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HEADER HYDROLASE 12-OCT-17 6EQD
TITLE CRYSTAL STRUCTURE OF A POLYETHYLENE TEREPHTHALATE DEGRADING HYDROLASE
TITLE 2 FROM IDEONELLA SAKAIENSIS COLLECTED AT LONG WAVELENGTH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: PETASE;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C41;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PETASE, PET DEGRADATION, A/B HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.P.AUSTIN,M.D.ALLEN,C.W.JOHNSON,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 25-APR-18 6EQD 0
JRNL AUTH H.P.AUSTIN,M.D.ALLEN,B.DONOHOE,N.RORRER,F.KEARNS,R.SILVEIRA,
JRNL AUTH 2 B.POLLARD,G.DOMINICK,R.DUMAN,K.EL OMARI,V.MYKHAYLYK,
JRNL AUTH 3 A.WAGNER,W.MICHENER,A.AMORE,M.SKAF,M.CROWLEY,A.THORNE,
JRNL AUTH 4 C.JOHNSON,H.WOODCOCK,J.MCGEEHAN,G.T.BECKHAM
JRNL TITL CHARACTERIZATION AND ENGINEERING OF A PLASTIC-DEGRADING
JRNL TITL 2 AROMATIC POLYESTERASE
JRNL REF PROC.NATL.ACAD.SCI.USA 2018
JRNL REFN ESSN 1091-6490
JRNL DOI 10.1073/PNAS.1718804115
REMARK 2
REMARK 2 RESOLUTION. 1.70 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.9
REMARK 3 NUMBER OF REFLECTIONS : 95093
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4660
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 67.3774 - 5.2815 1.00 3800 202 0.1811 0.1625
REMARK 3 2 5.2815 - 4.1923 1.00 3693 171 0.1437 0.1562
REMARK 3 3 4.1923 - 3.6624 1.00 3592 202 0.1459 0.1474
REMARK 3 4 3.6624 - 3.3275 1.00 3582 193 0.1692 0.1922
REMARK 3 5 3.3275 - 3.0890 0.99 3542 182 0.1873 0.2170
REMARK 3 6 3.0890 - 2.9069 0.97 3468 191 0.1954 0.2237
REMARK 3 7 2.9069 - 2.7613 0.95 3354 199 0.1977 0.2461
REMARK 3 8 2.7613 - 2.6411 0.93 3302 180 0.2068 0.2517
REMARK 3 9 2.6411 - 2.5394 0.91 3202 182 0.2049 0.2241
REMARK 3 10 2.5394 - 2.4518 0.89 3174 157 0.2022 0.2361
REMARK 3 11 2.4518 - 2.3751 0.87 3096 159 0.2049 0.2262
REMARK 3 12 2.3751 - 2.3073 0.87 3058 162 0.2042 0.2046
REMARK 3 13 2.3073 - 2.2465 0.85 3015 149 0.2072 0.2213
REMARK 3 14 2.2465 - 2.1917 0.84 2939 133 0.2074 0.2489
REMARK 3 15 2.1917 - 2.1419 0.84 3009 136 0.2156 0.2693
REMARK 3 16 2.1419 - 2.0963 0.81 2853 141 0.2160 0.2306
REMARK 3 17 2.0963 - 2.0543 0.81 2894 143 0.2230 0.2649
REMARK 3 18 2.0543 - 2.0156 0.80 2807 141 0.2208 0.2480
REMARK 3 19 2.0156 - 1.9796 0.79 2817 144 0.2283 0.2718
REMARK 3 20 1.9796 - 1.9460 0.79 2752 150 0.2256 0.2316
REMARK 3 21 1.9460 - 1.9146 0.78 2750 139 0.2305 0.2583
REMARK 3 22 1.9146 - 1.8852 0.78 2715 140 0.2354 0.2623
REMARK 3 23 1.8852 - 1.8574 0.77 2727 146 0.2410 0.2589
REMARK 3 24 1.8574 - 1.8313 0.76 2668 159 0.2402 0.2752
REMARK 3 25 1.8313 - 1.8065 0.75 2625 125 0.2481 0.2771
REMARK 3 26 1.8065 - 1.7831 0.75 2660 136 0.2553 0.2970
REMARK 3 27 1.7831 - 1.7608 0.75 2609 127 0.2642 0.3094
REMARK 3 28 1.7608 - 1.7396 0.74 2626 125 0.3135 0.3825
REMARK 3 29 1.7396 - 1.7193 0.74 2618 125 0.3397 0.3500
REMARK 3 30 1.7193 - 1.7000 0.71 2486 121 0.3505 0.3947
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.002 5949
REMARK 3 ANGLE : 0.528 8109
REMARK 3 CHIRALITY : 0.044 895
REMARK 3 PLANARITY : 0.004 1070
REMARK 3 DIHEDRAL : 2.771 3540
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 6EQD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1200007044.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I23
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 2.4551
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 12M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95250
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 82.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.3
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.1
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 0.95200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MIB (MALONATE, IMIDAZOLE, BORATE)
