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HEADER HYDROLASE 29-SEP-16 5THM
TITLE ESTERASE-6 FROM DROSOPHILA MELANOGASTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE-6;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EST-6,CARBOXYLIC-ESTER HYDROLASE 6,CARBOXYLESTERASE-6;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: EST-6, EST6, CG6917;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOXYLESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.J.FRASER,C.J.JACKSON
REVDAT 1 08-MAR-17 5THM 0
JRNL AUTH F.YOUNUS,N.J.FRASER,C.COPPIN,J.W.LIU,T.CHERTEMPS,G.PANDEY,
JRNL AUTH 2 M.MAIBECHE-COISNE,R.J.RUSSELL,C.J.JACKSON,J.G.OAKESHOTT
JRNL TITL STRUCTURE AND KINETIC PROPERTIES OF ESTERASE 6, AN ODORANT
JRNL TITL 2 DEGRADING ENZYME (ODE) IN DROSOPHILA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 31400
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1588
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 40.3296 - 4.7792 1.00 2975 166 0.1397 0.1604
REMARK 3 2 4.7792 - 3.7943 1.00 2862 155 0.1274 0.1561
REMARK 3 3 3.7943 - 3.3149 1.00 2833 151 0.1551 0.2207
REMARK 3 4 3.3149 - 3.0120 1.00 2793 153 0.1759 0.2388
REMARK 3 5 3.0120 - 2.7961 1.00 2795 148 0.1716 0.2355
REMARK 3 6 2.7961 - 2.6313 1.00 2773 139 0.1710 0.2314
REMARK 3 7 2.6313 - 2.4996 0.99 2776 139 0.1677 0.2567
REMARK 3 8 2.4996 - 2.3908 1.00 2767 139 0.1584 0.2140
REMARK 3 9 2.3908 - 2.2987 0.99 2760 147 0.1542 0.2162
REMARK 3 10 2.2987 - 2.2194 0.90 2496 127 0.1668 0.3017
REMARK 3 11 2.2194 - 2.1500 0.72 1982 124 0.1696 0.2318
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.130
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 : 0.007 4364
REMARK 3 ANGLE : 0.915 5926
REMARK 3 CHIRALITY : 0.055 603
REMARK 3 PLANARITY : 0.005 776
REMARK 3 DIHEDRAL : 13.613 2548
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 5THM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000217040.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9655
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31402
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 40.322
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 11.70
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.52
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: MOLREP
REMARK 200 STARTING MODEL: 4FNG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M TRIS PH
REMARK 280 8.5 AND 25 % W/V POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277.15K
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 33.85650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.51900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.32250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.51900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.85650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.32250
REMARK 290 SMTRY3 4 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 ASP A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 SER A 1
REMARK 465 ASP A 2
REMARK 465 THR A 3
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 OG SER A 188 HN11 7BZ A 601 1.42
REMARK 500 OG SER A 188 BN1 7BZ A 601 1.99
