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HEADER BIOSYNTHETIC PROTEIN 17-MAY-19 6K3C
TITLE CRYSTAL STRUCTURE OF CLASS I PHA SYNTHASE (PHAC) MUTANT FROM
TITLE 2 CHROMOBACTERIUM SP. USM2 BOUND TO COENZYME A.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTRACELLULAR POLYHYDROXYALKANOATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHROMOBACTERIUM SP. USM2;
SOURCE 3 ORGANISM_TAXID: 611307;
SOURCE 4 GENE: PHAC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BIOPLASTIC SYNTHASE, CATALYTIC DOMAIN, COA BINDING., BIOSYNTHETIC
KEYWDS 2 PROTEIN, OPEN CONFORMATION, OPEN-CLOSED DIMER
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.CHEK,S.Y.KIM,T.MORI,T.HAKOSHIMA
REVDAT 2 27-MAY-20 6K3C 1 JRNL
REVDAT 1 29-APR-20 6K3C 0
JRNL AUTH M.F.CHEK,S.Y.KIM,T.MORI,H.T.TAN,K.SUDESH,T.HAKOSHIMA
JRNL TITL ASYMMETRIC OPEN-CLOSED DIMER MECHANISM OF
JRNL TITL 2 POLYHYDROXYALKANOATE SYNTHASE PHAC.
JRNL REF ISCIENCE V. 23 01084 2020
JRNL REFN ESSN 2589-0042
JRNL PMID 32388399
JRNL DOI 10.1016/J.ISCI.2020.101084
REMARK 2
REMARK 2 RESOLUTION. 3.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575)
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) : 3.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 14647
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 731
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 49.9598 - 5.2556 0.98 2961 156 0.1832 0.2199
REMARK 3 2 5.2556 - 4.1722 0.98 2881 151 0.2032 0.2108
REMARK 3 3 4.1722 - 3.6450 0.99 2908 153 0.2444 0.2877
REMARK 3 4 3.6450 - 3.3118 0.96 2808 147 0.3141 0.3746
REMARK 3 5 3.3118 - 3.0745 0.81 2358 124 0.3582 0.4502
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) : 0.550
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.110
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 : 0.004 6072
REMARK 3 ANGLE : 0.699 8287
REMARK 3 CHIRALITY : 0.046 901
REMARK 3 PLANARITY : 0.004 1048
REMARK 3 DIHEDRAL : 15.616 2182
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 6K3C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1300011846.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97914
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15234
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.074
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 : 3.300
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.07
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.51300
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 (1.11.1_2575)
