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HEADER HYDROLASE 05-MAY-25 9UTZ
TITLE THE STRUCTURE OF THE E147K/Q174E/D197K TRIPLE MUTANT OF PES-H1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PES-H1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET HYDROLASE, ENZYME ENGINEERING, SALT TOLERANCE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.XIE,A.LIU
REVDAT 1 13-MAY-26 9UTZ 0
JRNL AUTH W.XIE,A.LIU
JRNL TITL THE STRUCTURE OF THE E147K/Q174E/D197K TRIPLE MUTANT OF
JRNL TITL 2 PES-H1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.21.1_5286: ???)
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) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 46798
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2368
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 36.4200 - 4.7000 1.00 2859 135 0.1792 0.1686
REMARK 3 2 4.7000 - 3.7300 1.00 2712 154 0.1469 0.1658
REMARK 3 3 3.7300 - 3.2600 1.00 2704 137 0.1637 0.1562
REMARK 3 4 3.2600 - 2.9600 1.00 2675 141 0.1777 0.2224
REMARK 3 5 2.9600 - 2.7500 1.00 2657 149 0.1873 0.2185
REMARK 3 6 2.7500 - 2.5900 1.00 2648 136 0.1901 0.2292
REMARK 3 7 2.5900 - 2.4600 1.00 2610 155 0.1809 0.2198
REMARK 3 8 2.4600 - 2.3500 1.00 2666 137 0.1761 0.2112
REMARK 3 9 2.3500 - 2.2600 1.00 2642 135 0.1850 0.2223
REMARK 3 10 2.2600 - 2.1800 1.00 2619 139 0.1915 0.2291
REMARK 3 11 2.1800 - 2.1100 1.00 2625 155 0.1848 0.2358
REMARK 3 12 2.1100 - 2.0500 1.00 2616 119 0.1898 0.2055
REMARK 3 13 2.0500 - 2.0000 1.00 2625 150 0.1901 0.2245
REMARK 3 14 2.0000 - 1.9500 1.00 2617 132 0.1908 0.2423
REMARK 3 15 1.9500 - 1.9100 0.97 2533 142 0.2021 0.2524
REMARK 3 16 1.9100 - 1.8700 0.93 2433 142 0.2165 0.2567
REMARK 3 17 1.8700 - 1.8300 0.83 2189 110 0.2171 0.2499
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.000
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 : 0.006 4034
REMARK 3 ANGLE : 0.809 5502
REMARK 3 CHIRALITY : 0.051 611
REMARK 3 PLANARITY : 0.010 730
REMARK 3 DIHEDRAL : 14.891 1454
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 9UTZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 08-MAY-25.
REMARK 100 THE DEPOSITION ID IS D_1300059154.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-25
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46882
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 43.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : 0.14700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.37700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% W/V PEG 6000, 0.1 M CITRIC ACID
REMARK 280 (PH 4.0), 30% V/V MPD, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 27.91800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.21000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.05800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.21000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.91800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.05800
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 HIS B -1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 32 CG CD1 CD2
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 457 O HOH B 480 2.03
REMARK 500 O HOH B 331 O HOH B 423 2.05
REMARK 500 O GLY A 51 O HOH A 301 2.08
REMARK 500 O HOH B 478 O HOH B 498 2.08
REMARK 500 O HOH A 475 O HOH A 480 2.09
REMARK 500 O THR A 46 O HOH A 302 2.09
