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HEADER HYDROLASE 27-MAY-25 9V77
TITLE INSIGHTS INTO A VERSATILE PET-DEGRADING ENZYME TMFAE-PETASE : FROM
TITLE 2 MOLECULAR MECHANISM TO PRACTICAL APPLICATIONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TMFAE - PETASE MUTANT Q223N;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GUT METAGENOME;
SOURCE 3 ORGANISM_TAXID: 749906;
SOURCE 4 EXPRESSION_SYSTEM: ROSETTA;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 3132615
KEYWDS PET HYDROLASE; STRUCTURE; MUTATION; LIGNIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.X.HOU,X.X.HOU
REVDAT 1 03-JUN-26 9V77 0
JRNL AUTH X.X.HOU,X.X.HOU
JRNL TITL INSIGHTS INTO A VERSATILE PET-DEGRADING ENZYME TMFAE-PETASE
JRNL TITL 2 : FROM MOLECULAR MECHANISM TO PRACTICAL APPLICATIONS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 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 : GEOSTD + MONOMER LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.7
REMARK 3 NUMBER OF REFLECTIONS : 42240
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.249
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.305
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.250
REMARK 3 FREE R VALUE TEST SET COUNT : 1796
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 30.2900 - 4.7000 0.94 3517 156 0.1969 0.2489
REMARK 3 2 4.7000 - 3.7300 0.97 3442 153 0.1956 0.2373
REMARK 3 3 3.7300 - 3.2600 0.99 3495 155 0.2074 0.2710
REMARK 3 4 3.2600 - 2.9600 0.92 3232 138 0.2706 0.3470
REMARK 3 5 2.9600 - 2.7500 0.89 3135 133 0.2937 0.3533
REMARK 3 6 2.7500 - 2.5900 0.92 3180 142 0.2750 0.2978
REMARK 3 7 2.5900 - 2.4600 0.87 3022 139 0.2863 0.3366
REMARK 3 8 2.4600 - 2.3500 0.83 2907 133 0.2966 0.4150
REMARK 3 9 2.3500 - 2.2600 0.84 2913 131 0.2894 0.3323
REMARK 3 10 2.2600 - 2.1800 0.89 3075 136 0.2869 0.3612
REMARK 3 11 2.1800 - 2.1100 0.89 3051 140 0.3181 0.4005
REMARK 3 12 2.1100 - 2.0500 0.88 3059 136 0.3341 0.4147
REMARK 3 13 2.0500 - 2.0000 0.70 2416 104 0.3940 0.4281
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) : 0.353
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.025
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.68
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 3726
REMARK 3 ANGLE : 0.932 5072
REMARK 3 CHIRALITY : 0.053 576
REMARK 3 PLANARITY : 0.007 658
REMARK 3 DIHEDRAL : 2.943 2212
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 9V77 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 30-MAY-25.
REMARK 100 THE DEPOSITION ID IS D_1300059762.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-24
REMARK 200 TEMPERATURE (KELVIN) : 150
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
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 EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46988
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES MONOHYDRATE PH 6.5;12% W/V
REMARK 280 POLYETHYLENE GLYCOL 20,000, VAPOR DIFFUSION, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 60.13550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.33000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.61200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 25.33000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.13550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.61200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 A 423 O HOH A 499 1.62
