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HEADER HYDROLASE 22-JUN-16 5LCN
TITLE STRUCTURE OF THE PYROCOCCUS FURIOSUS ESTERASE PF2001 WITH SPACE GROUP
TITLE 2 P212121
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS (STRAIN ATCC 43587 / DSM
SOURCE 3 3638 / JCM 8422 / VC1);
SOURCE 4 ORGANISM_TAXID: 186497;
SOURCE 5 STRAIN: ATCC 43587 / DSM 3638 / JCM 8422 / VC1;
SOURCE 6 GENE: PF2001;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, THEMOPHILIC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.VAREJAO,D.REVERTER
REVDAT 1 02-AUG-17 5LCN 0
JRNL AUTH N.VAREJAO,D.REVERTER
JRNL TITL STRUCTURE OF THE PYROCOCCUS FURIOSUS ESTERASE PF2001 WITH
JRNL TITL 2 SPACE GROUP P212121
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.9
REMARK 3 NUMBER OF REFLECTIONS : 38617
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1948
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 48.2558 - 6.2622 0.82 2610 144 0.1811 0.2204
REMARK 3 2 6.2622 - 4.9721 0.86 2623 121 0.1746 0.2218
REMARK 3 3 4.9721 - 4.3441 0.87 2608 139 0.1511 0.1915
REMARK 3 4 4.3441 - 3.9471 0.87 2596 148 0.1628 0.2231
REMARK 3 5 3.9471 - 3.6643 0.88 2611 146 0.1790 0.2416
REMARK 3 6 3.6643 - 3.4483 0.89 2641 136 0.1991 0.2751
REMARK 3 7 3.4483 - 3.2756 0.89 2658 130 0.2134 0.2817
REMARK 3 8 3.2756 - 3.1331 0.89 2625 150 0.2267 0.2933
REMARK 3 9 3.1331 - 3.0125 0.89 2601 146 0.2377 0.3309
REMARK 3 10 3.0125 - 2.9085 0.89 2651 134 0.2251 0.2618
REMARK 3 11 2.9085 - 2.8176 0.89 2617 145 0.2473 0.3832
REMARK 3 12 2.8176 - 2.7371 0.90 2660 147 0.2492 0.3320
REMARK 3 13 2.7371 - 2.6650 0.90 2659 133 0.2502 0.3187
REMARK 3 14 2.6650 - 2.6000 0.85 2509 129 0.2486 0.2951
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.100
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 : 0.003 8934
REMARK 3 ANGLE : 0.719 12083
REMARK 3 CHIRALITY : 0.028 1270
REMARK 3 PLANARITY : 0.004 1514
REMARK 3 DIHEDRAL : 12.725 3319
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 5LCN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1200000515.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
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 PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38776
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590
REMARK 200 RESOLUTION RANGE LOW (A) : 48.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.7
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 5G59
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 10% ETHYLENE GLYCOL, 0.1
REMARK 280 M HEPES SODIUM SALT, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 48.24750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.02450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.72000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.02450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.24750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.72000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 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 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 465 MET C 14