REMARK 500 O HOH A 335 O HOH A 454 2.09
REMARK 500 O HOH A 502 O HOH B 509 2.09
REMARK 500 O HOH B 393 O HOH B 495 2.11
REMARK 500 O HOH A 371 O HOH A 482 2.12
REMARK 500 O HOH A 305 O HOH A 320 2.13
REMARK 500 OD2 ASP A 107 O HOH A 303 2.14
REMARK 500 O HOH A 450 O HOH A 489 2.14
REMARK 500 O HOH A 321 O HOH A 387 2.14
REMARK 500 O HOH A 457 O HOH A 482 2.14
REMARK 500 O HOH A 502 O HOH A 510 2.15
REMARK 500 O HOH A 480 O HOH A 492 2.15
REMARK 500 O ALA B 34 O HOH B 301 2.16
REMARK 500 O HOH A 325 O HOH A 479 2.16
REMARK 500 OD2 ASP A 96 O HOH A 304 2.17
REMARK 500 O HOH A 501 O HOH A 511 2.17
REMARK 500 O HOH A 313 O HOH A 400 2.17
REMARK 500 O HOH B 323 O HOH B 489 2.17
REMARK 500 OG SER A 163 O HOH A 305 2.17
REMARK 500 O HOH B 315 O HOH B 433 2.19
REMARK 500 O HOH A 475 O HOH A 492 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 485 O HOH B 505 2555 2.14
REMARK 500 O HOH A 478 O HOH B 487 2555 2.15
REMARK 500 O HOH A 400 O HOH B 469 2555 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 63 -3.18 70.97
REMARK 500 SER A 130 -115.61 57.34
REMARK 500 ASN A 143 88.96 -158.79
REMARK 500 HIS A 184 -96.51 -123.05
REMARK 500 PRO A 242 -149.59 -84.47
REMARK 500 SER B 130 -123.60 63.58
REMARK 500 ASN B 143 92.28 -166.84
REMARK 500 HIS B 184 -97.39 -120.35
REMARK 500 PRO B 242 -148.80 -82.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 98 0.08 SIDE CHAIN
REMARK 500 ARG B 98 0.08 SIDE CHAIN
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 511 DISTANCE = 6.39 ANGSTROMS
DBREF 9UTZ A -3 258 PDB 9UTZ 9UTZ -3 258
DBREF 9UTZ B -3 258 PDB 9UTZ 9UTZ -3 258
SEQRES 1 A 262 GLY PRO HIS MET ALA ASN PRO TYR GLU ARG GLY PRO ASP
SEQRES 2 A 262 PRO THR GLU SER SER ILE GLU ALA VAL ARG GLY PRO PHE
SEQRES 3 A 262 ALA VAL ALA GLN THR THR VAL SER ARG LEU GLN ALA ASP
SEQRES 4 A 262 GLY PHE GLY GLY GLY THR ILE TYR TYR PRO THR ASP THR
SEQRES 5 A 262 SER GLN GLY THR PHE GLY ALA VAL ALA ILE SER PRO GLY
SEQRES 6 A 262 PHE THR ALA GLY GLN GLU SER ILE ALA TRP LEU GLY PRO
SEQRES 7 A 262 ARG ILE ALA SER GLN GLY PHE VAL VAL ILE THR ILE ASP
SEQRES 8 A 262 THR ILE THR ARG LEU ASP GLN PRO ASP SER ARG GLY ARG
SEQRES 9 A 262 GLN LEU GLN ALA ALA LEU ASP HIS LEU ARG THR ASN SER
SEQRES 10 A 262 VAL VAL ARG ASN ARG ILE ASP PRO ASN ARG MET ALA VAL
SEQRES 11 A 262 MET GLY HIS SER MET GLY GLY GLY GLY ALA LEU SER ALA
SEQRES 12 A 262 ALA ALA ASN ASN THR SER LEU LYS ALA ALA ILE PRO LEU
SEQRES 13 A 262 GLN GLY TRP HIS THR ARG LYS ASN TRP SER SER VAL ARG
SEQRES 14 A 262 THR PRO THR LEU VAL VAL GLY ALA GLU LEU ASP THR ILE
SEQRES 15 A 262 ALA PRO VAL SER SER HIS SER GLU ALA PHE TYR ASN SER
SEQRES 16 A 262 LEU PRO SER ASP LEU LYS LYS ALA TYR MET GLU LEU ARG
SEQRES 17 A 262 GLY ALA SER HIS LEU VAL SER ASN THR PRO ASP THR THR
SEQRES 18 A 262 THR ALA LYS TYR SER ILE ALA TRP LEU LYS ARG PHE VAL
SEQRES 19 A 262 ASP ASP ASP LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA
SEQRES 20 A 262 PRO ASP ASP PHE ALA ILE SER GLU TYR ARG SER THR CYS
SEQRES 21 A 262 PRO PHE
SEQRES 1 B 262 GLY PRO HIS MET ALA ASN PRO TYR GLU ARG GLY PRO ASP
SEQRES 2 B 262 PRO THR GLU SER SER ILE GLU ALA VAL ARG GLY PRO PHE
SEQRES 3 B 262 ALA VAL ALA GLN THR THR VAL SER ARG LEU GLN ALA ASP
SEQRES 4 B 262 GLY PHE GLY GLY GLY THR ILE TYR TYR PRO THR ASP THR
SEQRES 5 B 262 SER GLN GLY THR PHE GLY ALA VAL ALA ILE SER PRO GLY
SEQRES 6 B 262 PHE THR ALA GLY GLN GLU SER ILE ALA TRP LEU GLY PRO