REMARK 280 25% PEG1500, PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.26450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.26450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 26.27800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 117.15550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.27800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 117.15550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 82.26450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.27800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 117.15550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.26450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.27800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 117.15550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 461 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 573 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 MET A 1
REMARK 465 ASN A 2
REMARK 465 PHE A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 ARG A 8
REMARK 465 LEU A 9
REMARK 465 MET A 10
REMARK 465 GLN A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 VAL A 14
REMARK 465 LEU A 15
REMARK 465 GLY A 16
REMARK 465 GLY A 17
REMARK 465 LEU A 18
REMARK 465 MET A 19
REMARK 465 ALA A 20
REMARK 465 VAL A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 THR A 26
REMARK 465 ALA A 27
REMARK 465 GLN A 28
REMARK 465 GLU A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 PHE B 3
REMARK 465 PRO B 4
REMARK 465 ARG B 5
REMARK 465 ALA B 6
REMARK 465 SER B 7
REMARK 465 ARG B 8
REMARK 465 LEU B 9
REMARK 465 MET B 10
REMARK 465 GLN B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 VAL B 14
REMARK 465 LEU B 15
REMARK 465 GLY B 16
REMARK 465 GLY B 17
REMARK 465 LEU B 18
REMARK 465 MET B 19
REMARK 465 ALA B 20
REMARK 465 VAL B 21
REMARK 465 SER B 22
REMARK 465 ALA B 23
REMARK 465 ALA B 24
REMARK 465 ALA B 25
REMARK 465 THR B 26
REMARK 465 ALA B 27
REMARK 465 GLN B 28
REMARK 465 HIS B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 PHE C 3
REMARK 465 PRO C 4
REMARK 465 ARG C 5
REMARK 465 ALA C 6
REMARK 465 SER C 7
REMARK 465 ARG C 8
REMARK 465 LEU C 9
REMARK 465 MET C 10
REMARK 465 GLN C 11
REMARK 465 ALA C 12
REMARK 465 ALA C 13
REMARK 465 VAL C 14
REMARK 465 LEU C 15
REMARK 465 GLY C 16
REMARK 465 GLY C 17
REMARK 465 LEU C 18
REMARK 465 MET C 19
REMARK 465 ALA C 20
REMARK 465 VAL C 21
REMARK 465 SER C 22
REMARK 465 ALA C 23
REMARK 465 ALA C 24
REMARK 465 ALA C 25
REMARK 465 THR C 26
REMARK 465 ALA C 27
REMARK 465 GLN C 28
REMARK 465 GLU C 292
REMARK 465 HIS C 293
REMARK 465 HIS C 294
REMARK 465 HIS C 295
REMARK 465 HIS C 296
REMARK 465 HIS C 297
REMARK 465 HIS C 298
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 O HOH B 590 O HOH B 607 1.87
REMARK 500 O HOH B 587 O HOH B 627 1.89
REMARK 500 O HOH B 548 O HOH B 621 1.92
REMARK 500 O HOH B 608 O HOH B 615 1.92
REMARK 500 O HOH B 682 O HOH B 683 1.97
REMARK 500 O HOH C 550 O HOH C 613 2.04
REMARK 500 O HOH A 438 O HOH A 474 2.05
REMARK 500 O HOH B 561 O HOH B 625 2.06
REMARK 500 O HOH B 573 O HOH B 609 2.06
REMARK 500 O HOH B 569 O HOH B 603 2.07
REMARK 500 O HOH C 560 O HOH C 620 2.07
REMARK 500 O HOH B 531 O HOH B 693 2.08
REMARK 500 O HOH B 622 O HOH B 629 2.10
REMARK 500 O HOH A 462 O HOH A 521 2.10
REMARK 500 O HOH C 506 O HOH C 587 2.12
REMARK 500 O HOH B 598 O HOH B 611 2.12
REMARK 500 O HOH A 333 O HOH A 516 2.12
REMARK 500 O HOH B 599 O HOH B 640 2.12
REMARK 500 N ARG C 59 O HOH C 401 2.13
REMARK 500 O HOH B 583 O HOH B 674 2.14
REMARK 500 O HOH B 408 O HOH B 657 2.14
REMARK 500 O HOH A 453 O HOH A 495 2.15
REMARK 500 NH1 ARG C 53 O HOH C 402 2.15
REMARK 500 O HOH C 590 O HOH C 616 2.16
REMARK 500 O HOH C 521 O HOH C 549 2.16
REMARK 500 O GLY A 48 O HOH A 301 2.18
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 O HOH C 548 O HOH C 548 3556 2.06
REMARK 500 O HOH B 584 O HOH C 627 5555 2.17
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 SER A 160 -118.27 61.67
REMARK 500 SER A 214 -86.00 -134.66
REMARK 500 THR B 88 -0.53 69.63
REMARK 500 SER B 160 -119.96 62.68
REMARK 500 SER B 214 -85.23 -130.38
REMARK 500 THR C 88 -3.57 68.46
REMARK 500 SER C 160 -120.94 60.71
REMARK 500 ALA C 183 54.10 39.40
REMARK 500 SER C 214 -84.54 -129.48
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 CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 301
DBREF1 6EQD A 1 290 UNP PETH_IDESA
DBREF2 6EQD A A0A0K8P6T7 1 290