REMARK 200 STARTING MODEL: 5XAV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PEG3350, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 84.90100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.92600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.90100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.92600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY A 173
REMARK 465 VAL A 562
REMARK 465 ALA A 563
REMARK 465 ALA A 564
REMARK 465 ALA A 565
REMARK 465 LEU A 566
REMARK 465 ASN A 567
REMARK 465 GLY B 173
REMARK 465 PRO B 174
REMARK 465 PHE B 175
REMARK 465 GLN B 176
REMARK 465 ALA B 347
REMARK 465 ALA B 348
REMARK 465 GLY B 349
REMARK 465 GLY B 350
REMARK 465 ILE B 351
REMARK 465 ILE B 352
REMARK 465 SER B 353
REMARK 465 GLY B 354
REMARK 465 LYS B 355
REMARK 465 ILE B 478
REMARK 465 ALA B 479
REMARK 465 GLY B 480
REMARK 465 SER B 481
REMARK 465 ILE B 482
REMARK 465 ASN B 483
REMARK 465 PRO B 484
REMARK 465 VAL B 485
REMARK 465 THR B 486
REMARK 465 LYS B 487
REMARK 465 ASP B 488
REMARK 465 PRO B 548
REMARK 465 ALA B 549
REMARK 465 PRO B 550
REMARK 465 GLY B 551
REMARK 465 SER B 552
REMARK 465 TYR B 553
REMARK 465 VAL B 554
REMARK 465 LEU B 555
REMARK 465 ALA B 556
REMARK 465 LYS B 557
REMARK 465 ALA B 558
REMARK 465 MET B 559
REMARK 465 PRO B 560
REMARK 465 PRO B 561
REMARK 465 VAL B 562
REMARK 465 ALA B 563
REMARK 465 ALA B 564
REMARK 465 ALA B 565
REMARK 465 LEU B 566
REMARK 465 ASN B 567
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 ASN A 220 -163.59 -109.68
REMARK 500 LEU A 227 -80.87 -84.85
REMARK 500 GLU A 266 -74.92 -73.43
REMARK 500 CYS A 291 -125.34 50.21
REMARK 500 LYS A 345 45.73 -109.93
REMARK 500 PHE A 361 -59.00 -132.00
REMARK 500 LEU A 379 -73.33 -64.98
REMARK 500 ASN A 415 75.04 54.69
REMARK 500 GLU A 446 31.17 -75.01
REMARK 500 LEU A 462 59.75 -98.40
REMARK 500 SER A 475 -154.10 -109.65
REMARK 500 ASP A 488 73.68 51.84
REMARK 500 ASN B 192 -151.34 -148.09
REMARK 500 CYS B 218 49.77 -69.77
REMARK 500 LEU B 227 -53.47 -138.07
REMARK 500 GLU B 266 -74.76 -67.42
REMARK 500 CYS B 291 -151.21 58.39
REMARK 500 HIS B 324 34.14 -86.30
REMARK 500 LEU B 546 -158.20 -81.88
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 A 607 DISTANCE = 6.20 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue COA B 601
DBREF 6K3C A 175 567 UNP E1APK1 E1APK1_9NEIS 175 567
DBREF 6K3C B 175 567 UNP E1APK1 E1APK1_9NEIS 175 567
SEQADV 6K3C GLY A 173 UNP E1APK1 EXPRESSION TAG
SEQADV 6K3C PRO A 174 UNP E1APK1 EXPRESSION TAG
SEQADV 6K3C ASN A 447 UNP E1APK1 ASP 447 ENGINEERED MUTATION
SEQADV 6K3C GLY B 173 UNP E1APK1 EXPRESSION TAG
SEQADV 6K3C PRO B 174 UNP E1APK1 EXPRESSION TAG