REMARK 500 O HOH B 361 O HOH B 398 1.82
REMARK 500 O HOH B 350 O HOH B 361 1.83
REMARK 500 O HOH A 357 O HOH A 520 1.84
REMARK 500 O PHE A 244 O HOH A 301 1.86
REMARK 500 O LEU A 64 O HOH A 302 1.87
REMARK 500 O ASP B 74 O HOH B 301 1.89
REMARK 500 O HOH A 533 O HOH A 538 1.90
REMARK 500 O LEU A 205 O HOH A 303 1.90
REMARK 500 O HOH A 402 O HOH A 525 1.91
REMARK 500 O GLY A 16 O HOH A 304 1.91
REMARK 500 O GLY A 56 O HOH A 305 1.92
REMARK 500 O HOH B 380 O HOH B 407 1.92
REMARK 500 O HOH A 492 O HOH A 540 1.93
REMARK 500 N ALA B 78 O HOH B 301 1.94
REMARK 500 O HOH B 355 O HOH B 420 1.94
REMARK 500 O HOH A 432 O HOH A 483 1.95
REMARK 500 O HOH A 513 O HOH A 563 1.99
REMARK 500 O HOH B 397 O HOH B 435 2.00
REMARK 500 O HOH A 530 O HOH A 553 2.01
REMARK 500 O HOH A 421 O HOH A 446 2.02
REMARK 500 NH2 ARG B 38 O HOH B 302 2.02
REMARK 500 NE2 GLN A 236 O HOH A 306 2.02
REMARK 500 OE1 GLU B 238 O HOH B 303 2.02
REMARK 500 O LEU A 58 O HOH A 307 2.04
REMARK 500 OG1 THR B 160 O HOH B 304 2.04
REMARK 500 NZ LYS A 164 O HOH A 308 2.04
REMARK 500 N GLY B 16 O HOH B 305 2.05
REMARK 500 O HOH A 493 O HOH A 571 2.05
REMARK 500 O HOH A 322 O HOH A 500 2.06
REMARK 500 OE2 GLU A 151 O HOH A 309 2.06
REMARK 500 O HOH A 480 O HOH A 502 2.06
REMARK 500 O HOH A 515 O HOH A 534 2.07
REMARK 500 O HOH B 402 O HOH B 510 2.07
REMARK 500 O HOH A 482 O HOH A 564 2.07
REMARK 500 O THR B 144 O HOH B 306 2.07
REMARK 500 O HOH B 305 O HOH B 452 2.07
REMARK 500 O HOH A 476 O HOH A 512 2.07
REMARK 500 O HOH B 447 O HOH B 476 2.08
REMARK 500 O HOH A 371 O HOH A 510 2.08
REMARK 500 O HOH B 423 O HOH B 524 2.08
REMARK 500 OG1 THR A 46 O HOH A 304 2.09
REMARK 500 O HOH B 415 O HOH B 530 2.09
REMARK 500 O HOH A 310 O HOH A 449 2.09
REMARK 500 O HOH B 371 O HOH B 450 2.09
REMARK 500 OE1 GLN A 162 O HOH A 310 2.09
REMARK 500 O HOH A 372 O HOH A 451 2.09
REMARK 500 N ALA A 209 O HOH A 303 2.10
REMARK 500 O HOH B 307 O HOH B 393 2.10
REMARK 500 O LYS B 154 O HOH B 307 2.10
REMARK 500
REMARK 500 THIS ENTRY HAS 73 CLOSE CONTACTS
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 497 O HOH B 449 2455 2.03
REMARK 500 O HOH A 504 O HOH B 414 1556 2.08
REMARK 500 O HOH A 535 O HOH B 494 1556 2.11
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 29 178.52 172.61
REMARK 500 SER A 96 -119.99 60.68
REMARK 500 GLN A 109 75.97 53.58
REMARK 500 GLN A 195 56.09 -118.61
REMARK 500 MET A 198 -42.65 -131.05
REMARK 500 THR A 212 4.65 -69.47
REMARK 500 HIS A 226 -71.24 -50.99
REMARK 500 VAL A 227 68.87 -67.97
REMARK 500 SER B 96 -122.59 55.74
REMARK 500 PRO B 182 1.83 -64.44
REMARK 500 GLN B 195 49.61 -105.94
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 A 580 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A 581 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A 582 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 583 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A 584 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A 585 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A 586 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 587 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH A 588 