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HEADER HYDROLASE 01-OCT-19 6SYV
TITLE THE GLUCURONOYL ESTERASE OTCE15A S267A VARIANT 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
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 6SYV 0
JRNL AUTH S.MAZURKEWICH,J.C.NAVARRO POULSEN,J.LARSBRINK,L.LO LEGGIO
JRNL TITL THE GLUCURONOYL ESTERASE OTCE15A S267A VARIANT FROM OPITUTUS
JRNL TITL 2 TERRAE IN COMPLEX WITH D-GLUCURONATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.12 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) : 1.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.7
REMARK 3 NUMBER OF REFLECTIONS : 102078
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.480
REMARK 3 FREE R VALUE TEST SET COUNT : 7637
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 36.2200 - 3.4800 0.97 3758 307 0.1261 0.1460
REMARK 3 2 3.4800 - 2.7600 0.93 3585 283 0.1313 0.1467
REMARK 3 3 2.7600 - 2.4100 0.95 3633 300 0.1359 0.1559
REMARK 3 4 2.4100 - 2.1900 0.96 3699 295 0.1370 0.1608
REMARK 3 5 2.1900 - 2.0400 0.95 3692 295 0.1380 0.1482
REMARK 3 6 2.0400 - 1.9200 0.95 3668 294 0.1454 0.1627
REMARK 3 7 1.9200 - 1.8200 0.95 3653 300 0.1459 0.1723
REMARK 3 8 1.8200 - 1.7400 0.95 3673 292 0.1582 0.1785
REMARK 3 9 1.7400 - 1.6700 0.96 3662 299 0.1586 0.1688
REMARK 3 10 1.6700 - 1.6200 0.96 3722 298 0.1577 0.1923
REMARK 3 11 1.6200 - 1.5600 0.95 3685 301 0.1652 0.2004
REMARK 3 12 1.5600 - 1.5200 0.95 3657 293 0.1672 0.1914
REMARK 3 13 1.5200 - 1.4800 0.95 3668 294 0.1724 0.1895
REMARK 3 14 1.4800 - 1.4400 0.95 3649 296 0.1924 0.2357
REMARK 3 15 1.4400 - 1.4100 0.94 3654 296 0.2207 0.2454
REMARK 3 16 1.4100 - 1.3800 0.94 3633 295 0.2298 0.2448
REMARK 3 17 1.3800 - 1.3500 0.93 3588 290 0.2390 0.2555
REMARK 3 18 1.3500 - 1.3300 0.94 3610 294 0.2548 0.2729
REMARK 3 19 1.3300 - 1.3000 0.93 3582 291 0.2674 0.3172
REMARK 3 20 1.3000 - 1.2800 0.93 3612 293 0.2974 0.2973
REMARK 3 21 1.2800 - 1.2600 0.91 3512 284 0.3030 0.3197
REMARK 3 22 1.2600 - 1.2400 0.75 2854 232 0.3135 0.3428
REMARK 3 23 1.2400 - 1.2200 0.66 2574 209 0.3118 0.3018
REMARK 3 24 1.2200 - 1.2100 0.60 2306 187 0.3138 0.3223
REMARK 3 25 1.2100 - 1.1900 0.54 2110 171 0.3295 0.3519
REMARK 3 26 1.1900 - 1.1700 0.47 1794 146 0.3206 0.3185
REMARK 3 27 1.1700 - 1.1600 0.46 1797 145 0.3383 0.3614
REMARK 3 28 1.1600 - 1.1500 0.41 1567 128 0.3779 0.4210
REMARK 3 29 1.1500 - 1.1300 0.39 1512 123 0.4052 0.4467
REMARK 3 30 1.1300 - 1.1200 0.34 1332 106 0.4380 0.4535
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.307
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.99
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 3435
REMARK 3 ANGLE : 1.186 4675
REMARK 3 CHIRALITY : 0.082 490
REMARK 3 PLANARITY : 0.009 623
REMARK 3 DIHEDRAL : 21.697 1252
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 6SYV 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_1292104587.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873127
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102117
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.120
