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HEADER HYDROLASE 12-OCT-17 6EQH
TITLE CRYSTAL STRUCTURE OF A POLYETHYLENE TEREPHTHALATE DEGRADING HYDROLASE
TITLE 2 FROM IDEONELLA SAKAIENSIS IN SPACEGROUP C2221
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 (STRAIN 201-F6);
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
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 6EQH 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. 1.58 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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.68
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 139743
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 6926
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 43.6930 - 4.9072 0.99 4708 263 0.1676 0.1779
REMARK 3 2 4.9072 - 3.8958 1.00 4529 244 0.1305 0.1568
REMARK 3 3 3.8958 - 3.4035 1.00 4488 261 0.1409 0.1368
REMARK 3 4 3.4035 - 3.0924 1.00 4476 207 0.1555 0.1682
REMARK 3 5 3.0924 - 2.8708 1.00 4515 219 0.1616 0.1757
REMARK 3 6 2.8708 - 2.7016 1.00 4443 236 0.1670 0.1810
REMARK 3 7 2.7016 - 2.5663 1.00 4456 224 0.1648 0.1922
REMARK 3 8 2.5663 - 2.4546 1.00 4426 245 0.1678 0.1767
REMARK 3 9 2.4546 - 2.3601 1.00 4430 224 0.1685 0.1771
REMARK 3 10 2.3601 - 2.2787 1.00 4423 222 0.1625 0.1693
REMARK 3 11 2.2787 - 2.2074 1.00 4424 235 0.1674 0.1806
REMARK 3 12 2.2074 - 2.1443 1.00 4430 239 0.1695 0.1893
REMARK 3 13 2.1443 - 2.0879 1.00 4410 225 0.1747 0.2173
REMARK 3 14 2.0879 - 2.0370 1.00 4409 227 0.1748 0.1811
REMARK 3 15 2.0370 - 1.9906 1.00 4434 214 0.1709 0.1852
REMARK 3 16 1.9906 - 1.9483 1.00 4412 213 0.1776 0.2081
REMARK 3 17 1.9483 - 1.9093 1.00 4415 221 0.1945 0.2056
REMARK 3 18 1.9093 - 1.8733 1.00 4391 215 0.1983 0.2403
REMARK 3 19 1.8733 - 1.8398 1.00 4436 213 0.1924 0.2388
REMARK 3 20 1.8398 - 1.8086 1.00 4389 213 0.2019 0.2097
REMARK 3 21 1.8086 - 1.7795 1.00 4420 232 0.1990 0.2519
REMARK 3 22 1.7795 - 1.7521 1.00 4358 223 0.2086 0.2394
REMARK 3 23 1.7521 - 1.7263 1.00 4421 230 0.2284 0.2409
REMARK 3 24 1.7263 - 1.7020 1.00 4360 217 0.2328 0.2624
REMARK 3 25 1.7020 - 1.6790 1.00 4385 256 0.2486 0.2687
REMARK 3 26 1.6790 - 1.6572 1.00 4378 233 0.2575 0.2796
REMARK 3 27 1.6572 - 1.6365 1.00 4357 250 0.2756 0.2922
REMARK 3 28 1.6365 - 1.6168 1.00 4404 222 0.2956 0.3425
REMARK 3 29 1.6168 - 1.5980 1.00 4304 257 0.3052 0.3275
REMARK 3 30 1.5980 - 1.5800 0.99 4386 246 0.3457 0.3455
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.770
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 : 0.007 5995
REMARK 3 ANGLE : 0.826 8186
REMARK 3 CHIRALITY : 0.055 904
REMARK 3 PLANARITY : 0.006 1081
REMARK 3 DIHEDRAL : 2.607 4831
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 6EQH 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_1200007062.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 139895
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 49.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.74200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6EQD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M MGSO4, 0.1 M MES, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 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 82.56150
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 82.56150
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 26.35100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 117.06700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.35100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 117.06700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 82.56150
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.35100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 117.06700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.56150
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.35100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 117.06700
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 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 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 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 457 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 519 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 581 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 LEU C 291
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 C 325 O HOH C 539 1.80
REMARK 500 O HOH A 544 O HOH A 564 1.81
REMARK 500 O HOH C 479 O HOH C 521 1.83
REMARK 500 O HOH A 366 O HOH A 535 1.84
REMARK 500 O HOH A 425 O HOH A 566 1.88
REMARK 500 O HOH A 303 O HOH A 540 1.88
REMARK 500 N ARG C 59 O HOH C 301 1.89
REMARK 500 O HOH A 366 O HOH B 565 1.95
REMARK 500 O HOH A 494 O HOH A 581 1.98
REMARK 500 O HOH C 415 O HOH C 561 2.00
REMARK 500 O HOH B 338 O HOH B 524 2.00
REMARK 500 O HOH B 364 O HOH B 533 2.01
REMARK 500 O HOH C 414 O HOH C 488 2.06
REMARK 500 OE2 GLU B 204 O HOH B 301 2.08
REMARK 500 O HOH A 459 O HOH A 467 2.08
REMARK 500 O HOH C 447 O HOH C 544 2.08
REMARK 500 O HOH A 592 O HOH A 627 2.09
REMARK 500 O HOH A 367 O HOH A 573 2.09
REMARK 500 O HOH B 370 O HOH B 598 2.10