REMARK 465 HIS C 15
REMARK 465 HIS C 16
REMARK 465 HIS C 17
REMARK 465 HIS C 18
REMARK 465 HIS C 19
REMARK 465 LYS C 113
REMARK 465 GLY C 209
REMARK 465 ARG C 210
REMARK 465 PRO C 211
REMARK 465 MET D 14
REMARK 465 HIS D 15
REMARK 465 HIS D 16
REMARK 465 HIS D 17
REMARK 465 HIS D 18
REMARK 465 GLY D 209
REMARK 465 ARG D 210
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 311 O HOH A 329 1.99
REMARK 500 OD1 ASP C 119 NH1 ARG C 157 2.19
REMARK 500 O PRO A 174 O HOH A 301 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 SER A 77 -149.82 -113.27
REMARK 500 ALA A 81 100.00 -43.91
REMARK 500 TYR A 84 -30.68 -152.16
REMARK 500 THR A 116 -102.39 55.75
REMARK 500 SER A 149 -113.69 53.65
REMARK 500 PRO A 263 -158.20 -73.36
REMARK 500 VAL A 265 29.17 36.15
REMARK 500 SER B 77 -158.19 -122.74
REMARK 500 ALA B 81 103.70 -45.49
REMARK 500 TYR B 84 -31.57 -147.94
REMARK 500 THR B 116 -106.96 54.52
REMARK 500 SER B 140 48.86 -150.37
REMARK 500 SER B 149 -110.69 55.96
REMARK 500 PRO B 174 99.27 -67.21
REMARK 500 PRO B 192 151.39 -47.02
REMARK 500 GLU B 204 -133.27 -73.97
REMARK 500 VAL B 214 -7.72 -143.27
REMARK 500 PRO B 263 -157.34 -76.73
REMARK 500 VAL B 265 29.53 37.89
REMARK 500 SER C 77 -147.51 -125.16
REMARK 500 SER C 78 -157.75 -160.01
REMARK 500 ALA C 81 98.43 -55.26
REMARK 500 TYR C 84 -32.07 -153.88
REMARK 500 THR C 116 -134.62 50.73
REMARK 500 SER C 140 41.15 -144.71
REMARK 500 SER C 149 -119.13 56.73
REMARK 500 ASN C 213 92.33 -40.22
REMARK 500 ASP C 261 52.20 -111.16
REMARK 500 PRO C 263 -169.23 -68.04
REMARK 500 VAL C 265 31.49 36.63
REMARK 500 PHE C 271 74.17 -119.45
REMARK 500 HIS D 20 149.74 -170.06
REMARK 500 SER D 77 -152.33 -131.12
REMARK 500 TYR D 84 -28.13 -157.55
REMARK 500 VAL D 117 -167.86 -128.08
REMARK 500 ASP D 119 -38.05 -135.12
REMARK 500 SER D 149 -113.55 54.10
REMARK 500 PRO D 263 -162.65 -69.72
REMARK 500 VAL D 265 28.93 37.82
REMARK 500 PHE D 271 71.18 -118.83
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 1PE C 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE D 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G59 RELATED DB: PDB
REMARK 900 SIMILAR PROTEIN, DIFFERENT SPACE GROUP
DBREF 5LCN A 21 288 UNP Q8TZJ1 Q8TZJ1_PYRFU 21 288
DBREF 5LCN B 21 288 UNP Q8TZJ1 Q8TZJ1_PYRFU 21 288
DBREF 5LCN C 21 288 UNP Q8TZJ1 Q8TZJ1_PYRFU 21 288
DBREF 5LCN D 21 288 UNP Q8TZJ1 Q8TZJ1_PYRFU 21 288
SEQADV 5LCN MET A 14 UNP Q8TZJ1 INITIATING METHIONINE
SEQADV 5LCN HIS A 15 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS A 16 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS A 17 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS A 18 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS A 19 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS A 20 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN MET B 14 UNP Q8TZJ1 INITIATING METHIONINE
