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HEADER HYDROLASE 01-APR-15 4Z49
TITLE HOMO SAPIENS FATTY ACID SYNTHETASE, THIOESTERASE DOMAIN AT 1.7
TITLE 2 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 2221-2502;
COMPND 5 EC: 3.1.2.14;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FASN, FAS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FATTY ACID SYNTHETASE, THIOESTERASE, FAS-TE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SPRAGGON
REVDAT 1 16-MAR-16 4Z49 0
JRNL AUTH I.H.PARK,J.D.VENABLE,C.STECKLER,S.E.CELLITTI,S.A.LESLEY,
JRNL AUTH 2 G.SPRAGGON,A.BROCK
JRNL TITL ESTIMATION OF HYDROGEN-EXCHANGE PROTECTION FACTORS FROM MD
JRNL TITL 2 SIMULATION BASED ON AMIDE HYDROGEN BONDING ANALYSIS.
JRNL REF J.CHEM.INF.MODEL. V. 55 1914 2015
JRNL REFN ESSN 1549-960X
JRNL PMID 26241692
JRNL DOI 10.1021/ACS.JCIM.5B00185
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 57757
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 2872
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.74
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.58
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4225
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2361
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4011
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.07
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 214
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4203
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 699
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09260
REMARK 3 B22 (A**2) : 0.08230
REMARK 3 B33 (A**2) : -0.17480
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.71940
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.185
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.113
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.111
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.106
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.107
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4383 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5970 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1514 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 99 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 667 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4383 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 575 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6205 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.21
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.83
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6817 0.3617 4.2116
REMARK 3 T TENSOR
REMARK 3 T11: -0.0296 T22: -0.0128
REMARK 3 T33: -0.0063 T12: 0.0002
REMARK 3 T13: 0.0065 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 0.5754 L22: 0.4317
REMARK 3 L33: 0.5161 L12: 0.0436
REMARK 3 L13: -0.0643 L23: -0.0757
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: -0.0475 S13: -0.0972
REMARK 3 S21: -0.0182 S22: -0.0425 S23: -0.0160
REMARK 3 S31: 0.0601 S32: 0.0147 S33: 0.0392
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6951 26.1660 23.9272
REMARK 3 T TENSOR
REMARK 3 T11: -0.0276 T22: 0.0082
REMARK 3 T33: -0.0113 T12: -0.0051
REMARK 3 T13: 0.0040 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.2162 L22: 0.3763
REMARK 3 L33: 0.6567 L12: 0.0575
REMARK 3 L13: -0.0288 L23: -0.2097
REMARK 3 S TENSOR
REMARK 3 S11: 0.0011 S12: -0.0370 S13: 0.0143
REMARK 3 S21: 0.0023 S22: 0.0183 S23: -0.0153
REMARK 3 S31: -0.0367 S32: -0.0095 S33: -0.0194