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A 589 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A 590 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH A 591 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH A 592 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH A 593 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A 594 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH A 595 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH A 596 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH A 597 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH A 598 DISTANCE = 7.47 ANGSTROMS
REMARK 525 HOH A 599 DISTANCE = 7.82 ANGSTROMS
REMARK 525 HOH A 600 DISTANCE = 7.84 ANGSTROMS
REMARK 525 HOH A 601 DISTANCE = 8.76 ANGSTROMS
REMARK 525 HOH A 602 DISTANCE = 9.43 ANGSTROMS
REMARK 525 HOH A 603 DISTANCE = 10.33 ANGSTROMS
REMARK 525 HOH B 545 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B 546 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH B 547 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 548 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH B 549 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH B 550 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH B 551 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH B 552 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH B 553 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH B 554 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH B 555 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH B 556 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH B 557 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH B 558 DISTANCE = 7.19 ANGSTROMS
REMARK 525 HOH B 559 DISTANCE = 7.31 ANGSTROMS
REMARK 525 HOH B 560 DISTANCE = 7.45 ANGSTROMS
REMARK 525 HOH B 561 DISTANCE = 7.61 ANGSTROMS
REMARK 525 HOH B 562 DISTANCE = 7.70 ANGSTROMS
REMARK 525 HOH B 563 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH B 564 DISTANCE = 8.79 ANGSTROMS
REMARK 525 HOH B 565 DISTANCE = 9.02 ANGSTROMS
REMARK 525 HOH B 566 DISTANCE = 9.41 ANGSTROMS
REMARK 525 HOH B 567 DISTANCE = 10.82 ANGSTROMS
REMARK 525 HOH B 568 DISTANCE = 11.21 ANGSTROMS
DBREF 9V77 A 16 250 PDB 9V77 9V77 16 250
DBREF 9V77 B 16 250 PDB 9V77 9V77 16 250
SEQRES 1 A 235 GLY SER GLN ALA VAL LEU LEU LEU HIS ALA TYR SER GLY
SEQRES 2 A 235 SER SER ASN ASP VAL ARG MET LEU SER ARG SER LEU GLU
SEQRES 3 A 235 LYS ALA GLY TYR THR VAL TYR SER PRO ASN PHE SER GLY
SEQRES 4 A 235 HIS GLY THR LEU ARG PRO GLU ASP ILE LEU GLU GLN THR
SEQRES 5 A 235 PRO GLU GLN TRP TRP GLN ASP THR VAL ALA ALA VAL ASN
SEQRES 6 A 235 PHE LEU ARG GLU LYS GLY TYR GLU LYS VAL ALA VAL PHE
SEQRES 7 A 235 GLY LEU SER MET GLY GLY ILE PHE ALA MET ARG THR LEU
SEQRES 8 A 235 THR GLU GLN ILE PRO GLY VAL ILE GLY GLY GLY PHE PHE
SEQRES 9 A 235 CYS SER PRO ILE LEU PRO THR LYS ASN HIS VAL PRO GLU
SEQRES 10 A 235 ASN PHE VAL ARG TYR ALA GLN GLN VAL LEU THR THR ALA
SEQRES 11 A 235 GLY ILE SER ALA GLU GLU GLN ALA LYS ARG LEU PRO GLN
SEQRES 12 A 235 ILE THR GLU GLN VAL LYS ASP GLN LEU SER GLU ILE GLU
SEQRES 13 A 235 GLN GLY THR GLN LEU THR ALA ALA LYS LEU PRO LYS VAL
SEQRES 14 A 235 THR LEU PRO VAL PHE ALA ALA GLN ALA GLY GLN ASP GLU
SEQRES 15 A 235 MET ILE ASP ALA LYS VAL VAL LEU GLN THR VAL ALA GLN