REMARK 200 RESOLUTION RANGE LOW (A) : 36.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.7
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.08792
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 38.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 1.04400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.760
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 (%): 32.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ENZYME MIXED 50/50 WITH RESERVOIR
REMARK 280 SOLUTION CONTAINING MORPHEUS SCREEN SOLUTION G12: 0.1 M
REMARK 280 CARBOXYLIC ACIDS (0.2M SODIUM FORMATE; 0.2M AMMONIUM ACETATE;
REMARK 280 0.2M SODIUM CITRATE TRIBASIC DIHYDRATE; 0.2M SODIUM POTASSIUM
REMARK 280 TARTRATE TETRAHYDRATE; 0.2M SODIUM OXAMATE), 0.1 M BUFFER SYSTEM
REMARK 280 3 PH 8.5 (TRIS; BICINE), AND 50 % V/V PRECIPITANT MIX 4 (25% V/V
REMARK 280 MPD; 25% PEG 1000; 25% W/V PEG 3350)., VAPOR DIFFUSION, SITTING
REMARK 280 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: 3420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 27.0 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 12
REMARK 465 GLY A 13
REMARK 465 SER A 14
REMARK 465 SER A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 HIS A 21
REMARK 465 SER A 22
REMARK 465 SER A 23
REMARK 465 GLU A 24
REMARK 465 ASN A 25
REMARK 465 LEU A 26
REMARK 465 TYR A 27
REMARK 465 PHE A 28
REMARK 465 GLN A 29
REMARK 465 GLY A 30
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 50.71 -95.57
REMARK 500 ARG A 57 -55.51 -124.80
REMARK 500 ARG A 57 -57.64 -120.83
REMARK 500 VAL A 70 -70.25 -124.93
REMARK 500 ASP A 150 110.06 -28.65
REMARK 500 ALA A 224 110.36 -30.63
REMARK 500 ASP A 226 -138.94 -132.89
REMARK 500 ALA A 267 -129.86 60.91
REMARK 500 HIS A 328 43.97 -144.97
REMARK 500 ASP A 360 69.74 65.07
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 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 303 O
REMARK 620 2 GLU A 305 O 93.5
REMARK 620 3 HOH A 849 O 101.7 98.1
REMARK 620 4 HOH A 613 O 86.0 84.3 171.7
REMARK 620 5 HOH A 913 O 159.2 89.0 98.3 73.7
REMARK 620 6 HOH A 708 O 85.6 153.1 108.4 68.8 83.0
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 MG 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 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO 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
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GCU A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BDP A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 517
DBREF 6SYV A 33 432 UNP B1ZMF4 B1ZMF4_OPITP 33 432
SEQADV 6SYV MET A 12 UNP B1ZMF4 INITIATING METHIONINE