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4Z49 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208610.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-05
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 : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59827
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.08400
REMARK 200 FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.48600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.960
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-3350, 0.2M POTASSIUM CHLORIDE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 58.79550
REMARK 290 SMTRY3 2 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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 LEU A 2345
REMARK 465 ALA A 2346
REMARK 465 TYR A 2347
REMARK 465 THR A 2348
REMARK 465 GLN A 2349
REMARK 465 SER A 2350
REMARK 465 TYR A 2351
REMARK 465 ARG A 2352
REMARK 465 ALA A 2353
REMARK 465 LYS A 2354
REMARK 465 LEU A 2355
REMARK 465 THR A 2356
REMARK 465 PRO A 2357
REMARK 465 GLY A 2452
REMARK 465 ALA A 2453
REMARK 465 TYR A 2454
REMARK 465 GLY A 2455
REMARK 465 GLU A 2456
REMARK 465 ASP A 2457
REMARK 465 LEU A 2458
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 A2308 -114.16 59.00
REMARK 500 ASP A2480 -169.28 -110.11
REMARK 500 THR B2274 -165.88 -115.48
REMARK 500 SER B2308 -116.12 55.33
REMARK 500 GLU B2456 76.54 -18.66
REMARK 500 ASP B2457 6.03 -177.75
REMARK 500 ASP B2480 -169.27 -109.78
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 A2920 DISTANCE = 7.21 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 K B2601 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B2308 OG
REMARK 620 2 HOH B2782 O 73.0
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 K B 2601
DBREF 4Z49 A 2221 2502 UNP P49327 FAS_HUMAN 2221 2502
DBREF 4Z49 B 2221 2502 UNP P49327 FAS_HUMAN 2221 2502
SEQRES 1 A 282 SER LEU LEU VAL ASN PRO GLU GLY PRO THR LEU MET ARG
SEQRES 2 A 282 LEU ASN SER VAL GLN SER SER GLU ARG PRO LEU PHE LEU
SEQRES 3 A 282 VAL HIS PRO ILE GLU GLY SER THR THR VAL PHE HIS SER
SEQRES 4 A 282 LEU ALA SER ARG LEU SER ILE PRO THR TYR GLY LEU GLN
SEQRES 5 A 282 CYS THR ARG ALA ALA PRO LEU ASP SER ILE HIS SER LEU
SEQRES 6 A 282 ALA ALA TYR TYR ILE ASP CYS ILE ARG GLN VAL GLN PRO
SEQRES 7 A 282 GLU GLY PRO TYR ARG VAL ALA GLY TYR SER TYR GLY ALA
SEQRES 8 A 282 CYS VAL ALA PHE GLU MET CYS SER GLN LEU GLN ALA GLN
SEQRES 9 A 282 GLN SER PRO ALA PRO THR HIS ASN SER LEU PHE LEU PHE
SEQRES 10 A 282 ASP GLY SER PRO THR TYR VAL LEU ALA TYR THR GLN SER
SEQRES 11 A 282 TYR ARG ALA LYS LEU THR PRO GLY CYS GLU ALA GLU ALA
SEQRES 12 A 282 GLU THR GLU ALA ILE CYS PHE PHE VAL GLN GLN PHE THR
SEQRES 13 A 282 ASP MET GLU HIS ASN ARG VAL LEU GLU ALA LEU LEU PRO
SEQRES 14 A 282 LEU LYS GLY LEU GLU GLU ARG VAL ALA ALA ALA VAL ASP
SEQRES 15 A 282 LEU ILE ILE LYS SER HIS GLN GLY LEU ASP ARG GLN GLU
SEQRES 16 A 282 LEU SER PHE ALA ALA ARG SER PHE TYR TYR LYS LEU ARG
SEQRES 17 A 282 ALA ALA GLU GLN TYR THR PRO LYS ALA LYS TYR HIS GLY
SEQRES 18 A 282 ASN VAL MET LEU LEU ARG ALA LYS THR GLY GLY ALA TYR
SEQRES 19 A 282 GLY GLU ASP LEU GLY ALA ASP TYR ASN LEU SER GLN VAL
SEQRES 20 A 282 CYS ASP GLY LYS VAL SER VAL HIS VAL ILE GLU GLY ASP
SEQRES 21 A 282 HIS ARG THR LEU LEU GLU GLY SER GLY LEU GLU SER ILE
SEQRES 22 A 282 ILE SER ILE ILE HIS SER SER LEU ALA
SEQRES 1 B 282 SER LEU LEU VAL ASN PRO GLU GLY PRO THR LEU MET ARG
SEQRES 2 B 282 LEU ASN SER VAL GLN SER SER GLU ARG PRO LEU PHE LEU
SEQRES 3 B 282 VAL HIS PRO ILE GLU GLY SER THR THR VAL PHE HIS SER
SEQRES 4 B 282 LEU ALA SER ARG LEU SER ILE PRO THR TYR GLY LEU GLN