REMARK 500 SG CYS A 65 O HOH A 960 2.10
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 ARG A 230 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 230 NE - CZ - NH2 ANGL. DEV. = -7.5 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 ALA A 58 39.57 -98.54
REMARK 500 ASN A 94 113.54 -160.80
REMARK 500 PHE A 144 12.16 -142.28
REMARK 500 SER A 188 -126.17 58.07
REMARK 500 VAL A 222 -81.13 -91.16
REMARK 500 SER A 272 -131.71 57.12
REMARK 500 PHE A 397 -45.32 -133.09
REMARK 500 ASN A 423 84.77 -168.96
REMARK 500 HIS A 445 116.52 -28.70
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 7BZ A 601
DBREF 5THM A 1 523 UNP P08171 EST6_DROME 22 544
SEQADV 5THM MET A -9 UNP P08171 INITIATING METHIONINE
SEQADV 5THM HIS A -8 UNP P08171 EXPRESSION TAG
SEQADV 5THM HIS A -7 UNP P08171 EXPRESSION TAG
SEQADV 5THM HIS A -6 UNP P08171 EXPRESSION TAG
SEQADV 5THM HIS A -5 UNP P08171 EXPRESSION TAG
SEQADV 5THM HIS A -4 UNP P08171 EXPRESSION TAG
SEQADV 5THM HIS A -3 UNP P08171 EXPRESSION TAG
SEQADV 5THM ASP A -2 UNP P08171 EXPRESSION TAG
SEQADV 5THM HIS A -1 UNP P08171 EXPRESSION TAG
SEQADV 5THM MET A 0 UNP P08171 EXPRESSION TAG
SEQADV 5THM VAL A 15 UNP P08171 LYS 36 ENGINEERED MUTATION
SEQADV 5THM LEU A 145 UNP P08171 VAL 166 ENGINEERED MUTATION
SEQADV 5THM MLY A 208 UNP P08171 ARG 229 ENGINEERED MUTATION
SEQADV 5THM GLU A 229 UNP P08171 GLY 250 ENGINEERED MUTATION
SEQADV 5THM SER A 237 UNP P08171 ASN 258 ENGINEERED MUTATION
SEQADV 5THM ALA A 247 UNP P08171 THR 268 ENGINEERED MUTATION
SEQADV 5THM GLY A 290 UNP P08171 ASP 311 ENGINEERED MUTATION
SEQADV 5THM PHE A 292 UNP P08171 ILE 313 ENGINEERED MUTATION
SEQADV 5THM VAL A 335 UNP P08171 ILE 356 ENGINEERED MUTATION
SEQADV 5THM GLY A 383 UNP P08171 GLU 404 ENGINEERED MUTATION
SEQADV 5THM GLY A 400 UNP P08171 SER 421 ENGINEERED MUTATION
SEQADV 5THM VAL A 416 UNP P08171 ALA 437 ENGINEERED MUTATION
SEQADV 5THM SER A 450 UNP P08171 PHE 471 ENGINEERED MUTATION
SEQADV 5THM SER A 456 UNP P08171 PHE 477 ENGINEERED MUTATION
SEQADV 5THM ASP A 485 UNP P08171 ASN 506 ENGINEERED MUTATION
SEQADV 5THM THR A 511 UNP P08171 ILE 532 ENGINEERED MUTATION
SEQRES 1 A 533 MET HIS HIS HIS HIS HIS HIS ASP HIS MET SER ASP THR
SEQRES 2 A 533 ASP ASP PRO LEU LEU VAL GLN LEU PRO GLN GLY VAL LEU
SEQRES 3 A 533 ARG GLY ARG ASP ASN GLY SER TYR TYR SER TYR GLU SER
SEQRES 4 A 533 ILE PRO TYR ALA GLU PRO PRO THR GLY ASP LEU ARG PHE
SEQRES 5 A 533 GLU ALA PRO GLU PRO TYR MLY GLN MLY TRP SER ASP ILE
SEQRES 6 A 533 PHE ASP ALA THR MLY THR PRO VAL ALA CYS LEU GLN TRP
SEQRES 7 A 533 ASP GLN PHE THR PRO GLY ALA ASN MLY LEU VAL GLY GLU
SEQRES 8 A 533 GLU ASP CYS LEU THR VAL SER VAL TYR MLY PRO MLY ASN
SEQRES 9 A 533 SER MLY ARG ASN SER PHE PRO VAL VAL ALA HIS ILE HIS
SEQRES 10 A 533 GLY GLY ALA PHE MET PHE GLY ALA ALA TRP GLN ASN GLY
SEQRES 11 A 533 HIS GLU ASN VAL MET ARG GLU GLY MLY PHE ILE LEU VAL
SEQRES 12 A 533 LYS ILE SER TYR ARG LEU GLY PRO LEU GLY PHE LEU SER
SEQRES 13 A 533 THR GLY ASP ARG ASP LEU PRO GLY ASN TYR GLY LEU LYS
SEQRES 14 A 533 ASP GLN ARG LEU ALA LEU MLY TRP ILE MLY GLN ASN ILE
SEQRES 15 A 533 ALA SER PHE GLY GLY GLU PRO GLN ASN VAL LEU LEU VAL