SEQADV 6SYV GLY A 13 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV SER A 14 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV SER A 15 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV HIS A 16 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV HIS A 17 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV HIS A 18 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV HIS A 19 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV HIS A 20 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV HIS A 21 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV SER A 22 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV SER A 23 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV GLU A 24 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV ASN A 25 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV LEU A 26 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV TYR A 27 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV PHE A 28 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV GLN A 29 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV GLY A 30 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV HIS A 31 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV SER A 32 UNP B1ZMF4 EXPRESSION TAG
SEQADV 6SYV ALA A 267 UNP B1ZMF4 SER 267 ENGINEERED MUTATION
SEQRES 1 A 421 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLU
SEQRES 2 A 421 ASN LEU TYR PHE GLN GLY HIS SER ALA TYR THR LEU PRO
SEQRES 3 A 421 ASP PRO LEU VAL GLY ALA ASP GLY THR ARG VAL HIS ASP
SEQRES 4 A 421 ARG ALA THR TRP GLN HIS ARG ARG ARG PRO GLU LEU LEU
SEQRES 5 A 421 GLN LEU PHE ALA ARG GLU VAL TYR GLY ARG THR PRO LEU
SEQRES 6 A 421 GLY ARG PRO GLU GLY MET VAL PHE LYS VAL THR THR MET
SEQRES 7 A 421 GLU HIS ALA ALA LEU GLY GLY ALA ALA THR ARG LYS GLU
SEQRES 8 A 421 VAL THR VAL ARG PHE GLY ARG ASP PRO ASN ALA PRO SER
SEQRES 9 A 421 MET GLN LEU LEU LEU TYR VAL PRO ASN ALA VAL ILE ALA
SEQRES 10 A 421 ARG ALA GLU ARG ALA PRO VAL PHE LEU GLY LEU ASN PHE
SEQRES 11 A 421 TYR GLY ASN HIS THR VAL HIS THR ASP PRO ALA ILE ALA
SEQRES 12 A 421 LEU SER ALA ARG TRP ILE PRO ALA GLU ALA PRO ASN GLY
SEQRES 13 A 421 ALA ASN HIS ARG ALA THR GLU ALA ALA ARG GLY SER ASP
SEQRES 14 A 421 ALA GLN LYS TRP PRO VAL GLU GLN ILE LEU ALA ARG GLY
SEQRES 15 A 421 TYR ALA VAL ALA THR VAL TYR CYS GLY ASP LEU CYS PRO
SEQRES 16 A 421 ASP ARG PRO ASP GLY LEU ASN ALA SER VAL ALA SER TRP
SEQRES 17 A 421 LEU ASP ALA ALA ALA GLY ASP GLN ARG ALA PRO ASP ALA
SEQRES 18 A 421 TRP GLY ALA ILE GLY VAL TRP ALA TRP GLY LEU SER ARG
SEQRES 19 A 421 ALA LEU ASP TYR LEU GLU THR ASP PRO LEU VAL ASP ALA
SEQRES 20 A 421 SER ARG VAL ALA VAL HIS GLY HIS ALA ARG LEU GLY LYS
SEQRES 21 A 421 ALA ALA LEU TRP ALA GLY ALA GLN ASP ASP ARG PHE ALA
SEQRES 22 A 421 LEU VAL ILE SER ASN GLU SER GLY CYS GLY GLY ALA ALA
SEQRES 23 A 421 LEU SER LYS ARG ILE HIS GLY GLU THR VAL ALA ARG ILE
SEQRES 24 A 421 ASN THR VAL PHE PRO HIS TRP PHE ALA ARG ASN PHE ARG
SEQRES 25 A 421 ARG TYR ASP ASP HIS GLU GLU ALA LEU PRO VAL ASP GLN
SEQRES 26 A 421 HIS GLU LEU LEU ALA LEU VAL ALA PRO ARG PRO LEU TYR
SEQRES 27 A 421 VAL ALA SER ALA GLU ASP ASP ASP TRP ALA ASP PRO ARG
SEQRES 28 A 421 GLY GLU PHE LEU ALA VAL LYS ALA ALA GLU PRO VAL PHE
SEQRES 29 A 421 ARG LEU PHE GLY GLN THR GLY PRO SER GLY GLU ASP VAL
SEQRES 30 A 421 PRO ARG VAL ASN GLU PRO SER GLY GLY ALA LEU ARG TYR
SEQRES 31 A 421 HIS ILE ARG PRO GLY PRO HIS GLY MET THR ALA GLN ASP
SEQRES 32 A 421 TRP ALA PHE TYR LEU ALA PHE ALA ASP GLU TRP LEU LYS
