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HEADER HYDROLASE 26-MAY-16 5G5M
TITLE STRUCTURE OF THE PYROCOCCUS FURIOSUS ESTERASE PF2001 WITH SPACE GROUP
TITLE 2 P21
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS HYDROLASE, ESTERASE, THEMOPHILIC
EXPDTA X-RAY DIFFRACTION
AUTHOR N.VAREJAO,D.REVERTER
REVDAT 1 21-JUN-17 5G5M 0
JRNL AUTH N.VAREJAO,R.V.ALMEIDA,D.REVERTER
JRNL TITL STRUCTURAL BASIS FOR THE SUBSTRATE CHANNEL FORMATION UPON
JRNL TITL 2 DIMERIZATION OF THE HYPERTHERMOPHILIC PF2001 ESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 32511
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) : 0.186
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1603
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 70.8690 - 4.6033 0.98 2812 168 0.1397 0.1719
REMARK 3 2 4.6033 - 3.6538 0.98 2831 143 0.1497 0.2006
REMARK 3 3 3.6538 - 3.1919 0.99 2807 142 0.1910 0.2447
REMARK 3 4 3.1919 - 2.9001 0.99 2807 153 0.2184 0.2707
REMARK 3 5 2.9001 - 2.6922 0.99 2793 166 0.2196 0.2858
REMARK 3 6 2.6922 - 2.5335 0.99 2809 144 0.2214 0.2918
REMARK 3 7 2.5335 - 2.4066 0.99 2814 127 0.2141 0.2842
REMARK 3 8 2.4066 - 2.3018 0.99 2816 117 0.2249 0.2707
REMARK 3 9 2.3018 - 2.2132 0.99 2814 136 0.2247 0.2631
REMARK 3 10 2.2132 - 2.1368 0.99 2840 137 0.2322 0.3326
REMARK 3 11 2.1368 - 2.0700 0.99 2765 170 0.2506 0.2943
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.190
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1632 -8.9199 170.2836
REMARK 3 T TENSOR
REMARK 3 T11: 0.2404 T22: 0.2016
REMARK 3 T33: 0.2272 T12: -0.0126
REMARK 3 T13: -0.0730 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 1.3728 L22: 0.7353
REMARK 3 L33: 2.3852 L12: -0.3069
REMARK 3 L13: -1.6159 L23: 0.2632
REMARK 3 S TENSOR
REMARK 3 S11: -0.1353 S12: -0.0924 S13: -0.0615
REMARK 3 S21: 0.1550 S22: 0.0555 S23: 0.0220
REMARK 3 S31: 0.1830 S32: 0.1717 S33: 0.0673
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 5G5M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1290066952.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PIXEL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32672
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 70.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.70000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
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: PDB ENTRY 5G59
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 10% ETHYLENE GLYCOL, 0.1
REMARK 280 M HEPES PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 38.72100
REMARK 290 SMTRY3 2 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: 2240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.6 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 MET A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 GLY A 21
REMARK 465 TYR A 22
REMARK 465 LYS A 23
REMARK 465 MET A 24
REMARK 465 VAL A 25
REMARK 465 GLU A 204
REMARK 465 LEU A 205
REMARK 465 PHE A 206
REMARK 465 SER A 207
REMARK 465 GLY A 208
REMARK 465 GLY A 209
REMARK 465 ARG A 210
REMARK 465 PRO A 211
REMARK 465 ILE A 212
REMARK 465 ASN A 213
REMARK 465 MET B 14
REMARK 465 HIS B 15
REMARK 465 HIS B 16
REMARK 465 HIS B 17
REMARK 465 HIS B 18
REMARK 465 HIS B 19
REMARK 465 HIS B 20
REMARK 465 GLY B 21
REMARK 465 TYR B 22
REMARK 465 LYS B 23
REMARK 465 MET B 24
REMARK 465 LEU B 205
REMARK 465 PHE B 206
REMARK 465 SER B 207
REMARK 465 GLY B 208
REMARK 465 GLY B 209
REMARK 465 ARG B 210
REMARK 465 PRO B 211
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 2017 O HOH B 2032 2.09
