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HEADER STRUCTURAL PROTEIN 23-MAY-16 5G59
TITLE STRUCTURE OF THE PYROCOCCUS FURIOSUS ESTERASE PF2001 WITH SPACE GROUP
TITLE 2 P3121
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 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 5G59 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. 1.61 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) : 1.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 39550
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1913
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 52.6951 - 3.8874 1.00 2863 98 0.1505 0.1532
REMARK 3 2 3.8874 - 3.0856 1.00 2695 171 0.1615 0.1788
REMARK 3 3 3.0856 - 2.6956 1.00 2704 128 0.1758 0.2116
REMARK 3 4 2.6956 - 2.4491 1.00 2677 151 0.1732 0.2034
REMARK 3 5 2.4491 - 2.2736 1.00 2687 132 0.1726 0.2182
REMARK 3 6 2.2736 - 2.1395 1.00 2678 142 0.1646 0.1828
REMARK 3 7 2.1395 - 2.0324 1.00 2677 134 0.1639 0.2001
REMARK 3 8 2.0324 - 1.9439 1.00 2677 140 0.1671 0.1977
REMARK 3 9 1.9439 - 1.8691 1.00 2665 141 0.1651 0.1958
REMARK 3 10 1.8691 - 1.8046 1.00 2668 144 0.1692 0.2349
REMARK 3 11 1.8046 - 1.7482 1.00 2654 146 0.1821 0.1991
REMARK 3 12 1.7482 - 1.6982 1.00 2665 120 0.1767 0.1985
REMARK 3 13 1.6982 - 1.6535 1.00 2658 123 0.1800 0.2192
REMARK 3 14 1.6535 - 1.6131 1.00 2669 143 0.1943 0.2165
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.630
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 2309
REMARK 3 ANGLE : 1.058 3129
REMARK 3 CHIRALITY : 0.046 326
REMARK 3 PLANARITY : 0.005 395
REMARK 3 DIHEDRAL : 12.359 850
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 -10:9999)
REMARK 3 ORIGIN FOR THE GROUP (A): 86.1932 73.1231 48.8675
REMARK 3 T TENSOR
REMARK 3 T11: 0.0835 T22: 0.0596
REMARK 3 T33: 0.0767 T12: -0.0067
REMARK 3 T13: 0.0050 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.1483 L22: 1.0126
REMARK 3 L33: 0.8845 L12: 0.4685
REMARK 3 L13: 0.2221 L23: 0.3719
REMARK 3 S TENSOR
REMARK 3 S11: -0.0413 S12: 0.0485 S13: 0.0024
REMARK 3 S21: -0.0382 S22: 0.0483 S23: -0.0526
REMARK 3 S31: 0.0236 S32: -0.0516 S33: -0.0023
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 5G59 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_1290066907.
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) : 0.9998
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 : 39571
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.610
REMARK 200 RESOLUTION RANGE LOW (A) : 52.660
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 17.70
REMARK 200 R MERGE (I) : 0.24000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.61
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 17.60
REMARK 200 R MERGE FOR SHELL (I) : 1.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% MPD, 10% PEG 4000, 0.1 M IMIDAZOLE
REMARK 280 -HCL, PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 15.94767
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.89533
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.89533
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 15.94767
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A2114 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 16 NE2 HIS A 16 CD2 -0.068
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 40 16.37 87.10
REMARK 500 SER A 77 -155.16 -102.94
REMARK 500 TYR A 84 -36.92 -144.79
REMARK 500 VAL A 117 48.50 33.89
REMARK 500 ASP A 119 -79.75 -84.95
REMARK 500 SER A 149 -124.65 60.84
REMARK 500 VAL A 265 23.59 43.86
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 A2041 DISTANCE = 5.87 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HG A1289 HG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 167 SG
REMARK 620 2 MET A 287 SD 87.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 1289
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 1290
REMARK 900
REMARK 900 RELATED ENTRIES
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 5G59 A 21 288 UNP Q8TZJ1 Q8TZJ1_PYRFU 21 288
SEQADV 5G59 MET A 14 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G59 HIS A 15 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G59 HIS A 16 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G59 HIS A 17 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G59 HIS A 18 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G59 HIS A 19 UNP Q8TZJ1 EXPRESSION TAG
SEQADV 5G59 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
HET HG A1289 1
HET HG A1290 1
HETNAM HG MERCURY (II) ION
FORMUL 2 HG 2(HG 2+)
FORMUL 4 HOH *153(H2 O)
HELIX 1 1 HIS A 16 ASN A 26 1 11
HELIX 2 2 THR A 35 SER A 40 5 6
HELIX 3 3 TYR A 84 GLU A 95 1 12
HELIX 4 4 LYS A 120 TYR A 136 1 17
HELIX 5 5 PRO A 137 SER A 140 5 4
HELIX 6 6 SER A 149 VAL A 162 1 14
HELIX 7 7 TYR A 176 LYS A 190 1 15
HELIX 8 8 PRO A 192 TRP A 194 5 3
HELIX 9 9 LEU A 195 GLY A 208 1 14
HELIX 10 10 ASN A 213 LEU A 215 5 3
HELIX 11 11 ASN A 216 ILE A 221 1 6
HELIX 12 12 LYS A 237 LYS A 249 1 13
HELIX 13 13 ARG A 266 PHE A 271 1 6
HELIX 14 14 PHE A 271 MET A 287 1 17
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
LINK HG HG A1289 SG CYS A 167 1555 1555 2.32
LINK HG HG A1289 SD MET A 287 1555 1555 2.97
LINK HG HG A1290 O VAL A 145 1555 1555 3.07
SITE 1 AC1 4 CYS A 166 CYS A 167 TRP A 286 MET A 287
SITE 1 AC2 4 VAL A 145 CYS A 167 GLY A 168 LEU A 283
CRYST1 105.334 105.334 47.843 90.00 90.00 120.00 P 31 2 1 6
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 0.009494 0.005481 0.000000 0.00000
SCALE2 0.000000 0.010962 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020902 0.00000
TER 2242 GLY A 288
MASTER 325 0 2 14 8 0 2 6 2392 1 5 22
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