SEQRES 16 A 533 GLY HIS SER ALA GLY GLY ALA SER VAL HIS LEU GLN MET
SEQRES 17 A 533 LEU ARG GLU ASP PHE GLY GLN LEU ALA MLY ALA ALA PHE
SEQRES 18 A 533 SER PHE SER GLY ASN ALA LEU ASP PRO TRP VAL ILE GLN
SEQRES 19 A 533 MLY GLY ALA ARG GLU ARG ALA PHE GLU LEU GLY ARG SER
SEQRES 20 A 533 VAL GLY CYS GLU SER ALA GLU ASP SER ALA SER LEU MLY
SEQRES 21 A 533 MLY CYS LEU MLY SER MLY PRO ALA SER GLU LEU VAL THR
SEQRES 22 A 533 ALA VAL ARG MLY PHE LEU ILE PHE SER TYR VAL PRO PHE
SEQRES 23 A 533 ALA PRO PHE SER PRO VAL LEU GLU PRO SER ASP ALA PRO
SEQRES 24 A 533 GLY ALA PHE ILE THR GLN ASP PRO ARG ASP VAL ILE MLY
SEQRES 25 A 533 SER GLY MLY PHE GLY GLN VAL PRO TRP ALA VAL SER TYR
SEQRES 26 A 533 VAL THR GLU ASP GLY GLY TYR ASN ALA ALA LEU LEU LEU
SEQRES 27 A 533 MLY GLU ARG MLY SER GLY VAL VAL ILE ASP ASP LEU ASN
SEQRES 28 A 533 GLU ARG TRP LEU GLU LEU ALA PRO TYR LEU LEU PHE TYR
SEQRES 29 A 533 ARG ASP THR MLY THR MLY MLY ASP MET ASP ASP TYR SER
SEQRES 30 A 533 ARG MLY ILE MLY GLN GLU TYR ILE GLY ASN GLN ARG PHE
SEQRES 31 A 533 ASP ILE GLY SER TYR SER GLU LEU GLN ARG LEU PHE THR
SEQRES 32 A 533 ASP ILE LEU PHE LYS ASN GLY THR GLN GLU SER LEU ASP
SEQRES 33 A 533 LEU HIS ARG MLY TYR GLY MLY SER PRO VAL TYR ALA TYR
SEQRES 34 A 533 VAL TYR ASP ASN PRO ALA GLU MLY GLY ILE ALA GLN VAL
SEQRES 35 A 533 LEU ALA ASN ARG THR ASP TYR ASP PHE GLY THR VAL HIS
SEQRES 36 A 533 GLY ASP ASP TYR SER LEU ILE PHE GLU ASN SER VAL ARG
SEQRES 37 A 533 ASP VAL GLU MET ARG PRO ASP GLU GLN ILE ILE SER ARG
SEQRES 38 A 533 ASN PHE ILE ASN MET LEU ALA ASP PHE ALA SER SER ASP
SEQRES 39 A 533 ASP GLY SER LEU MLY TYR GLY GLU CYS ASP PHE MLY ASP
SEQRES 40 A 533 ASN VAL GLY SER GLU MLY PHE GLN LEU LEU ALA ILE TYR
SEQRES 41 A 533 THR ASP GLY CYS GLN ASN ARG GLN HIS VAL GLU PHE PRO
MODRES 5THM MLY A 49 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 51 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 60 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 77 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 91 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 93 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 96 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 129 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 166 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 169 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 225 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 250 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 251 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 254 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 256 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 267 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 302 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 305 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 329 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 332 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 358 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 360 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 361 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 369 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 371 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 410 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 413 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 427 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 489 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 496 LYS MODIFIED RESIDUE