SEQADV 5LCN HIS B 15 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS B 16 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS B 17 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS B 18 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS B 19 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS B 20 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN MET C 14 UNP Q8TZJ1 INITIATING METHIONINE
SEQADV 5LCN HIS C 15 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS C 16 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS C 17 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS C 18 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS C 19 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS C 20 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN MET D 14 UNP Q8TZJ1 INITIATING METHIONINE
SEQADV 5LCN HIS D 15 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS D 16 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS D 17 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS D 18 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS D 19 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5LCN HIS D 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
SEQRES 1 C 275 MET HIS HIS HIS HIS HIS HIS GLY TYR LYS MET VAL ASN
SEQRES 2 C 275 PRO PRO ARG VAL VAL GLY ASN TRP THR PRO LYS ASP LEU
SEQRES 3 C 275 SER PHE GLU TYR LYS ASP VAL GLU ILE THR THR GLU ASP
SEQRES 4 C 275 ASN VAL LYS LEU SER GLY TRP TRP ILE ASP ASN GLY SER
SEQRES 5 C 275 ASP LYS THR VAL ILE PRO LEU HIS GLY TYR THR SER SER
SEQRES 6 C 275 ARG TRP ALA GLU HIS TYR MET ARG PRO VAL ILE GLU PHE
SEQRES 7 C 275 LEU LEU LYS GLU GLY TYR ASN VAL LEU ALA PHE ASP PHE
SEQRES 8 C 275 ARG ALA HIS GLY LYS SER GLY GLY LYS TYR THR THR VAL
SEQRES 9 C 275 GLY ASP LYS GLU ILE LEU ASP LEU LYS ALA GLY VAL LYS
SEQRES 10 C 275 TRP LEU LYS ASP ASN TYR PRO GLU LYS SER LYS ARG ILE
SEQRES 11 C 275 GLY VAL ILE GLY PHE SER MET GLY ALA LEU VAL ALA ILE
SEQRES 12 C 275 ARG GLY LEU SER GLU VAL LYS GLU ILE CYS CYS GLY VAL
SEQRES 13 C 275 ALA ASP SER PRO PRO ILE TYR LEU ASP LYS THR GLY ALA
SEQRES 14 C 275 ARG GLY MET LYS TYR PHE ALA LYS LEU PRO GLU TRP LEU
SEQRES 15 C 275 TYR SER PHE VAL LYS PRO PHE SER GLU LEU PHE SER GLY
SEQRES 16 C 275 GLY ARG PRO ILE ASN VAL LEU ASN TYR THR ASN SER ILE
SEQRES 17 C 275 LYS LYS PRO LEU PHE LEU ILE ILE GLY ARG ARG ASP THR
SEQRES 18 C 275 LEU VAL LYS VAL GLU GLU VAL GLN GLU PHE TYR GLU ARG
SEQRES 19 C 275 ASN LYS HIS VAL ASN PRO ASN VAL GLU LEU TRP VAL THR
SEQRES 20 C 275 ASP ALA PRO HIS VAL ARG THR ILE GLN VAL PHE PRO GLU
SEQRES 21 C 275 GLU TRP LYS SER ARG VAL GLY GLU PHE LEU LYS ARG TRP
SEQRES 22 C 275 MET GLY
SEQRES 1 D 275 MET HIS HIS HIS HIS HIS HIS GLY TYR LYS MET VAL ASN
SEQRES 2 D 275 PRO PRO ARG VAL VAL GLY ASN TRP THR PRO LYS ASP LEU
SEQRES 3 D 275 SER PHE GLU TYR LYS ASP VAL GLU ILE THR THR GLU ASP
SEQRES 4 D 275 ASN VAL LYS LEU SER GLY TRP TRP ILE ASP ASN GLY SER
