASP ARG PHE ALA LEU VAL ILE SER ASN
SEQRES 21 A 403 GLU SER GLY CYS GLY GLY ALA ALA LEU SER LYS ARG ILE
SEQRES 22 A 403 HIS GLY GLU THR VAL ALA ARG ILE ASN THR VAL PHE PRO
SEQRES 23 A 403 HIS TRP PHE ALA ARG ASN PHE ARG ARG TYR ASP ASP HIS
SEQRES 24 A 403 GLU GLU ALA LEU PRO VAL ASP GLN HIS GLU LEU LEU ALA
SEQRES 25 A 403 LEU VAL ALA PRO ARG PRO LEU TYR VAL ALA SER ALA GLU
SEQRES 26 A 403 ASP ASP ASP TRP ALA ASP PRO ARG GLY GLU PHE LEU ALA
SEQRES 27 A 403 VAL LYS ALA ALA GLU PRO VAL PHE ARG LEU PHE GLY GLN
SEQRES 28 A 403 THR GLY PRO SER GLY GLU ASP VAL PRO ARG VAL ASN GLU
SEQRES 29 A 403 PRO SER GLY GLY ALA LEU ARG TYR HIS ILE ARG PRO GLY
SEQRES 30 A 403 PRO HIS GLY MET THR ALA GLN ASP TRP ALA PHE TYR LEU
SEQRES 31 A 403 ALA PHE ALA ASP GLU TRP LEU LYS SER ALA LEU PRO ALA
HET AU A 501 1
HET AU A 502 1
HET CA A 503 1
HET MG A 504 1
HET MG A 505 1
HET MPD A 506 22
HET EDO A 507 10
HET EDO A 508 10
HET EDO A 509 10
HET EDO A 510 10
HET EDO A 511 10
HETNAM AU GOLD ION
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 AU 2(AU 1+)
FORMUL 4 CA CA 2+
FORMUL 5 MG 2(MG 2+)
FORMUL 7 MPD C6 H14 O2
FORMUL 8 EDO 5(C2 H6 O2)
FORMUL 13 HOH *402(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 ARG A 129 1 6
HELIX 5 AA5 GLY A 143 VAL A 147 5 5
HELIX 6 AA6 GLU A 174 ARG A 177 5 4
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 GLU A 251 1 18
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 THR A 104 N LYS A 85
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 THR A 198 N LEU A 119
SHEET 5 AA1 9 ALA A 133 ASN A 140 1 N PRO A 134 O ALA A 195
SHEET 6 AA1 9 VAL A 256 HIS A 266 1 O ALA A 262 N VAL A 135
SHEET 7 AA1 9 LEU A 285 ASN A 289 1 O ILE A 287 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
SHEET 1 AA2 2 GLY A 167 ALA A 168 0
SHEET 2 AA2 2 ARG A 171 ALA A 172 -1 O ARG A 171 N ALA A 168
LINK SG CYS A 293 AU AU A 501 1555 1555 2.25
LINK SG CYS A 293 AU AU A 502 1555 1555 2.44
LINK N GLY A 294 AU AU A 502 1555 1555 2.72
LINK O HIS A 303 CA CA A 503 1555 1555 2.26
LINK O GLU A 305 CA CA A 503 1555 1555 2.37
LINK AU AU A 501 O HOH A 902 1555 1555 2.48
LINK CA CA A 503 O HOH A 829 1555 1555 2.40
LINK CA CA A 503 O HOH A 616 1555 1555 2.32
LINK CA CA A 503 O HOH A 636 1555 1555 2.34
LINK CA CA A 503 O HOH A 902 1555 1555 2.38
LINK MG MG A 504 O HOH A 852 1555 1555 2.64
LINK MG MG A 505 O HOH A 953 1555 1555 2.66
LINK MG MG A 505 O HOH A 614 1555 1655 2.02
LINK MG MG A 505 O HOH A 676 1555 1655 2.11
LINK MG MG A 505 O HOH A 717 1555 1655 2.08
LINK MG MG A 505 O HOH A 916 1555 1655 2.30
LINK MG MG A 505 O HOH A 964 1555 1655 2.07
CISPEP 1 ALA A 344 PRO A 345 0 5.06
SITE 1 AC1 8 CYS A 293 GLU A 305 THR A 306 VAL A 307
SITE 2 AC1 8 AU A 502 CA A 503 HOH A 756 HOH A 902
SITE 1 AC2 6 CYS A 293 GLY A 294 SER A 299 PHE A 322
SITE 2 AC2 6 AU A 501 HOH A 655
SITE 1 AC3 7 HIS A 303 GLU A 305 AU A 501 HOH A 616
SITE 2 AC3 7 HOH A 636 HOH A 829 HOH A 902
SITE 1 AC4 3 LEU A 94 GLY A 95 HOH A 852
SITE 1 AC5 6 HOH A 614 HOH A 676 HOH A 717 HOH A 916
SITE 2 AC5 6 HOH A 953 HOH A 964
SITE 1 AC6 5 VAL A 41 GLY A 42 ALA A 43 GLN A 413
SITE 2 AC6 5 HOH A 719
SITE 1 AC7 6 GLY A 81 ARG A 109 ARG A 362 ASP A 387
SITE 2 AC7 6 VAL A 388 HOH A 723
SITE 1 AC8 5 ARG A 158 TRP A 159 PRO A 206 HOH A 602
SITE 2 AC8 5 HOH A 832
SITE 1 AC9 5 ALA A 284 LYS A 427 EDO A 510 HOH A 621
SITE 2 AC9 5 HOH A 662
SITE 1 AD1 6 SER A 259 ARG A 282 LYS A 427 EDO A 509
SITE 2 AD1 6 HOH A 662 HOH A 797
SITE 1 AD2 4 ALA A 130 ASP A 226 GLN A 227 HOH A 619
CRYST1 43.693 44.608 50.558 76.57 67.17 70.65 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 0.022887 -0.008038 -0.008738 0.00000
SCALE2 0.000000 0.023760 -0.002852 0.00000
SCALE3 0.000000 0.000000 0.021614 0.00000
TER 6250 PRO A 431
MASTER 351 0 11 20 11 0 20 6 3508 1 88 31
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