MODRES 5THM MLY A 503 LYS MODIFIED RESIDUE
HET MLY A 49 11
HET MLY A 51 11
HET MLY A 60 11
HET MLY A 77 11
HET MLY A 91 11
HET MLY A 93 11
HET MLY A 96 11
HET MLY A 129 11
HET MLY A 166 11
HET MLY A 169 11
HET MLY A 208 11
HET MLY A 225 11
HET MLY A 250 11
HET MLY A 251 11
HET MLY A 254 11
HET MLY A 256 11
HET MLY A 267 11
HET MLY A 302 11
HET MLY A 305 11
HET MLY A 329 11
HET MLY A 332 11
HET MLY A 358 11
HET MLY A 360 11
HET MLY A 361 11
HET MLY A 369 11
HET MLY A 371 11
HET MLY A 410 11
HET MLY A 413 11
HET MLY A 427 11
HET MLY A 489 11
HET MLY A 496 11
HET MLY A 503 11
HET 7BZ A 601 12
HETNAM MLY N-DIMETHYL-LYSINE
HETNAM 7BZ N,N-DIMETHYLBORANAMINE
FORMUL 1 MLY 32(C8 H18 N2 O2)
FORMUL 2 7BZ C2 H8 B N
FORMUL 3 HOH *322(H2 O)
HELIX 1 AA1 THR A 37 ARG A 41 5 5
HELIX 2 AA2 ALA A 115 ASN A 119 5 5
HELIX 3 AA3 HIS A 121 GLY A 128 1 8
HELIX 4 AA4 LEU A 139 LEU A 145 1 7
HELIX 5 AA5 ASN A 155 ILE A 172 1 18
HELIX 6 AA6 ALA A 173 PHE A 175 5 3
HELIX 7 AA7 SER A 188 LEU A 199 1 12
HELIX 8 AA8 ASP A 202 LEU A 206 5 5
HELIX 9 AA9 GLY A 226 VAL A 238 1 13
HELIX 10 AB1 ASP A 245 SER A 255 1 11
HELIX 11 AB2 PRO A 257 ALA A 264 1 8
HELIX 12 AB3 VAL A 265 LEU A 269 5 5
HELIX 13 AB4 ASP A 296 GLY A 304 1 9
HELIX 14 AB5 GLY A 320 ALA A 325 1 6
HELIX 15 AB6 LEU A 326 MLY A 329 5 4
HELIX 16 AB7 VAL A 335 ASP A 338 5 4
HELIX 17 AB8 ASP A 339 LEU A 352 1 14
HELIX 18 AB9 THR A 359 GLY A 376 1 18
HELIX 19 AC1 SER A 384 PHE A 397 1 14
HELIX 20 AC2 PHE A 397 GLY A 412 1 16
HELIX 21 AC3 GLY A 428 ASN A 435 1 8
HELIX 22 AC4 ASP A 448 PHE A 453 1 6
HELIX 23 AC5 ARG A 463 SER A 483 1 21
SHEET 1 AA1 3 LEU A 8 LEU A 11 0
SHEET 2 AA1 3 GLY A 14 ARG A 17 -1 O GLY A 14 N LEU A 11
SHEET 3 AA1 3 PHE A 56 ASP A 57 1 O PHE A 56 N ARG A 17
SHEET 1 AA211 ARG A 19 ASP A 20 0
SHEET 2 AA211 TYR A 24 PRO A 31 -1 O SER A 26 N ARG A 19
SHEET 3 AA211 THR A 86 PRO A 92 -1 O MLY A 91 N TYR A 25
SHEET 4 AA211 ILE A 131 ILE A 135 -1 O LEU A 132 N TYR A 90
SHEET 5 AA211 PHE A 100 ILE A 106 1 N HIS A 105 O VAL A 133
SHEET 6 AA211 GLY A 177 HIS A 187 1 O VAL A 185 N ALA A 104
SHEET 7 AA211 ALA A 209 PHE A 213 1 O PHE A 213 N GLY A 186
SHEET 8 AA211 TRP A 311 VAL A 316 1 O ALA A 312 N SER A 212
SHEET 9 AA211 VAL A 416 ASP A 422 1 O TYR A 417 N TRP A 311
SHEET 10 AA211 PHE A 504 TYR A 510 1 O LEU A 507 N ALA A 418
SHEET 11 AA211 GLY A 513 HIS A 519 -1 O GLN A 515 N ALA A 508
SHEET 1 AA3 2 GLN A 67 TRP A 68 0
SHEET 2 AA3 2 LEU A 78 VAL A 79 -1 O VAL A 79 N GLN A 67
SHEET 1 AA4 2 MLY A 489 TYR A 490 0
SHEET 2 AA4 2 CYS A 493 ASP A 494 -1 O CYS A 493 N TYR A 490
SSBOND 1 CYS A 65 CYS A 84 1555 1555 2.05
SSBOND 2 CYS A 240 CYS A 252 1555 1555 2.07
LINK C TYR A 48 N MLY A 49 1555 1555 1.33
LINK C MLY A 49 N GLN A 50 1555 1555 1.33