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 PRO A 28 C - N - CD ANGL. DEV. = -16.4 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 SER A 77 -157.58 -102.42
REMARK 500 ALA A 81 111.82 -38.04
REMARK 500 TYR A 84 -37.47 -146.83
REMARK 500 ASP A 119 -82.13 -69.93
REMARK 500 SER A 149 -123.76 56.89
REMARK 500 VAL A 265 22.28 39.23
REMARK 500 SER B 77 -157.31 -106.95
REMARK 500 TYR B 84 -34.24 -146.91
REMARK 500 VAL B 117 41.11 38.22
REMARK 500 ASP B 119 -80.15 -84.10
REMARK 500 SER B 140 46.68 -145.77
REMARK 500 SER B 149 -125.19 59.67
REMARK 500 VAL B 265 22.66 37.48
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 QRL A 1289
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5G59 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE PYROCOCCUS FURIOSUS ESTERASE PF2001 WITH SPACE
REMARK 900 GROUP P3121
REMARK 900 RELATED ID: 5G5C RELATED DB: PDB
REMARK 900 STRUCTURE OF THE PYROCOCCUS FURIOSUS ESTERASE PF2001 WITH SPACE
REMARK 900 GROUP C2221
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 DELETION OF THE 20 FIRST RESIDUES
DBREF 5G5M A 21 288 UNP Q8TZJ1 Q8TZJ1_PYRFU 21 288
DBREF 5G5M B 21 288 UNP Q8TZJ1 Q8TZJ1_PYRFU 21 288
SEQADV 5G5M MET A 14 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS A 15 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS A 16 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS A 17 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS A 18 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS A 19 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS A 20 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M MET B 14 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS B 15 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS B 16 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS B 17 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS B 18 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS B 19 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5M HIS B 20 UNP Q8TZJ1 EXPRESSION TAG
SEQRES 1 A 275 MET HIS HIS HIS HIS HIS HIS GLY TYR LYS MET VAL ASN
SEQRES 2 A 275 PRO PRO ARG VAL VAL GLY ASN TRP THR PRO LYS ASP LEU
SEQRES 3 A 275 SER PHE GLU TYR LYS ASP VAL GLU ILE THR THR GLU ASP
SEQRES 4 A 275 ASN VAL LYS LEU SER GLY TRP TRP ILE ASP ASN GLY SER
SEQRES 5 A 275 ASP LYS THR VAL ILE PRO LEU HIS GLY TYR THR SER SER
SEQRES 6 A 275 ARG TRP ALA GLU HIS TYR MET ARG PRO VAL ILE GLU PHE
SEQRES 7 A 275 LEU LEU LYS GLU GLY TYR ASN VAL LEU ALA PHE ASP PHE
SEQRES 8 A 275 ARG ALA HIS GLY LYS SER GLY GLY LYS TYR THR THR VAL
SEQRES 9 A 275 GLY ASP LYS GLU ILE LEU ASP LEU LYS ALA GLY VAL LYS
SEQRES 10 A 275 TRP LEU LYS ASP ASN TYR PRO GLU LYS SER LYS ARG ILE
SEQRES 11 A 275 GLY VAL ILE GLY PHE SER MET GLY ALA LEU VAL ALA ILE
SEQRES 12 A 275 ARG GLY LEU SER GLU VAL LYS GLU ILE CYS CYS GLY VAL
SEQRES 13 A 275 ALA ASP SER PRO PRO ILE TYR LEU ASP LYS THR GLY ALA
SEQRES 14 A 275 ARG GLY MET LYS TYR PHE ALA LYS LEU PRO GLU TRP LEU
SEQRES 15 A 275 TYR SER PHE VAL LYS PRO PHE SER GLU LEU PHE SER GLY
SEQRES 16 A 275 GLY ARG PRO ILE ASN VAL LEU ASN TYR THR ASN SER ILE
SEQRES 17 A 275 LYS LYS PRO LEU PHE LEU ILE ILE GLY ARG ARG ASP THR
SEQRES 18 A 275 LEU VAL LYS VAL GLU GLU VAL GLN GLU PHE TYR GLU ARG
SEQRES 19 A 275 ASN LYS HIS VAL ASN PRO ASN VAL GLU LEU TRP VAL THR
SEQRES 20 A 275 ASP ALA PRO HIS VAL ARG THR ILE GLN VAL PHE PRO GLU
SEQRES 21 A 275 GLU TRP LYS SER ARG VAL GLY GLU PHE LEU LYS ARG TRP
SEQRES 22 A 275 MET GLY
SEQRES 1 B 275 MET HIS HIS HIS HIS HIS HIS GLY TYR LYS MET VAL ASN
SEQRES 2 B 275 PRO PRO ARG VAL VAL GLY ASN TRP THR PRO LYS ASP LEU
SEQRES 3 B 275 SER PHE GLU TYR LYS ASP VAL GLU ILE THR THR GLU ASP