SEQRES 5 D 275 ASP LYS THR VAL ILE PRO LEU HIS GLY TYR THR SER SER
SEQRES 6 D 275 ARG TRP ALA GLU HIS TYR MET ARG PRO VAL ILE GLU PHE
SEQRES 7 D 275 LEU LEU LYS GLU GLY TYR ASN VAL LEU ALA PHE ASP PHE
SEQRES 8 D 275 ARG ALA HIS GLY LYS SER GLY GLY LYS TYR THR THR VAL
SEQRES 9 D 275 GLY ASP LYS GLU ILE LEU ASP LEU LYS ALA GLY VAL LYS
SEQRES 10 D 275 TRP LEU LYS ASP ASN TYR PRO GLU LYS SER LYS ARG ILE
SEQRES 11 D 275 GLY VAL ILE GLY PHE SER MET GLY ALA LEU VAL ALA ILE
SEQRES 12 D 275 ARG GLY LEU SER GLU VAL LYS GLU ILE CYS CYS GLY VAL
SEQRES 13 D 275 ALA ASP SER PRO PRO ILE TYR LEU ASP LYS THR GLY ALA
SEQRES 14 D 275 ARG GLY MET LYS TYR PHE ALA LYS LEU PRO GLU TRP LEU
SEQRES 15 D 275 TYR SER PHE VAL LYS PRO PHE SER GLU LEU PHE SER GLY
SEQRES 16 D 275 GLY ARG PRO ILE ASN VAL LEU ASN TYR THR ASN SER ILE
SEQRES 17 D 275 LYS LYS PRO LEU PHE LEU ILE ILE GLY ARG ARG ASP THR
SEQRES 18 D 275 LEU VAL LYS VAL GLU GLU VAL GLN GLU PHE TYR GLU ARG
SEQRES 19 D 275 ASN LYS HIS VAL ASN PRO ASN VAL GLU LEU TRP VAL THR
SEQRES 20 D 275 ASP ALA PRO HIS VAL ARG THR ILE GLN VAL PHE PRO GLU
SEQRES 21 D 275 GLU TRP LYS SER ARG VAL GLY GLU PHE LEU LYS ARG TRP
SEQRES 22 D 275 MET GLY
HET 1PE C 300 16
HET 1PE D 300 16
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 5 1PE 2(C10 H22 O6)
FORMUL 7 HOH *82(H2 O)
HELIX 1 AA1 THR A 35 SER A 40 5 6
HELIX 2 AA2 TYR A 84 GLY A 96 1 13
HELIX 3 AA3 LYS A 120 TYR A 136 1 17
HELIX 4 AA4 SER A 149 VAL A 162 1 14
HELIX 5 AA5 TYR A 176 MET A 185 1 10
HELIX 6 AA6 LYS A 186 ALA A 189 5 4
HELIX 7 AA7 PRO A 192 SER A 197 1 6
HELIX 8 AA8 VAL A 199 GLY A 208 1 10
HELIX 9 AA9 ASN A 213 THR A 218 5 6
HELIX 10 AB1 LYS A 237 LYS A 249 1 13
HELIX 11 AB2 ARG A 266 PHE A 271 1 6
HELIX 12 AB3 PHE A 271 MET A 287 1 17
HELIX 13 AB4 THR B 35 SER B 40 5 6
HELIX 14 AB5 TYR B 84 GLY B 96 1 13
HELIX 15 AB6 LYS B 120 TYR B 136 1 17
HELIX 16 AB7 PRO B 137 SER B 140 5 4
HELIX 17 AB8 SER B 149 VAL B 162 1 14
HELIX 18 AB9 TYR B 176 ALA B 189 1 14
HELIX 19 AC1 PRO B 192 LYS B 200 1 9
HELIX 20 AC2 PRO B 201 SER B 203 5 3
HELIX 21 AC3 VAL B 214 ASN B 219 5 6
HELIX 22 AC4 LYS B 237 LYS B 249 1 13
HELIX 23 AC5 ARG B 266 PHE B 271 1 6
HELIX 24 AC6 PHE B 271 MET B 287 1 17
HELIX 25 AC7 THR C 35 SER C 40 5 6
HELIX 26 AC8 TYR C 84 GLY C 96 1 13
HELIX 27 AC9 LYS C 120 TYR C 136 1 17
HELIX 28 AD1 PRO C 137 LYS C 141 5 5
HELIX 29 AD2 SER C 149 VAL C 162 1 14
HELIX 30 AD3 TYR C 176 ALA C 189 1 14
HELIX 31 AD4 PRO C 192 PHE C 206 1 15
HELIX 32 AD5 ASN C 213 LEU C 215 5 3
HELIX 33 AD6 ASN C 216 ILE C 221 1 6
HELIX 34 AD7 LYS C 237 LYS C 249 1 13
HELIX 35 AD8 ARG C 266 PHE C 271 1 6
HELIX 36 AD9 PHE C 271 MET C 287 1 17
HELIX 37 AE1 THR D 35 SER D 40 5 6
HELIX 38 AE2 TYR D 84 GLU D 95 1 12
HELIX 39 AE3 LYS D 120 TYR D 136 1 17
HELIX 40 AE4 PRO D 137 SER D 140 5 4
HELIX 41 AE5 SER D 149 VAL D 162 1 14
HELIX 42 AE6 TYR D 176 ALA D 189 1 14
HELIX 43 AE7 PRO D 192 PHE D 206 1 15
HELIX 44 AE8 VAL D 214 ASN D 219 5 6