SEQRES 16 A 235 LEU THR GLN THR TYR ILE THR PHE ASN TRP TYR PRO ASN
SEQRES 17 A 235 SER GLY HIS VAL ILE THR VAL GLY PRO ASP HIS LYS GLN
SEQRES 18 A 235 LEU GLU GLN ASP VAL ALA SER PHE LEU ALA SER LEU SER
SEQRES 19 A 235 TRP
SEQRES 1 B 235 GLY SER GLN ALA VAL LEU LEU LEU HIS ALA TYR SER GLY
SEQRES 2 B 235 SER SER ASN ASP VAL ARG MET LEU SER ARG SER LEU GLU
SEQRES 3 B 235 LYS ALA GLY TYR THR VAL TYR SER PRO ASN PHE SER GLY
SEQRES 4 B 235 HIS GLY THR LEU ARG PRO GLU ASP ILE LEU GLU GLN THR
SEQRES 5 B 235 PRO GLU GLN TRP TRP GLN ASP THR VAL ALA ALA VAL ASN
SEQRES 6 B 235 PHE LEU ARG GLU LYS GLY TYR GLU LYS VAL ALA VAL PHE
SEQRES 7 B 235 GLY LEU SER MET GLY GLY ILE PHE ALA MET ARG THR LEU
SEQRES 8 B 235 THR GLU GLN ILE PRO GLY VAL ILE GLY GLY GLY PHE PHE
SEQRES 9 B 235 CYS SER PRO ILE LEU PRO THR LYS ASN HIS VAL PRO GLU
SEQRES 10 B 235 ASN PHE VAL ARG TYR ALA GLN GLN VAL LEU THR THR ALA
SEQRES 11 B 235 GLY ILE SER ALA GLU GLU GLN ALA LYS ARG LEU PRO GLN
SEQRES 12 B 235 ILE THR GLU GLN VAL LYS ASP GLN LEU SER GLU ILE GLU
SEQRES 13 B 235 GLN GLY THR GLN LEU THR ALA ALA LYS LEU PRO LYS VAL
SEQRES 14 B 235 THR LEU PRO VAL PHE ALA ALA GLN ALA GLY GLN ASP GLU
SEQRES 15 B 235 MET ILE ASP ALA LYS VAL VAL LEU GLN THR VAL ALA GLN
SEQRES 16 B 235 LEU THR GLN THR TYR ILE THR PHE ASN TRP TYR PRO ASN
SEQRES 17 B 235 SER GLY HIS VAL ILE THR VAL GLY PRO ASP HIS LYS GLN
SEQRES 18 B 235 LEU GLU GLN ASP VAL ALA SER PHE LEU ALA SER LEU SER
SEQRES 19 B 235 TRP
FORMUL 3 HOH *571(H2 O)
HELIX 1 AA1 SER A 29 ASP A 32 5 4
HELIX 2 AA2 VAL A 33 LYS A 42 1 10
HELIX 3 AA3 PRO A 60 GLU A 65 1 6
HELIX 4 AA4 THR A 67 GLY A 86 1 20
HELIX 5 AA5 SER A 96 GLU A 108 1 13
HELIX 6 AA6 HIS A 129 ALA A 145 1 17
HELIX 7 AA7 SER A 148 ALA A 179 1 32
HELIX 8 AA8 LYS A 180 VAL A 184 5 5
HELIX 9 AA9 ASP A 200 LYS A 202 5 3
HELIX 10 AB1 VAL A 203 ALA A 209 1 7
HELIX 11 AB2 ASP A 233 ALA A 246 1 14
HELIX 12 AB3 SER B 29 ASP B 32 5 4
HELIX 13 AB4 VAL B 33 ALA B 43 1 11
HELIX 14 AB5 PRO B 60 GLU B 65 1 6
HELIX 15 AB6 THR B 67 GLU B 84 1 18
HELIX 16 AB7 SER B 96 GLU B 108 1 13
HELIX 17 AB8 HIS B 129 ALA B 145 1 17
HELIX 18 AB9 SER B 148 LYS B 180 1 33
HELIX 19 AC1 LEU B 181 VAL B 184 5 4
HELIX 20 AC2 ASP B 200 LYS B 202 5 3
HELIX 21 AC3 VAL B 203 ALA B 209 1 7
HELIX 22 AC4 ASP B 233 SER B 247 1 15
SHEET 1 AA1 6 THR A 46 TYR A 48 0
SHEET 2 AA1 6 ALA A 19 LEU A 23 1 N VAL A 20 O TYR A 48
SHEET 3 AA1 6 VAL A 90 LEU A 95 1 O PHE A 93 N LEU A 21
SHEET 4 AA1 6 VAL A 113 PHE A 119 1 O PHE A 119 N GLY A 94
SHEET 5 AA1 6 VAL A 188 ALA A 193 1 O PHE A 189 N GLY A 116
SHEET 6 AA1 6 ILE A 216 TYR A 221 1 O ASN A 219 N ALA A 190
SHEET 1 AA2 6 THR B 46 TYR B 48 0
SHEET 2 AA2 6 ALA B 19 LEU B 23 1 N VAL B 20 O THR B 46
SHEET 3 AA2 6 VAL B 90 GLY B 94 1 O PHE B 93 N LEU B 21
SHEET 4 AA2 6 VAL B 113 PHE B 119 1 O PHE B 119 N GLY B 94
SHEET 5 AA2 6 VAL B 188 ALA B 193 1 O ALA B 191 N PHE B 118
SHEET 6 AA2 6 ILE B 216 TYR B 221 1 O THR B 217 N ALA B 190
CRYST1 120.271 113.224 50.660 90.00 90.00 90.00 P 21 21 21 8
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 0.008315 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008832 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019739 0.00000
TER 1823 TRP A 250
TER 3646 TRP B 250
MASTER 376 0 0 22 12 0 0 6 4215 2 0 38
END |