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HEADER STRUCTURAL PROTEIN 23-MAY-16 5G5C
TITLE STRUCTURE OF THE PYROCOCCUS FURIOSUS ESTERASE PF2001 WITH SPACE GROUP
TITLE 2 C2221
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: YES, UNP RESIDUES 21-288;
COMPND 5 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 STRUCTURAL PROTEIN, ESTERASE, THEMOPHILIC
EXPDTA X-RAY DIFFRACTION
AUTHOR N.VAREJAO,D.REVERTER
REVDAT 1 21-JUN-17 5G5C 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. 1.18 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) : 1.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.44
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 79503
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3863
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 40.4616 - 3.5824 1.00 2887 146 0.1619 0.1814
REMARK 3 2 3.5824 - 2.8437 1.00 2767 149 0.1773 0.1807
REMARK 3 3 2.8437 - 2.4843 1.00 2743 143 0.1810 0.2196
REMARK 3 4 2.4843 - 2.2571 1.00 2765 115 0.1766 0.1776
REMARK 3 5 2.2571 - 2.0954 1.00 2708 136 0.1745 0.1702
REMARK 3 6 2.0954 - 1.9718 1.00 2750 124 0.1681 0.1988
REMARK 3 7 1.9718 - 1.8731 1.00 2710 144 0.1666 0.1758
REMARK 3 8 1.8731 - 1.7916 1.00 2710 147 0.1720 0.1958
REMARK 3 9 1.7916 - 1.7226 1.00 2696 129 0.1738 0.1853
REMARK 3 10 1.7226 - 1.6631 1.00 2692 142 0.1727 0.1797
REMARK 3 11 1.6631 - 1.6111 1.00 2709 134 0.1711 0.1709
REMARK 3 12 1.6111 - 1.5651 1.00 2670 131 0.1690 0.2119
REMARK 3 13 1.5651 - 1.5239 1.00 2720 127 0.1719 0.1850
REMARK 3 14 1.5239 - 1.4867 1.00 2695 129 0.1753 0.1925
REMARK 3 15 1.4867 - 1.4529 1.00 2681 134 0.1762 0.1912
REMARK 3 16 1.4529 - 1.4220 1.00 2698 139 0.1806 0.1871
REMARK 3 17 1.4220 - 1.3935 1.00 2695 135 0.1870 0.1811
REMARK 3 18 1.3935 - 1.3672 1.00 2654 141 0.1868 0.1851
REMARK 3 19 1.3672 - 1.3428 1.00 2692 152 0.1913 0.2035
REMARK 3 20 1.3428 - 1.3200 1.00 2641 138 0.1959 0.2368
REMARK 3 21 1.3200 - 1.2988 1.00 2698 149 0.1980 0.2055
REMARK 3 22 1.2988 - 1.2788 1.00 2658 127 0.2013 0.2491
REMARK 3 23 1.2788 - 1.2600 1.00 2678 152 0.2138 0.2389
REMARK 3 24 1.2600 - 1.2422 1.00 2680 139 0.2164 0.2333
REMARK 3 25 1.2422 - 1.2254 1.00 2689 142 0.2356 0.2552
REMARK 3 26 1.2254 - 1.2095 1.00 2652 132 0.2428 0.2353
REMARK 3 27 1.2095 - 1.1944 1.00 2674 145 0.2469 0.2136
REMARK 3 28 1.1944 - 1.1800 1.00 2628 142 0.2745 0.2867
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.560
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 2227
REMARK 3 ANGLE : 1.109 3019
REMARK 3 CHIRALITY : 0.048 318
REMARK 3 PLANARITY : 0.006 378
REMARK 3 DIHEDRAL : 12.875 832
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 21:288)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0206 -16.7855 18.1594
REMARK 3 T TENSOR
REMARK 3 T11: 0.0848 T22: 0.0944
REMARK 3 T33: 0.0834 T12: -0.0278
REMARK 3 T13: 0.0140 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 0.8013 L22: 0.7792
REMARK 3 L33: 0.6288 L12: 0.1482
REMARK 3 L13: 0.0334 L23: -0.1042
REMARK 3 S TENSOR
REMARK 3 S11: 0.0452 S12: -0.1166 S13: 0.0117
REMARK 3 S21: 0.0790 S22: -0.0440 S23: -0.0028
REMARK 3 S31: -0.0107 S32: -0.0374 S33: -0.0019
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 5G5C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1290066912.
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) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79722
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.180
REMARK 200 RESOLUTION RANGE LOW (A) : 135.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
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 (%): 40.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.96450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.96450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 24.29800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.45750
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.29800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.45750
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 67.96450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.29800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 36.45750
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 67.96450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.29800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 36.45750
REMARK 290 SMTRY3 8 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: 3400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.1 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 -48.59600
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 67.96450
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2003 LIES ON A SPECIAL POSITION.
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 THR A 115
REMARK 465 THR A 116
REMARK 465 VAL A 117
REMARK 465 GLY A 118
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 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 -159.38 -96.57
REMARK 500 TYR A 84 -34.68 -145.32
REMARK 500 SER A 149 -122.90 58.57
REMARK 500 VAL A 265 16.43 46.97
REMARK 500
REMARK 500 REMARK: NULL
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: 5G5M RELATED DB: PDB
REMARK 900 STRUCTURE OF THE PYROCOCCUS FURIOSUS ESTERASE PF2001 WITH SPACE
REMARK 900 GROUP P21
DBREF 5G5C A 21 288 UNP Q8TZJ1 Q8TZJ1_PYRFU 21 288
SEQADV 5G5C MET A 14 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5C HIS A 15 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5C HIS A 16 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5C HIS A 17 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5C HIS A 18 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5C HIS A 19 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G5C HIS A 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
FORMUL 2 HOH *157(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 LYS A 186 1 11
HELIX 7 7 TYR A 187 LEU A 191 5 5
HELIX 8 8 PRO A 192 PHE A 206 1 15
HELIX 9 9 ASN A 216 ILE A 221 1 6
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
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
CRYST1 48.596 72.915 135.929 90.00 90.00 90.00 C 2 2 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 0.020578 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013715 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007357 0.00000
TER 2162 GLY A 288
MASTER 310 0 0 12 8 0 0 6 2296 1 0 22
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