SEQADV 6K3C ASN B 447 UNP E1APK1 ASP 447 ENGINEERED MUTATION
SEQRES 1 A 395 GLY PRO PHE GLN ILE GLY LYS ASN LEU VAL VAL THR PRO
SEQRES 2 A 395 GLY GLU VAL VAL PHE ARG ASN GLU LEU ILE GLU LEU ILE
SEQRES 3 A 395 GLN TYR THR PRO THR THR GLU LYS VAL HIS GLU LYS PRO
SEQRES 4 A 395 LEU LEU PHE VAL PRO PRO CYS ILE ASN LYS TYR TYR LEU
SEQRES 5 A 395 MET ASP LEU GLN PRO ASP ASN SER MET VAL ARG HIS PHE
SEQRES 6 A 395 VAL GLY GLN GLY TYR ARG VAL PHE LEU VAL SER TRP ARG
SEQRES 7 A 395 SER ALA VAL PRO GLU MET LYS ASN PHE THR TRP GLU THR
SEQRES 8 A 395 TYR ILE GLU LYS GLY VAL PHE ALA ALA ALA GLU ALA VAL
SEQRES 9 A 395 GLN LYS ILE THR LYS GLN PRO THR MET ASN ALA LEU GLY
SEQRES 10 A 395 PHE CYS VAL GLY GLY VAL ILE LEU THR THR ALA LEU CYS
SEQRES 11 A 395 VAL ALA GLN ALA LYS GLY LEU LYS TYR PHE ASP SER ALA
SEQRES 12 A 395 THR PHE MET THR SER LEU ILE ASP HIS ALA GLU PRO GLY
SEQRES 13 A 395 GLU ILE SER PHE PHE ILE ASP GLU ALA LEU VAL ALA SER
SEQRES 14 A 395 ARG GLU ALA LYS MET ALA ALA GLY GLY ILE ILE SER GLY
SEQRES 15 A 395 LYS GLU ILE GLY ARG THR PHE ALA SER LEU ARG ALA ASN
SEQRES 16 A 395 ASP LEU VAL TRP ASN TYR VAL VAL ASN ASN TYR LEU LEU
SEQRES 17 A 395 GLY LYS THR PRO ALA PRO PHE ASP LEU LEU TYR TRP ASN
SEQRES 18 A 395 ASN ASP ALA VAL ASP LEU PRO LEU PRO MET HIS THR PHE
SEQRES 19 A 395 MET LEU ARG GLN PHE TYR ILE ASN ASN ALA LEU ILE THR
SEQRES 20 A 395 PRO GLY ALA ILE THR LEU CYS GLY VAL PRO ILE ASP ILE
SEQRES 21 A 395 SER LYS ILE ASP ILE PRO VAL TYR MET PHE ALA ALA ARG
SEQRES 22 A 395 GLU ASN HIS ILE VAL LEU TRP SER SER ALA TYR SER GLY
SEQRES 23 A 395 LEU LYS TYR LEU SER GLY THR PRO SER ARG ARG PHE VAL
SEQRES 24 A 395 LEU GLY ALA SER GLY HIS ILE ALA GLY SER ILE ASN PRO
SEQRES 25 A 395 VAL THR LYS ASP LYS ARG ASN TYR TRP THR ASN GLU GLN
SEQRES 26 A 395 LEU PRO VAL ASN PRO GLU GLU TRP LEU GLU GLY ALA GLN
SEQRES 27 A 395 SER HIS PRO GLY SER TRP TRP LYS ASP TRP ASP ALA TRP
SEQRES 28 A 395 LEU ALA PRO GLN SER GLY LYS GLN VAL PRO ALA PRO LYS
SEQRES 29 A 395 MET LEU GLY SER LYS GLU PHE PRO PRO LEU GLN PRO ALA
SEQRES 30 A 395 PRO GLY SER TYR VAL LEU ALA LYS ALA MET PRO PRO VAL
SEQRES 31 A 395 ALA ALA ALA LEU ASN
SEQRES 1 B 395 GLY PRO PHE GLN ILE GLY LYS ASN LEU VAL VAL THR PRO
SEQRES 2 B 395 GLY GLU VAL VAL PHE ARG ASN GLU LEU ILE GLU LEU ILE
SEQRES 3 B 395 GLN TYR THR PRO THR THR GLU LYS VAL HIS GLU LYS PRO
SEQRES 4 B 395 LEU LEU PHE VAL PRO PRO CYS ILE ASN LYS TYR TYR LEU
SEQRES 5 B 395 MET ASP LEU GLN PRO ASP ASN SER MET VAL ARG HIS PHE
SEQRES 6 B 395 VAL GLY GLN GLY TYR ARG VAL PHE LEU VAL SER TRP ARG