LINK C GLN A 50 N MLY A 51 1555 1555 1.33
LINK C MLY A 51 N TRP A 52 1555 1555 1.33
LINK C THR A 59 N MLY A 60 1555 1555 1.33
LINK C MLY A 60 N THR A 61 1555 1555 1.32
LINK C ASN A 76 N MLY A 77 1555 1555 1.33
LINK C MLY A 77 N LEU A 78 1555 1555 1.33
LINK C TYR A 90 N MLY A 91 1555 1555 1.33
LINK C MLY A 91 N PRO A 92 1555 1555 1.34
LINK C PRO A 92 N MLY A 93 1555 1555 1.33
LINK C MLY A 93 N ASN A 94 1555 1555 1.32
LINK C SER A 95 N MLY A 96 1555 1555 1.33
LINK C MLY A 96 N ARG A 97 1555 1555 1.33
LINK C GLY A 128 N MLY A 129 1555 1555 1.33
LINK C MLY A 129 N PHE A 130 1555 1555 1.33
LINK C LEU A 165 N MLY A 166 1555 1555 1.33
LINK C MLY A 166 N TRP A 167 1555 1555 1.33
LINK C ILE A 168 N MLY A 169 1555 1555 1.33
LINK C MLY A 169 N GLN A 170 1555 1555 1.33
LINK C ALA A 207 N MLY A 208 1555 1555 1.33
LINK C MLY A 208 N ALA A 209 1555 1555 1.34
LINK C GLN A 224 N MLY A 225 1555 1555 1.33
LINK C MLY A 225 N GLY A 226 1555 1555 1.33
LINK C LEU A 249 N MLY A 250 1555 1555 1.33
LINK C MLY A 250 N MLY A 251 1555 1555 1.33
LINK C MLY A 251 N CYS A 252 1555 1555 1.33
LINK C LEU A 253 N MLY A 254 1555 1555 1.33
LINK C MLY A 254 N SER A 255 1555 1555 1.34
LINK C SER A 255 N MLY A 256 1555 1555 1.33
LINK C MLY A 256 N PRO A 257 1555 1555 1.34
LINK C ARG A 266 N MLY A 267 1555 1555 1.33
LINK C MLY A 267 N PHE A 268 1555 1555 1.33
LINK C ILE A 301 N MLY A 302 1555 1555 1.33
LINK C MLY A 302 N SER A 303 1555 1555 1.33
LINK C GLY A 304 N MLY A 305 1555 1555 1.33
LINK C MLY A 305 N PHE A 306 1555 1555 1.33
LINK C LEU A 328 N MLY A 329 1555 1555 1.33
LINK C MLY A 329 N GLU A 330 1555 1555 1.33
LINK C ARG A 331 N MLY A 332 1555 1555 1.33
LINK C MLY A 332 N SER A 333 1555 1555 1.33
LINK C THR A 357 N MLY A 358 1555 1555 1.33
LINK C MLY A 358 N THR A 359 1555 1555 1.33
LINK C THR A 359 N MLY A 360 1555 1555 1.33
LINK C MLY A 360 N MLY A 361 1555 1555 1.34
LINK C MLY A 361 N ASP A 362 1555 1555 1.33
LINK C ARG A 368 N MLY A 369 1555 1555 1.33
LINK C MLY A 369 N ILE A 370 1555 1555 1.34
LINK C ILE A 370 N MLY A 371 1555 1555 1.33
LINK C MLY A 371 N GLN A 372 1555 1555 1.33
LINK C ARG A 409 N MLY A 410 1555 1555 1.33
LINK C MLY A 410 N TYR A 411 1555 1555 1.33
LINK C GLY A 412 N MLY A 413 1555 1555 1.33
LINK C MLY A 413 N SER A 414 1555 1555 1.33
LINK C GLU A 426 N MLY A 427 1555 1555 1.33
LINK C MLY A 427 N GLY A 428 1555 1555 1.33
LINK C LEU A 488 N MLY A 489 1555 1555 1.33
LINK C MLY A 489 N TYR A 490 1555 1555 1.33
LINK C PHE A 495 N MLY A 496 1555 1555 1.32
LINK C MLY A 496 N ASP A 497 1555 1555 1.34
LINK C GLU A 502 N MLY A 503 1555 1555 1.33
LINK C MLY A 503 N PHE A 504 1555 1555 1.33
CISPEP 1 VAL A 274 PRO A 275 0 -4.55
CISPEP 2 TYR A 322 ASN A 323 0 7.81
SITE 1 AC1 7 GLY A 109 ALA A 110 PHE A 113 SER A 188
SITE 2 AC1 7 ALA A 189 TYR A 322 HIS A 445
CRYST1 67.713 80.645 107.038 90.00 90.00 90.00 P 21 21 21 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 0.014768 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012400 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009342 0.00000
TER 4253 PRO A 523
MASTER 286 0 33 23 18 0 2 6 4513 1 428 41
END |