DBREF1 6EQD B 1 290 UNP PETH_IDESA
DBREF2 6EQD B A0A0K8P6T7 1 290
DBREF1 6EQD C 1 290 UNP PETH_IDESA
DBREF2 6EQD C A0A0K8P6T7 1 290
SEQADV 6EQD LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD LEU B 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD GLU B 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS B 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS B 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS B 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS B 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS B 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS B 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD LEU C 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD GLU C 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS C 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS C 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS C 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS C 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS C 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQD HIS C 298 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 A 298 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 A 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 A 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 A 298 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 A 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 A 298 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 A 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 A 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 A 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 A 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 A 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 A 298 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 A 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 A 298 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 A 298 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 A 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 A 298 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 A 298 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 A 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 A 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 A 298 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 A 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 B 298 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 B 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 B 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 B 298 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 B 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 B 298 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 B 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 B 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 B 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 B 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 B 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 B 298 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 B 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 B 298 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 B 298 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 B 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 B 298 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 B 298 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 B 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 B 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 B 298 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 B 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 C 298 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 C 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 C 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 C 298 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 C 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 C 298 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 C 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 C 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 C 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 C 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 C 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 C 298 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 C 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 C 298 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 C 298 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 C 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 C 298 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 C 298 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 C 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 C 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 C 298 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 C 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
HET CL B 301 1
HET CL C 301 1
HETNAM CL CHLORIDE ION
FORMUL 4 CL 2(CL 1-)
FORMUL 6 HOH *812(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 PRO A 210 SER A 213 5 4
HELIX 7 AA7 SER A 214 MET A 222 1 9
HELIX 8 AA8 ASN A 246 ASP A 263 1 18
HELIX 9 AA9 ASP A 265 ARG A 267 5 3
HELIX 10 AB1 TYR A 268 GLU A 274 1 7
HELIX 11 AB2 THR B 39 ALA B 45 1 7
HELIX 12 AB3 ARG B 90 LYS B 95 5 6
HELIX 13 AB4 TRP B 96 SER B 103 1 8
HELIX 14 AB5 GLN B 119 GLY B 139 1 21
HELIX 15 AB6 SER B 160 ASN B 173 1 14
HELIX 16 AB7 SER B 214 MET B 222 1 9
HELIX 17 AB8 ASN B 246 ASP B 263 1 18
HELIX 18 AB9 ASP B 265 ARG B 267 5 3
HELIX 19 AC1 TYR B 268 GLU B 274 1 7
HELIX 20 AC2 THR C 39 ALA C 45 1 7
HELIX 21 AC3 ARG C 90 LYS C 95 5 6
HELIX 22 AC4 TRP C 96 SER C 103 1 8
HELIX 23 AC5 GLN C 119 GLY C 139 1 21
HELIX 24 AC6 SER C 160 ASN C 173 1 14
HELIX 25 AC7 PRO C 210 SER C 213 5 4
HELIX 26 AC8 SER C 214 MET C 222 1 9
HELIX 27 AC9 ASN C 246 ASP C 263 1 18
HELIX 28 AD1 ASP C 265 ARG C 267 5 3
HELIX 29 AD2 TYR C 268 GLU C 274 1 7
SHEET 1 AA1 6 VAL A 52 THR A 56 0
SHEET 2 AA1 6 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 6 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 6 VAL A 78 VAL A 84 1 N ILE A 81 O ILE A 109
SHEET 5 AA1 6 VAL A 149 TRP A 159 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 6 ALA A 178 GLN A 182 1 O GLN A 182 N GLY A 158
SHEET 1 AA2 3 THR A 198 CYS A 203 0
SHEET 2 AA2 3 LYS A 227 ILE A 232 1 O ILE A 232 N ALA A 202
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ARG A 285 N PHE A 229
SHEET 1 AA3 6 VAL B 52 THR B 56 0
SHEET 2 AA3 6 ALA B 65 PRO B 71 -1 O VAL B 68 N PHE B 55
SHEET 3 AA3 6 VAL B 107 ASP B 112 -1 O VAL B 108 N TYR B 69
SHEET 4 AA3 6 VAL B 78 VAL B 84 1 N ILE B 81 O ILE B 109
SHEET 5 AA3 6 VAL B 149 TRP B 159 1 O ASP B 150 N VAL B 78
SHEET 6 AA3 6 ALA B 178 GLN B 182 1 O GLN B 182 N GLY B 158
SHEET 1 AA4 3 THR B 198 CYS B 203 0
SHEET 2 AA4 3 LYS B 227 ILE B 232 1 O LEU B 230 N ALA B 202
SHEET 3 AA4 3 VAL B 281 ALA B 287 -1 O ARG B 285 N PHE B 229
SHEET 1 AA5 6 VAL C 52 THR C 56 0
SHEET 2 AA5 6 ALA C 65 PRO C 71 -1 O VAL C 68 N PHE C 55
SHEET 3 AA5 6 VAL C 107 ASP C 112 -1 O VAL C 108 N TYR C 69
SHEET 4 AA5 6 VAL C 78 VAL C 84 1 N ILE C 81 O ILE C 109
SHEET 5 AA5 6 VAL C 149 TRP C 159 1 O ASP C 150 N VAL C 78
SHEET 6 AA5 6 ALA C 178 GLN C 182 1 O GLN C 182 N GLY C 158
SHEET 1 AA6 3 THR C 198 CYS C 203 0
SHEET 2 AA6 3 LYS C 227 ILE C 232 1 O ILE C 232 N ALA C 202
SHEET 3 AA6 3 VAL C 281 ALA C 287 -1 O ARG C 285 N PHE C 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.04
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.03
SSBOND 3 CYS B 203 CYS B 239 1555 1555 2.04
SSBOND 4 CYS B 273 CYS B 289 1555 1555 2.03
SSBOND 5 CYS C 203 CYS C 239 1555 1555 2.03
SSBOND 6 CYS C 273 CYS C 289 1555 1555 2.03
SITE 1 AC1 2 SER B 175 HOH B 624
SITE 1 AC2 3 HOH C 412 HOH C 610 HOH C 639
CRYST1 52.556 234.311 164.529 90.00 90.00 90.00 C 2 2 21 24
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 0.019028 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004268 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006078 0.00000
TER 1934 LEU A 291
TER 3877 GLU B 292
TER 5811 LEU C 291
MASTER 463 0 2 29 27 0 2 6 6622 3 12 69
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