REMARK 500 O HOH A 392 O HOH A 548 2.10
REMARK 500 O HOH C 497 O HOH C 526 2.11
REMARK 500 O HOH C 465 O HOH C 575 2.11
REMARK 500 O HOH B 490 O HOH B 493 2.11
REMARK 500 O HOH C 301 O HOH C 520 2.12
REMARK 500 O HOH B 526 O HOH B 614 2.12
REMARK 500 O HOH C 338 O HOH C 549 2.13
REMARK 500 O HOH C 305 O HOH C 343 2.13
REMARK 500 O HOH A 573 O HOH A 603 2.13
REMARK 500 OE1 GLN C 119 O HOH C 302 2.14
REMARK 500 O HOH C 392 O HOH C 537 2.14
REMARK 500 O HOH A 480 O HOH A 619 2.14
REMARK 500 O HOH B 501 O HOH B 609 2.15
REMARK 500 O HOH A 301 O HOH A 552 2.16
REMARK 500 O HOH B 378 O HOH B 607 2.16
REMARK 500 O HOH A 302 O HOH A 371 2.16
REMARK 500 O HOH B 409 O HOH B 620 2.17
REMARK 500 O HOH C 331 O HOH C 500 2.18
REMARK 500 N THR B 29 O HOH B 302 2.18
REMARK 500 O HOH B 485 O HOH B 580 2.18
REMARK 500 O HOH B 303 O HOH B 566 2.19
REMARK 500 OG SER C 121 O HOH C 303 2.19
REMARK 500 O HOH B 315 O HOH B 403 2.19
REMARK 500 O HOH A 559 O HOH A 587 2.19
REMARK 500 O HOH B 452 O HOH B 478 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 O HOH A 504 O HOH A 504 3757 2.02
REMARK 500 O HOH A 608 O HOH A 627 3757 2.08
REMARK 500 O HOH C 561 O HOH C 597 3856 2.09
REMARK 500 O HOH B 304 O HOH B 346 8477 2.11
REMARK 500 O HOH A 592 O HOH A 608 3757 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 53 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 53 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
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 THR A 88 -3.02 69.85
REMARK 500 SER A 160 -122.71 64.89
REMARK 500 ALA A 183 55.19 39.34
REMARK 500 SER A 214 -86.16 -132.78
REMARK 500 THR B 88 -0.45 71.18
REMARK 500 SER B 160 -123.10 66.39
REMARK 500 SER B 214 -86.07 -133.96
REMARK 500 THR C 88 -0.96 70.79
REMARK 500 SER C 160 -120.35 63.08
REMARK 500 SER C 214 -86.28 -138.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 642 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH B 643 DISTANCE = 6.43 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6EQD RELATED DB: PDB
REMARK 900 ORIGINAL PETASE STRUCTURE
DBREF1 6EQH A 1 290 UNP PETH_IDESA
DBREF2 6EQH A A0A0K8P6T7 1 290
DBREF1 6EQH B 1 290 UNP PETH_IDESA
DBREF2 6EQH B A0A0K8P6T7 1 290
DBREF1 6EQH C 1 290 UNP PETH_IDESA
DBREF2 6EQH C A0A0K8P6T7 1 290
SEQADV 6EQH LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH LEU B 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH GLU B 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS B 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS B 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS B 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS B 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS B 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS B 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH LEU C 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH GLU C 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS C 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS C 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS C 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS C 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH HIS C 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6EQH 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
FORMUL 4 HOH *990(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 SER A 214 MET A 222 1 9
HELIX 7 AA7 ASN A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
HELIX 10 AB1 THR B 39 ALA B 45 1 7
HELIX 11 AB2 ARG B 90 LYS B 95 5 6
HELIX 12 AB3 TRP B 96 SER B 103 1 8
HELIX 13 AB4 GLN B 119 GLY B 139 1 21
HELIX 14 AB5 SER B 160 ASN B 173 1 14
HELIX 15 AB6 SER B 214 MET B 222 1 9
HELIX 16 AB7 ASN B 246 ASP B 263 1 18
HELIX 17 AB8 ASP B 265 ARG B 267 5 3
HELIX 18 AB9 TYR B 268 GLU B 274 1 7
HELIX 19 AC1 THR C 39 ALA C 45 1 7
HELIX 20 AC2 ARG C 90 LYS C 95 5 6
HELIX 21 AC3 TRP C 96 SER C 103 1 8
HELIX 22 AC4 GLN C 119 GLY C 139 1 21
HELIX 23 AC5 SER C 160 ASN C 173 1 14
HELIX 24 AC6 PRO C 210 SER C 213 5 4
HELIX 25 AC7 SER C 214 MET C 222 1 9
HELIX 26 AC8 ASN C 246 ASP C 263 1 18
HELIX 27 AC9 ASP C 265 ARG C 267 5 3
HELIX 28 AD1 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 GLN A 228 N ILE A 200
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 GLY B 158 1 O ASP B 150 N VAL B 78
SHEET 6 AA3 6 ALA B 178 ALA B 179 1 O ALA B 178 N VAL B 156
SHEET 1 AA4 3 THR B 198 CYS B 203 0
SHEET 2 AA4 3 LYS B 227 ILE B 232 1 O ILE B 232 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 2.06
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.04
SSBOND 3 CYS B 203 CYS B 239 1555 1555 2.07
SSBOND 4 CYS B 273 CYS B 289 1555 1555 2.03
SSBOND 5 CYS C 203 CYS C 239 1555 1555 2.06
SSBOND 6 CYS C 273 CYS C 289 1555 1555 2.06
CRYST1 52.702 234.134 165.123 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 0.018975 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004271 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006056 0.00000
TER 1950 LEU A 291
TER 3909 GLU B 292
TER 5846 SER C 290
MASTER 509 0 0 28 27 0 0 6 6790 3 12 69
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