SEQRES 7 B 395 SER ALA VAL PRO GLU MET LYS ASN PHE THR TRP GLU THR
SEQRES 8 B 395 TYR ILE GLU LYS GLY VAL PHE ALA ALA ALA GLU ALA VAL
SEQRES 9 B 395 GLN LYS ILE THR LYS GLN PRO THR MET ASN ALA LEU GLY
SEQRES 10 B 395 PHE CYS VAL GLY GLY VAL ILE LEU THR THR ALA LEU CYS
SEQRES 11 B 395 VAL ALA GLN ALA LYS GLY LEU LYS TYR PHE ASP SER ALA
SEQRES 12 B 395 THR PHE MET THR SER LEU ILE ASP HIS ALA GLU PRO GLY
SEQRES 13 B 395 GLU ILE SER PHE PHE ILE ASP GLU ALA LEU VAL ALA SER
SEQRES 14 B 395 ARG GLU ALA LYS MET ALA ALA GLY GLY ILE ILE SER GLY
SEQRES 15 B 395 LYS GLU ILE GLY ARG THR PHE ALA SER LEU ARG ALA ASN
SEQRES 16 B 395 ASP LEU VAL TRP ASN TYR VAL VAL ASN ASN TYR LEU LEU
SEQRES 17 B 395 GLY LYS THR PRO ALA PRO PHE ASP LEU LEU TYR TRP ASN
SEQRES 18 B 395 ASN ASP ALA VAL ASP LEU PRO LEU PRO MET HIS THR PHE
SEQRES 19 B 395 MET LEU ARG GLN PHE TYR ILE ASN ASN ALA LEU ILE THR
SEQRES 20 B 395 PRO GLY ALA ILE THR LEU CYS GLY VAL PRO ILE ASP ILE
SEQRES 21 B 395 SER LYS ILE ASP ILE PRO VAL TYR MET PHE ALA ALA ARG
SEQRES 22 B 395 GLU ASN HIS ILE VAL LEU TRP SER SER ALA TYR SER GLY
SEQRES 23 B 395 LEU LYS TYR LEU SER GLY THR PRO SER ARG ARG PHE VAL
SEQRES 24 B 395 LEU GLY ALA SER GLY HIS ILE ALA GLY SER ILE ASN PRO
SEQRES 25 B 395 VAL THR LYS ASP LYS ARG ASN TYR TRP THR ASN GLU GLN
SEQRES 26 B 395 LEU PRO VAL ASN PRO GLU GLU TRP LEU GLU GLY ALA GLN
SEQRES 27 B 395 SER HIS PRO GLY SER TRP TRP LYS ASP TRP ASP ALA TRP
SEQRES 28 B 395 LEU ALA PRO GLN SER GLY LYS GLN VAL PRO ALA PRO LYS
SEQRES 29 B 395 MET LEU GLY SER LYS GLU PHE PRO PRO LEU GLN PRO ALA
SEQRES 30 B 395 PRO GLY SER TYR VAL LEU ALA LYS ALA MET PRO PRO VAL
SEQRES 31 B 395 ALA ALA ALA LEU ASN
HET COA B 601 48
HETNAM COA COENZYME A
FORMUL 3 COA C21 H36 N7 O16 P3 S
FORMUL 4 HOH *14(H2 O)
HELIX 1 AA1 LYS A 221 ASP A 226 5 6
HELIX 2 AA2 SER A 232 GLY A 241 1 10
HELIX 3 AA3 VAL A 253 LYS A 257 5 5
HELIX 4 AA4 THR A 260 LYS A 267 1 8
HELIX 5 AA5 GLY A 268 LYS A 281 1 14
HELIX 6 AA6 CYS A 291 LYS A 307 1 17
HELIX 7 AA7 GLY A 328 ILE A 334 5 7
HELIX 8 AA8 ASP A 335 LYS A 345 1 11
HELIX 9 AA9 SER A 353 PHE A 361 1 9
HELIX 10 AB1 PHE A 361 LEU A 380 1 20
HELIX 11 AB2 PRO A 386 ASP A 395 1 10
HELIX 12 AB3 LEU A 401 PHE A 411 1 11
HELIX 13 AB4 LEU A 451 SER A 457 1 7
HELIX 14 AB5 GLY A 458 LEU A 462 5 5
HELIX 15 AB6 GLY A 476 ILE A 482 1 7
HELIX 16 AB7 ASN A 501 GLY A 508 1 8
HELIX 17 AB8 TRP A 516 ALA A 525 1 10
HELIX 18 AB9 SER A 552 ALA A 556 5 5
HELIX 19 AC1 ASN B 231 GLN B 240 1 10
HELIX 20 AC2 VAL B 253 LYS B 257 5 5
HELIX 21 AC3 THR B 260 LYS B 267 1 8
