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HEADER HYDROLASE 05-MAY-25 9UTY
TITLE THE STRUCTURE OF THE D197K MUTANT OF PES-H1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PES-H1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PES-H1;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 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;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 8 ORGANISM_TAXID: 256318;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 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 9UTY 0
JRNL AUTH W.XIE,A.LIU
JRNL TITL RATIONAL DESIGN OF THE POLYETHYLENE TEREPHTHALATE-DEGRADING
JRNL TITL 2 ENZYME PES-H1 WITH LOW SALT TOLERANCE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 54399
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880
REMARK 3 FREE R VALUE TEST SET COUNT : 2657
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 34.4600 - 4.6700 1.00 2907 158 0.1774 0.2128
REMARK 3 2 4.6600 - 3.7100 1.00 2812 131 0.1328 0.1237
REMARK 3 3 3.7000 - 3.2400 1.00 2767 145 0.1387 0.1541
REMARK 3 4 3.2400 - 2.9400 1.00 2754 126 0.1507 0.1909
REMARK 3 5 2.9400 - 2.7300 1.00 2743 142 0.1569 0.1659
REMARK 3 6 2.7300 - 2.5700 1.00 2697 165 0.1541 0.2177
REMARK 3 7 2.5700 - 2.4400 1.00 2711 144 0.1543 0.1863
REMARK 3 8 2.4400 - 2.3300 1.00 2716 135 0.1518 0.1883
REMARK 3 9 2.3300 - 2.2400 1.00 2705 144 0.1504 0.1851
REMARK 3 10 2.2400 - 2.1700 1.00 2716 137 0.1543 0.1616
REMARK 3 11 2.1700 - 2.1000 1.00 2683 144 0.1568 0.1952
REMARK 3 12 2.1000 - 2.0400 1.00 2718 147 0.1660 0.1994
REMARK 3 13 2.0400 - 1.9900 1.00 2668 138 0.1586 0.1927
REMARK 3 14 1.9900 - 1.9400 1.00 2684 152 0.1669 0.1899
REMARK 3 15 1.9400 - 1.8900 1.00 2714 122 0.1849 0.2115
REMARK 3 16 1.8900 - 1.8500 1.00 2694 137 0.1914 0.2465
REMARK 3 17 1.8500 - 1.8200 1.00 2675 136 0.2136 0.2302
REMARK 3 18 1.8200 - 1.7800 1.00 2720 130 0.2567 0.3125
REMARK 3 19 1.7800 - 1.7500 1.00 2658 124 0.3217 0.3279
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.300
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 4026
REMARK 3 ANGLE : 0.854 5494
REMARK 3 CHIRALITY : 0.053 611
REMARK 3 PLANARITY : 0.010 730
REMARK 3 DIHEDRAL : 13.533 1448
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 9UTY 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_1300059151.
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 : 54478
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 49.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.80
REMARK 200 R MERGE (I) : 0.17100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.25300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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 (%): 47.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
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 27.94500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.37000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.13500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.37000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.94500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.13500
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: 1260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18930 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 SER 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 470 MET B 0 CG SD CE
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 OE1 GLU A 202 O HOH A 301 1.92
REMARK 500 O HOH A 324 O HOH A 477 2.01
REMARK 500 OE2 GLU A 186 O HOH A 301 2.04
REMARK 500 O HOH A 475 O HOH B 476 2.05
REMARK 500 O HOH A 384 O HOH A 474 2.05
REMARK 500 O HOH A 304 O HOH A 339 2.07
REMARK 500 O HOH A 318 O HOH A 353 2.10
REMARK 500 O HOH A 309 O HOH A 401 2.11
REMARK 500 O HOH B 329 O HOH B 370 2.13
REMARK 500 O HOH A 451 O HOH A 492 2.13
REMARK 500 O HOH B 484 O HOH B 498 2.14
REMARK 500 OD2 ASP A 96 O HOH A 302 2.16
REMARK 500 O HOH B 342 O HOH B 435 2.16
REMARK 500 O HOH B 491 O HOH B 496 2.17
REMARK 500 O HOH A 505 O HOH B 494 2.18
REMARK 500 O HOH A 477 O HOH A 495 2.18
REMARK 500 O HOH A 480 O HOH A 484 2.19
REMARK 500 O HOH A 437 O HOH A 489 2.19
REMARK 500 O HOH A 370 O HOH A 446 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 356 O HOH B 458 2655 2.16
REMARK 500 O HOH A 488 O HOH B 484 2655 2.18
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 -3.81 70.38
REMARK 500 SER A 130 -116.62 53.47
REMARK 500 HIS A 184 -92.98 -120.48
REMARK 500 PRO A 242 -154.76 -85.26
REMARK 500 THR B 63 -1.46 62.68
REMARK 500 SER B 130 -122.87 61.57
REMARK 500 ASN B 143 93.77 -160.43
REMARK 500 HIS B 184 -93.52 -119.90
REMARK 500 PRO B 242 -141.05 -81.98
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 B 98 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9UTY A -3 258 PDB 9UTY 9UTY -3 258
DBREF 9UTY B -3 258 PDB 9UTY 9UTY -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 GLU 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 GLN 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 SER 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 GLU 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 GLN 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 *405(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 LEU A 240 5 8
HELIX 11 AB2 THR B 11 ALA B 17 1 7
HELIX 12 AB3 GLY B 65 ALA B 70 5 6
HELIX 13 AB4 TRP B 71 SER B 78 1 8
HELIX 14 AB5 GLN B 94 ARG B 110 1 17
HELIX 15 AB6 SER B 130 ASN B 142 1 13
HELIX 16 AB7 HIS B 184 LEU B 192 1 9
HELIX 17 AB8 SER B 207 THR B 213 5 7
HELIX 18 AB9 ASP B 215 ASP B 231 1 17
HELIX 19 AC1 ASP B 233 ARG B 235 5 3
HELIX 20 AC2 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 ILE A 42 N THR A 27
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 ILE A 84
SHEET 5 AA1 6 ILE A 119 HIS A 129 1 O ASP A 120 N PHE A 53
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 2.04
SSBOND 2 CYS B 241 CYS B 256 1555 1555 2.04
CISPEP 1 CYS A 241 PRO A 242 0 -2.68
CISPEP 2 CYS A 256 PRO A 257 0 -1.47
CISPEP 3 CYS B 241 PRO B 242 0 -9.81
CISPEP 4 CYS B 256 PRO B 257 0 -2.71
CRYST1 55.890 96.270 98.740 90.00 90.00 90.00 P 21 21 21 4
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 0.017892 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010387 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010128 0.00000
TER 1961 PHE A 258
TER 3933 PHE B 258
MASTER 323 0 0 20 18 0 0 6 4333 2 4 42
END |