SEQRES 5 B 282 CYS THR ARG ALA ALA PRO LEU ASP SER ILE HIS SER LEU
SEQRES 6 B 282 ALA ALA TYR TYR ILE ASP CYS ILE ARG GLN VAL GLN PRO
SEQRES 7 B 282 GLU GLY PRO TYR ARG VAL ALA GLY TYR SER TYR GLY ALA
SEQRES 8 B 282 CYS VAL ALA PHE GLU MET CYS SER GLN LEU GLN ALA GLN
SEQRES 9 B 282 GLN SER PRO ALA PRO THR HIS ASN SER LEU PHE LEU PHE
SEQRES 10 B 282 ASP GLY SER PRO THR TYR VAL LEU ALA TYR THR GLN SER
SEQRES 11 B 282 TYR ARG ALA LYS LEU THR PRO GLY CYS GLU ALA GLU ALA
SEQRES 12 B 282 GLU THR GLU ALA ILE CYS PHE PHE VAL GLN GLN PHE THR
SEQRES 13 B 282 ASP MET GLU HIS ASN ARG VAL LEU GLU ALA LEU LEU PRO
SEQRES 14 B 282 LEU LYS GLY LEU GLU GLU ARG VAL ALA ALA ALA VAL ASP
SEQRES 15 B 282 LEU ILE ILE LYS SER HIS GLN GLY LEU ASP ARG GLN GLU
SEQRES 16 B 282 LEU SER PHE ALA ALA ARG SER PHE TYR TYR LYS LEU ARG
SEQRES 17 B 282 ALA ALA GLU GLN TYR THR PRO LYS ALA LYS TYR HIS GLY
SEQRES 18 B 282 ASN VAL MET LEU LEU ARG ALA LYS THR GLY GLY ALA TYR
SEQRES 19 B 282 GLY GLU ASP LEU GLY ALA ASP TYR ASN LEU SER GLN VAL
SEQRES 20 B 282 CYS ASP GLY LYS VAL SER VAL HIS VAL ILE GLU GLY ASP
SEQRES 21 B 282 HIS ARG THR LEU LEU GLU GLY SER GLY LEU GLU SER ILE
SEQRES 22 B 282 ILE SER ILE ILE HIS SER SER LEU ALA
HET K B2601 1
HETNAM K POTASSIUM ION
FORMUL 3 K K 1+
FORMUL 4 HOH *699(H2 O)
HELIX 1 AA1 THR A 2254 VAL A 2256 5 3
HELIX 2 AA2 PHE A 2257 LEU A 2264 1 8
HELIX 3 AA3 SER A 2281 GLN A 2297 1 17
HELIX 4 AA4 SER A 2308 SER A 2326 1 19
HELIX 5 AA5 CYS A 2359 THR A 2376 1 18
HELIX 6 AA6 GLU A 2379 LEU A 2388 1 10
HELIX 7 AA7 GLY A 2392 HIS A 2408 1 17
HELIX 8 AA8 ASP A 2412 TYR A 2433 1 22
HELIX 9 AA9 ASN A 2463 CYS A 2468 1 6
HELIX 10 AB1 GLU A 2486 HIS A 2498 1 13
HELIX 11 AB2 THR B 2254 VAL B 2256 5 3
HELIX 12 AB3 PHE B 2257 LEU B 2264 1 8
HELIX 13 AB4 SER B 2281 GLN B 2297 1 17
HELIX 14 AB5 SER B 2308 SER B 2326 1 19
HELIX 15 AB6 SER B 2340 ALA B 2353 1 14
HELIX 16 AB7 CYS B 2359 ALA B 2361 5 3
HELIX 17 AB8 GLU B 2362 GLN B 2374 1 13
HELIX 18 AB9 GLU B 2379 LEU B 2388 1 10
HELIX 19 AC1 GLY B 2392 HIS B 2408 1 17
HELIX 20 AC2 ASP B 2412 TYR B 2433 1 22
HELIX 21 AC3 ASN B 2463 VAL B 2467 5 5
HELIX 22 AC4 GLU B 2486 LEU B 2501 1 16
SHEET 1 AA1 7 LEU A2231 ARG A2233 0
SHEET 2 AA1 7 THR A2268 LEU A2271 -1 O GLY A2270 N MET A2232
SHEET 3 AA1 7 LEU A2244 VAL A2247 1 N LEU A2244 O TYR A2269
SHEET 4 AA1 7 ARG A2303 TYR A2307 1 O ALA A2305 N VAL A2247
SHEET 5 AA1 7 SER A2333 PHE A2337 1 O SER A2333 N VAL A2304
SHEET 6 AA1 7 VAL A2443 ALA A2448 1 O MET A2444 N LEU A2336
SHEET 7 AA1 7 VAL A2472 ILE A2477 1 O ILE A2477 N ARG A2447
SHEET 1 AA2 7 LEU B2231 ARG B2233 0
SHEET 2 AA2 7 THR B2268 LEU B2271 -1 O GLY B2270 N MET B2232
SHEET 3 AA2 7 LEU B2244 VAL B2247 1 N LEU B2246 O LEU B2271
SHEET 4 AA2 7 ARG B2303 TYR B2307 1 O ALA B2305 N PHE B2245
SHEET 5 AA2 7 SER B2333 PHE B2337 1 O PHE B2337 N GLY B2306
SHEET 6 AA2 7 VAL B2443 ALA B2448 1 O MET B2444 N LEU B2336
SHEET 7 AA2 7 VAL B2472 ILE B2477 1 O ILE B2477 N ARG B2447
LINK OG SER B2308 K K B2601 1555 1555 2.95
LINK K K B2601 O HOH B2782 1555 1555 2.49
CISPEP 1 GLY A 2300 PRO A 2301 0 -2.62
CISPEP 2 SER A 2326 PRO A 2327 0 5.13
CISPEP 3 GLY B 2300 PRO B 2301 0 0.91
CISPEP 4 SER B 2326 PRO B 2327 0 7.95
SITE 1 AC1 5 PRO B2249 ILE B2250 SER B2308 TYR B2309
SITE 2 AC1 5 HOH B2782
CRYST1 38.726 117.591 63.284 90.00 105.58 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 0.025822 0.000000 0.007200 0.00000
SCALE2 0.000000 0.008504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016405 0.00000
TER 2060 ALA A2502
TER 4277 ALA B2502
MASTER 326 0 1 22 14 0 2 6 4903 2 3 44
END |