HELIX 45 AE9 LYS D 237 ARG D 247 1 11
HELIX 46 AF1 ARG D 266 PHE D 271 1 6
HELIX 47 AF2 GLU D 273 GLY D 288 1 16
SHEET 1 AA1 2 TYR A 22 ASN A 26 0
SHEET 2 AA1 2 ARG C 29 GLY C 32 -1 O ARG C 29 N ASN A 26
SHEET 1 AA2 2 VAL A 30 GLY A 32 0
SHEET 2 AA2 2 TYR C 22 VAL C 25 -1 O MET C 24 N VAL A 31
SHEET 1 AA3 8 LYS A 44 THR A 49 0
SHEET 2 AA3 8 LYS A 55 ILE A 61 -1 O LEU A 56 N ILE A 48
SHEET 3 AA3 8 ASN A 98 PHE A 102 -1 O ALA A 101 N TRP A 59
SHEET 4 AA3 8 LYS A 67 LEU A 72 1 N VAL A 69 O ASN A 98
SHEET 5 AA3 8 ARG A 142 PHE A 148 1 O ILE A 146 N LEU A 72
SHEET 6 AA3 8 ILE A 165 ASP A 171 1 O ASP A 171 N GLY A 147
SHEET 7 AA3 8 LEU A 225 GLY A 230 1 O PHE A 226 N ALA A 170
SHEET 8 AA3 8 VAL A 255 THR A 260 1 O GLU A 256 N LEU A 225
SHEET 1 AA4 2 TYR B 22 ASN B 26 0
SHEET 2 AA4 2 ARG D 29 GLY D 32 -1 O ARG D 29 N ASN B 26
SHEET 1 AA5 2 VAL B 30 VAL B 31 0
SHEET 2 AA5 2 MET D 24 VAL D 25 -1 O MET D 24 N VAL B 31
SHEET 1 AA6 8 LYS B 44 THR B 49 0
SHEET 2 AA6 8 LYS B 55 ILE B 61 -1 O LEU B 56 N ILE B 48
SHEET 3 AA6 8 ASN B 98 PHE B 102 -1 O ALA B 101 N TRP B 59
SHEET 4 AA6 8 LYS B 67 LEU B 72 1 N LYS B 67 O ASN B 98
SHEET 5 AA6 8 ARG B 142 PHE B 148 1 O ILE B 146 N LEU B 72
SHEET 6 AA6 8 CYS B 167 ASP B 171 1 O VAL B 169 N GLY B 147
SHEET 7 AA6 8 LEU B 225 GLY B 230 1 O ILE B 228 N ALA B 170
SHEET 8 AA6 8 VAL B 255 THR B 260 1 O TRP B 258 N LEU B 227
SHEET 1 AA7 8 LYS C 44 THR C 49 0
SHEET 2 AA7 8 LYS C 55 ILE C 61 -1 O LEU C 56 N ILE C 48
SHEET 3 AA7 8 ASN C 98 PHE C 102 -1 O VAL C 99 N ILE C 61
SHEET 4 AA7 8 LYS C 67 LEU C 72 1 N LYS C 67 O ASN C 98
SHEET 5 AA7 8 ARG C 142 PHE C 148 1 O ILE C 146 N LEU C 72
SHEET 6 AA7 8 ILE C 165 ASP C 171 1 O VAL C 169 N VAL C 145
SHEET 7 AA7 8 LEU C 225 GLY C 230 1 O PHE C 226 N ALA C 170
SHEET 8 AA7 8 VAL C 255 THR C 260 1 O GLU C 256 N LEU C 225
SHEET 1 AA8 8 LYS D 44 THR D 49 0
SHEET 2 AA8 8 LYS D 55 ILE D 61 -1 O LEU D 56 N ILE D 48
SHEET 3 AA8 8 ASN D 98 PHE D 102 -1 O VAL D 99 N ILE D 61
SHEET 4 AA8 8 LYS D 67 LEU D 72 1 N LYS D 67 O ASN D 98
SHEET 5 AA8 8 ARG D 142 PHE D 148 1 O ILE D 146 N LEU D 72
SHEET 6 AA8 8 CYS D 167 ASP D 171 1 O VAL D 169 N VAL D 145
SHEET 7 AA8 8 LEU D 225 GLY D 230 1 O PHE D 226 N ALA D 170
SHEET 8 AA8 8 VAL D 255 THR D 260 1 O GLU D 256 N LEU D 225
CISPEP 1 HIS D 20 GLY D 21 0 -2.28
SITE 1 AC1 7 TRP A 194 SER C 149 PHE C 206 LEU C 235
SITE 2 AC1 7 HIS C 264 VAL C 265 ARG C 266
SITE 1 AC2 9 TRP B 194 SER D 149 GLY D 181 GLY D 184
SITE 2 AC2 9 SER D 203 PHE D 206 LEU D 235 HIS D 264
SITE 3 AC2 9 VAL D 265
CRYST1 96.495 99.440 146.049 90.00 90.00 90.00 P 21 21 21 16
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 0.010363 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010056 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006847 0.00000
TER 2177 GLY A 288
TER 4311 GLY B 288
TER 6467 GLY C 288
TER 8649 GLY D 288
MASTER 342 0 2 47 40 0 5 6 8759 4 32 88
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