HELIX 22 AC4 GLY B 268 THR B 280 1 13
HELIX 23 AC5 CYS B 291 GLN B 305 1 15
HELIX 24 AC6 GLY B 328 PHE B 333 5 6
HELIX 25 AC7 ASP B 335 LYS B 345 1 11
HELIX 26 AC8 THR B 360 LEU B 364 5 5
HELIX 27 AC9 ASN B 367 LEU B 380 1 14
HELIX 28 AD1 ASP B 388 ASN B 393 1 6
HELIX 29 AD2 ASN B 394 LEU B 399 1 6
HELIX 30 AD3 PRO B 400 PHE B 411 1 12
HELIX 31 AD4 ASP B 431 ILE B 435 5 5
HELIX 32 AD5 LEU B 451 GLY B 458 1 8
HELIX 33 AD6 ASN B 501 GLY B 508 1 8
HELIX 34 AD7 TRP B 516 ALA B 525 1 10
HELIX 35 AD8 PRO B 526 GLY B 529 5 4
SHEET 1 AA110 GLY A 186 ARG A 191 0
SHEET 2 AA110 ILE A 195 TYR A 200 -1 O LEU A 197 N PHE A 190
SHEET 3 AA110 VAL A 244 TRP A 249 -1 O VAL A 244 N TYR A 200
SHEET 4 AA110 LEU A 212 VAL A 215 1 N LEU A 212 O PHE A 245
SHEET 5 AA110 ASN A 286 PHE A 290 1 O LEU A 288 N VAL A 215
SHEET 6 AA110 ALA A 315 MET A 318 1 O THR A 316 N GLY A 289
SHEET 7 AA110 VAL A 439 ALA A 444 1 O PHE A 442 N PHE A 317
SHEET 8 AA110 ARG A 468 GLY A 473 1 O GLY A 473 N ALA A 443
SHEET 9 AA110 TYR A 492 THR A 494 -1 O TRP A 493 N LEU A 472
SHEET 10 AA110 GLN A 510 HIS A 512 -1 O GLN A 510 N THR A 494
SHEET 1 AA2 2 LYS A 206 HIS A 208 0
SHEET 2 AA2 2 GLN A 531 PRO A 533 -1 O VAL A 532 N VAL A 207
SHEET 1 AA3 2 ILE A 351 ILE A 352 0
SHEET 2 AA3 2 LEU A 399 PRO A 400 -1 O LEU A 399 N ILE A 352
SHEET 1 AA4 2 THR A 424 LEU A 425 0
SHEET 2 AA4 2 VAL A 428 PRO A 429 -1 O VAL A 428 N LEU A 425
SHEET 1 AA510 GLY B 186 ARG B 191 0
SHEET 2 AA510 ILE B 195 TYR B 200 -1 O LEU B 197 N PHE B 190
SHEET 3 AA510 VAL B 244 TRP B 249 -1 O SER B 248 N GLU B 196
SHEET 4 AA510 LEU B 212 VAL B 215 1 N LEU B 212 O PHE B 245
SHEET 5 AA510 MET B 285 PHE B 290 1 O LEU B 288 N VAL B 215
SHEET 6 AA510 PHE B 312 MET B 318 1 O THR B 316 N GLY B 289
SHEET 7 AA510 VAL B 439 ALA B 444 1 O PHE B 442 N PHE B 317
SHEET 8 AA510 ARG B 468 ALA B 474 1 O ARG B 469 N MET B 441
SHEET 9 AA510 ASN B 491 ASN B 495 -1 O ASN B 491 N ALA B 474
SHEET 10 AA510 GLN B 510 PRO B 513 -1 O GLN B 510 N THR B 494
SHEET 1 AA6 2 LYS B 206 HIS B 208 0
SHEET 2 AA6 2 GLN B 531 PRO B 533 -1 O VAL B 532 N VAL B 207
CISPEP 1 ALA A 549 PRO A 550 0 4.97
SITE 1 AC1 9 ILE B 177 TYR B 223 MET B 225 CYS B 291
SITE 2 AC1 9 LEU B 380 GLY B 381 LYS B 382 ASN B 447
SITE 3 AC1 9 ILE B 449
CRYST1 169.802 61.852 82.566 90.00 106.73 90.00 C 1 2 1 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 0.005889 0.000000 0.001770 0.00000
SCALE2 0.000000 0.016168 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012647 0.00000
TER 3051 PRO A 561
TER 5848 GLN B 547
MASTER 308 0 1 35 28 0 3 6 5908 2 48 62
END |