SEQRES 7 B 262 ARG ILE ALA SER GLN GLY PHE VAL VAL ILE THR ILE ASP
SEQRES 8 B 262 THR ILE THR ARG LEU ASP GLN PRO ASP SER ARG GLY ARG
SEQRES 9 B 262 GLN LEU GLN ALA ALA LEU ASP HIS LEU ARG THR ASN SER
SEQRES 10 B 262 VAL VAL ARG ASN ARG ILE ASP PRO ASN ARG MET ALA VAL
SEQRES 11 B 262 MET GLY HIS SER MET GLY GLY GLY GLY ALA LEU SER ALA
SEQRES 12 B 262 ALA ALA ASN ASN THR SER LEU LYS ALA ALA ILE PRO LEU
SEQRES 13 B 262 GLN GLY TRP HIS THR ARG LYS ASN TRP SER SER VAL ARG
SEQRES 14 B 262 THR PRO THR LEU VAL VAL GLY ALA GLU LEU ASP THR ILE
SEQRES 15 B 262 ALA PRO VAL SER SER HIS SER GLU ALA PHE TYR ASN SER
SEQRES 16 B 262 LEU PRO SER ASP LEU LYS LYS ALA TYR MET GLU LEU ARG
SEQRES 17 B 262 GLY ALA SER HIS LEU VAL SER ASN THR PRO ASP THR THR
SEQRES 18 B 262 THR ALA LYS TYR SER ILE ALA TRP LEU LYS ARG PHE VAL
SEQRES 19 B 262 ASP ASP ASP LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA
SEQRES 20 B 262 PRO ASP ASP PHE ALA ILE SER GLU TYR ARG SER THR CYS
SEQRES 21 B 262 PRO PHE
FORMUL 3 HOH *431(H2 O)
HELIX 1 AA1 THR A 11 ALA A 17 1 7
HELIX 2 AA2 GLY A 65 ALA A 70 5 6
HELIX 3 AA3 TRP A 71 SER A 78 1 8
HELIX 4 AA4 GLN A 94 ASN A 112 1 19
HELIX 5 AA5 VAL A 115 ASN A 117 5 3
HELIX 6 AA6 SER A 130 ASN A 142 1 13
HELIX 7 AA7 HIS A 184 LEU A 192 1 9
HELIX 8 AA8 LEU A 209 THR A 213 5 5
HELIX 9 AA9 ASP A 215 ASP A 231 1 17
HELIX 10 AB1 ASP A 233 ARG A 235 5 3
HELIX 11 AB2 TYR A 236 CYS A 241 1 6
HELIX 12 AB3 THR B 11 ALA B 17 1 7
HELIX 13 AB4 GLY B 65 ALA B 70 5 6
HELIX 14 AB5 TRP B 71 SER B 78 1 8
HELIX 15 AB6 GLN B 94 ARG B 110 1 17
HELIX 16 AB7 VAL B 115 ASN B 117 5 3
HELIX 17 AB8 SER B 130 ASN B 142 1 13
HELIX 18 AB9 HIS B 184 LEU B 192 1 9
HELIX 19 AC1 SER B 207 THR B 213 5 7
HELIX 20 AC2 ASP B 215 ASP B 231 1 17
HELIX 21 AC3 ASP B 233 ARG B 235 5 3
HELIX 22 AC4 TYR B 236 CYS B 241 1 6
SHEET 1 AA1 6 VAL A 24 VAL A 29 0
SHEET 2 AA1 6 GLY A 40 PRO A 45 -1 O GLY A 40 N VAL A 29
SHEET 3 AA1 6 VAL A 82 ILE A 86 -1 O VAL A 83 N TYR A 43
SHEET 4 AA1 6 PHE A 53 SER A 59 1 N VAL A 56 O VAL A 82
SHEET 5 AA1 6 ILE A 119 HIS A 129 1 O MET A 127 N ALA A 57
SHEET 6 AA1 6 ALA A 148 LEU A 152 1 O LEU A 152 N GLY A 128
SHEET 1 AA2 3 THR A 168 ALA A 173 0
SHEET 2 AA2 3 LYS A 198 LEU A 203 1 O ALA A 199 N VAL A 170
SHEET 3 AA2 3 ILE A 249 SER A 254 -1 O ARG A 253 N TYR A 200
SHEET 1 AA3 6 VAL B 24 VAL B 29 0
SHEET 2 AA3 6 GLY B 40 PRO B 45 -1 O ILE B 42 N THR B 27
SHEET 3 AA3 6 VAL B 82 ILE B 86 -1 O VAL B 83 N TYR B 43
SHEET 4 AA3 6 PHE B 53 SER B 59 1 N VAL B 56 O ILE B 84
SHEET 5 AA3 6 ILE B 119 HIS B 129 1 O MET B 127 N ALA B 57
SHEET 6 AA3 6 ALA B 148 LEU B 152 1 O LEU B 152 N GLY B 128
SHEET 1 AA4 3 THR B 168 ALA B 173 0
SHEET 2 AA4 3 LYS B 198 LEU B 203 1 O ALA B 199 N VAL B 170
SHEET 3 AA4 3 ILE B 249 SER B 254 -1 O ARG B 253 N TYR B 200
SSBOND 1 CYS A 241 CYS A 256 1555 1555 2.05
SSBOND 2 CYS B 241 CYS B 256 1555 1555 2.04
CISPEP 1 CYS A 241 PRO A 242 0 -4.32
CISPEP 2 CYS A 256 PRO A 257 0 -3.14
CISPEP 3 CYS B 241 PRO B 242 0 -7.49
CISPEP 4 CYS B 256 PRO B 257 0 -2.85
CRYST1 55.836 96.116 98.420 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 0.017910 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010404 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010161 0.00000
TER 1961 PHE A 258
TER 3941 PHE B 258
MASTER 342 0 0 22 18 0 0 6 4362 2 4 42
END |