SEQRES 4 B 275 ASN VAL LYS LEU SER GLY TRP TRP ILE ASP ASN GLY SER
SEQRES 5 B 275 ASP LYS THR VAL ILE PRO LEU HIS GLY TYR THR SER SER
SEQRES 6 B 275 ARG TRP ALA GLU HIS TYR MET ARG PRO VAL ILE GLU PHE
SEQRES 7 B 275 LEU LEU LYS GLU GLY TYR ASN VAL LEU ALA PHE ASP PHE
SEQRES 8 B 275 ARG ALA HIS GLY LYS SER GLY GLY LYS TYR THR THR VAL
SEQRES 9 B 275 GLY ASP LYS GLU ILE LEU ASP LEU LYS ALA GLY VAL LYS
SEQRES 10 B 275 TRP LEU LYS ASP ASN TYR PRO GLU LYS SER LYS ARG ILE
SEQRES 11 B 275 GLY VAL ILE GLY PHE SER MET GLY ALA LEU VAL ALA ILE
SEQRES 12 B 275 ARG GLY LEU SER GLU VAL LYS GLU ILE CYS CYS GLY VAL
SEQRES 13 B 275 ALA ASP SER PRO PRO ILE TYR LEU ASP LYS THR GLY ALA
SEQRES 14 B 275 ARG GLY MET LYS TYR PHE ALA LYS LEU PRO GLU TRP LEU
SEQRES 15 B 275 TYR SER PHE VAL LYS PRO PHE SER GLU LEU PHE SER GLY
SEQRES 16 B 275 GLY ARG PRO ILE ASN VAL LEU ASN TYR THR ASN SER ILE
SEQRES 17 B 275 LYS LYS PRO LEU PHE LEU ILE ILE GLY ARG ARG ASP THR
SEQRES 18 B 275 LEU VAL LYS VAL GLU GLU VAL GLN GLU PHE TYR GLU ARG
SEQRES 19 B 275 ASN LYS HIS VAL ASN PRO ASN VAL GLU LEU TRP VAL THR
SEQRES 20 B 275 ASP ALA PRO HIS VAL ARG THR ILE GLN VAL PHE PRO GLU
SEQRES 21 B 275 GLU TRP LYS SER ARG VAL GLY GLU PHE LEU LYS ARG TRP
SEQRES 22 B 275 MET GLY
HET QRL A1289 9
HETNAM QRL S-METHYL HEXANETHIOATE
FORMUL 3 QRL C7 H14 O S
FORMUL 4 HOH *88(H2 O)
HELIX 1 1 THR A 35 SER A 40 5 6
HELIX 2 2 TYR A 84 GLU A 95 1 12
HELIX 3 3 LYS A 120 TYR A 136 1 17
HELIX 4 4 PRO A 137 SER A 140 5 4
HELIX 5 5 SER A 149 VAL A 162 1 14
HELIX 6 6 TYR A 176 ALA A 189 1 14
HELIX 7 7 PRO A 192 LYS A 200 1 9
HELIX 8 8 PRO A 201 SER A 203 5 3
HELIX 9 9 VAL A 214 SER A 220 5 7
HELIX 10 10 LYS A 237 LYS A 249 1 13
HELIX 11 11 ARG A 266 PHE A 271 1 6
HELIX 12 12 PHE A 271 GLY A 288 1 18
HELIX 13 13 THR B 35 SER B 40 5 6
HELIX 14 14 TYR B 84 GLY B 96 1 13
HELIX 15 15 LYS B 120 TYR B 136 1 17
HELIX 16 16 PRO B 137 SER B 140 5 4
HELIX 17 17 SER B 149 VAL B 162 1 14
HELIX 18 18 TYR B 176 LYS B 186 1 11
HELIX 19 19 PRO B 192 LYS B 200 1 9
HELIX 20 20 PRO B 201 GLU B 204 5 4
HELIX 21 21 ASN B 213 SER B 220 5 8
HELIX 22 22 LYS B 237 LYS B 249 1 13
HELIX 23 23 ARG B 266 PHE B 271 1 6
HELIX 24 24 PHE B 271 GLY B 288 1 18
SHEET 1 AA 8 LYS A 44 THR A 49 0
SHEET 2 AA 8 LYS A 55 ILE A 61 -1 O LEU A 56 N ILE A 48
SHEET 3 AA 8 ASN A 98 PHE A 102 -1 O VAL A 99 N ILE A 61
SHEET 4 AA 8 LYS A 67 LEU A 72 1 O LYS A 67 N ASN A 98
SHEET 5 AA 8 ARG A 142 PHE A 148 1 O ARG A 142 N THR A 68
SHEET 6 AA 8 ILE A 165 ASP A 171 1 N CYS A 166 O ILE A 143
SHEET 7 AA 8 LEU A 225 GLY A 230 1 O PHE A 226 N ALA A 170
SHEET 8 AA 8 VAL A 255 THR A 260 1 O GLU A 256 N LEU A 227
SHEET 1 BA 8 LYS B 44 THR B 49 0
SHEET 2 BA 8 LYS B 55 ILE B 61 -1 O LEU B 56 N ILE B 48
SHEET 3 BA 8 ASN B 98 PHE B 102 -1 O VAL B 99 N ILE B 61
SHEET 4 BA 8 LYS B 67 LEU B 72 1 O LYS B 67 N ASN B 98
SHEET 5 BA 8 ARG B 142 PHE B 148 1 O ARG B 142 N THR B 68
SHEET 6 BA 8 ILE B 165 ASP B 171 1 N CYS B 166 O ILE B 143
SHEET 7 BA 8 LEU B 225 GLY B 230 1 O PHE B 226 N ALA B 170
SHEET 8 BA 8 VAL B 255 THR B 260 1 O GLU B 256 N LEU B 227
CISPEP 1 LEU B 191 PRO B 192 0 -3.90
SITE 1 AC1 6 GLY A 74 HIS A 83 TYR A 84 HIS A 264
SITE 2 AC1 6 VAL A 265 ARG A 266
CRYST1 49.859 77.442 70.878 90.00 92.16 90.00 P 1 21 1 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 0.020057 0.000000 0.000756 0.00000
SCALE2 0.000000 0.012913 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014119 0.00000
TER 2065 GLY A 288
TER 4159 GLY B 288
MASTER 331 0 1 24 16 0 2 6 4251 2 9 44
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