SEQRES 33 A 421 SER ALA LEU PRO ALA
HET MG A 501 1
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 EDO A 509 10
HET EDO A 510 10
HET EDO A 511 10
HET EDO A 512 10
HET GCU A 513 22
HET BDP A 514 22
HET PEG A 515 34
HET PEG A 516 17
HET PEG A 517 17
HETNAM MG MAGNESIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GCU D-GLUCURONIC ACID
HETNAM BDP BETA-D-GLUCOPYRANURONIC ACID
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
HETSYN BDP D-GLUCURONIC ACID
FORMUL 2 MG MG 2+
FORMUL 3 EDO 11(C2 H6 O2)
FORMUL 14 GCU C6 H10 O7
FORMUL 15 BDP C6 H10 O7
FORMUL 16 PEG 3(C4 H10 O3)
FORMUL 19 HOH *368(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 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 GLU A 251 1 18
HELIX 13 AB4 ALA A 267 ASP A 280 1 14
HELIX 14 AB5 LEU A 298 ILE A 302 5 5
HELIX 15 AB6 THR A 306 PHE A 314 1 9
HELIX 16 AB7 ALA A 319 ASP A 326 5 8
HELIX 17 AB8 HIS A 328 LEU A 332 5 5
HELIX 18 AB9 ASP A 335 LEU A 342 1 8
HELIX 19 AC1 ASP A 356 ALA A 359 5 4
HELIX 20 AC2 ASP A 360 PHE A 378 1 19
HELIX 21 AC3 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 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 ASN A 289 N GLY A 265
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 HIS A 303 MG MG A 501 1555 1555 2.28
LINK O GLU A 305 MG MG A 501 1555 1555 2.20
LINK MG MG A 501 O HOH A 849 1555 1555 2.38
LINK MG MG A 501 O HOH A 613 1555 1555 2.59
LINK MG MG A 501 O HOH A 913 1555 1555 2.45
LINK MG MG A 501 O HOH A 708 1555 1555 2.42
CISPEP 1 ALA A 344 PRO A 345 0 5.65
SITE 1 AC1 6 HIS A 303 GLU A 305 HOH A 613 HOH A 708
SITE 2 AC1 6 HOH A 849 HOH A 913
SITE 1 AC2 3 PRO A 114 SER A 115 ARG A 158
SITE 1 AC3 8 ARG A 51 ASP A 110 PRO A 111 ASP A 355
SITE 2 AC3 8 ASP A 357 TRP A 358 HOH A 698 HOH A 853
SITE 1 AC4 2 ALA A 43 GLN A 413
SITE 1 AC5 4 LEU A 76 PRO A 79 GLU A 80 HOH A 637
SITE 1 AC6 3 LEU A 36 ASP A 38 HOH A 726
SITE 1 AC7 4 ARG A 57 ALA A 191 ARG A 192 THR A 312
SITE 1 AC8 4 ARG A 192 TYR A 194 ARG A 260 LEU A 426
SITE 1 AC9 6 TRP A 358 HIS A 408 GCU A 513 HOH A 698
SITE 2 AC9 6 HOH A 727 HOH A 771
SITE 1 AD1 2 ALA A 43 GLN A 413
SITE 1 AD2 3 PRO A 345 GLN A 380 TRP A 425
SITE 1 AD3 2 ALA A 130 HOH A 642
SITE 1 AD4 12 ALA A 267 ARG A 268 LYS A 271 GLU A 305
SITE 2 AD4 12 PHE A 314 TRP A 358 HIS A 408 EDO A 509
SITE 3 AD4 12 BDP A 514 HOH A 663 HOH A 771 HOH A 785
SITE 1 AD5 13 ALA A 267 ARG A 268 LYS A 271 GLU A 305
SITE 2 AD5 13 ILE A 310 PHE A 314 TRP A 317 TRP A 358
SITE 3 AD5 13 HIS A 408 GCU A 513 HOH A 663 HOH A 771
SITE 4 AD5 13 HOH A 785
SITE 1 AD6 8 LEU A 212 ASN A 213 SER A 218 ASP A 226
SITE 2 AD6 8 ARG A 228 HOH A 664 HOH A 717 HOH A 723
SITE 1 AD7 1 THR A 312
SITE 1 AD8 5 SER A 32 TYR A 34 THR A 35 LEU A 36
SITE 2 AD8 5 HOH A 877
CRYST1 43.507 44.497 50.367 76.43 66.96 70.22 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 0.022985 -0.008267 -0.008861 0.00000
SCALE2 0.000000 0.023883 -0.002837 0.00000
SCALE3 0.000000 0.000000 0.021726 0.00000
TER 6338 ALA A 432
MASTER 352 0 17 21 9 0 27 6 3566 1 230 33
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