| 4I4C-pdb | HEADER UNKNOWN FUNCTION 27-NOV-12 4I4C
TITLE CRYSTAL STRUCTURE OF THE PROTEIN FRSA COMPLEXED WITH UNKNOWN LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UPF0255 PROTEIN FRSA;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO VULNIFICUS;
SOURCE 3 ORGANISM_TAXID: 672;
SOURCE 4 GENE: FRSA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TWO-DOMAIN PROTEIN FRSA, UNKNOWN FUNCTION, UNKNOWN LIGAND
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FEDOROV,E.V.FEDOROV,B.DESAI,J.A.GERLT,N.RICHARDS,S.C.ALMO
REVDAT 1 09-OCT-13 4I4C 0
JRNL AUTH W.F.KELLETT,E.BRUNK,B.J.DESAI,A.A.FEDOROV,S.C.ALMO,
JRNL AUTH 2 J.A.GERLT,U.ROTHLISBERGER,N.G.RICHARDS
JRNL TITL COMPUTATIONAL, STRUCTURAL, AND KINETIC EVIDENCE THAT VIBRIO
JRNL TITL 2 VULNIFICUS FRSA IS NOT A COFACTOR-INDEPENDENT PYRUVATE
JRNL TITL 3 DECARBOXYLASE.
JRNL REF BIOCHEMISTRY V. 52 1842 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 23452154
JRNL DOI 10.1021/BI400093Y
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 51363
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2608
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 38.2916 - 5.1993 1.00 2672 142 0.1465 0.1586
REMARK 3 2 5.1993 - 4.1284 1.00 2634 153 0.1342 0.1827
REMARK 3 3 4.1284 - 3.6070 1.00 2611 143 0.1487 0.1790
REMARK 3 4 3.6070 - 3.2774 0.98 2606 117 0.1751 0.2431
REMARK 3 5 3.2774 - 3.0426 0.96 2522 146 0.1922 0.2279
REMARK 3 6 3.0426 - 2.8633 0.96 2526 128 0.1890 0.2432
REMARK 3 7 2.8633 - 2.7199 0.96 2529 158 0.2015 0.2258
REMARK 3 8 2.7199 - 2.6015 0.97 2549 130 0.1965 0.2602
REMARK 3 9 2.6015 - 2.5014 0.97 2511 140 0.2060 0.3009
REMARK 3 10 2.5014 - 2.4151 0.98 2574 143 0.2110 0.2397
REMARK 3 11 2.4151 - 2.3396 0.98 2550 135 0.2067 0.3044
REMARK 3 12 2.3396 - 2.2727 0.97 2556 139 0.2049 0.2838
REMARK 3 13 2.2727 - 2.2129 0.98 2567 115 0.2050 0.2633
REMARK 3 14 2.2129 - 2.1589 0.98 2550 152 0.2044 0.2806
REMARK 3 15 2.1589 - 2.1098 0.98 2553 129 0.2125 0.2783
REMARK 3 16 2.1098 - 2.0649 0.98 2567 153 0.2193 0.3182
REMARK 3 17 2.0649 - 2.0236 0.98 2567 130 0.2290 0.3061
REMARK 3 18 2.0236 - 1.9855 0.98 2571 131 0.2346 0.3002
REMARK 3 19 1.9855 - 1.9500 0.98 2540 124 0.2465 0.2882
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.330
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 : 0.008 6609
REMARK 3 ANGLE : 1.053 8925
REMARK 3 CHIRALITY : 0.072 972
REMARK 3 PLANARITY : 0.004 1125
REMARK 3 DIHEDRAL : 15.081 2469
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3107 17.1156 81.7416
REMARK 3 T TENSOR
REMARK 3 T11: 0.1446 T22: 0.1183
REMARK 3 T33: 0.1497 T12: -0.0025
REMARK 3 T13: -0.0206 T23: 0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 0.9237 L22: 1.4985
REMARK 3 L33: 1.2091 L12: -0.2360
REMARK 3 L13: -0.1698 L23: 0.5780
REMARK 3 S TENSOR
REMARK 3 S11: 0.0616 S12: 0.0112 S13: -0.0899
REMARK 3 S21: -0.2386 S22: 0.0031 S23: -0.0397
REMARK 3 S31: 0.0035 S32: -0.0474 S33: -0.0544
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain B
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5066 36.7994 41.7463
REMARK 3 T TENSOR
REMARK 3 T11: 0.1432 T22: 0.1457
REMARK 3 T33: 0.1266 T12: -0.0159
REMARK 3 T13: 0.0154 T23: -0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 0.7679 L22: 1.6510
REMARK 3 L33: 0.6416 L12: 0.0877
REMARK 3 L13: 0.2143 L23: 0.1930
REMARK 3 S TENSOR
REMARK 3 S11: 0.0387 S12: -0.0708 S13: 0.0329
REMARK 3 S21: 0.2413 S22: -0.0406 S23: -0.0278
REMARK 3 S31: 0.0369 S32: -0.0682 S33: 0.0043
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 4I4C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-12.
REMARK 100 THE RCSB ID CODE IS RCSB076287.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JAN-12
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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51363
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 38.284
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: BALBES
REMARK 200 STARTING MODEL: 3MVE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG MONOMETHYL ETHER 2000, 0.1M
REMARK 280 TRIS, 0.2M TRIMETHYLAMINE N-OXIDE, PH 8.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293.0K
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 52.27100
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 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 VAL A 5
REMARK 465 SER A 6
REMARK 465 LYS A 7
REMARK 465 ASN A 8
REMARK 465 LEU A 9
REMARK 465 SER A 10
REMARK 465 GLU A 11
REMARK 465 THR A 12
REMARK 465 LEU A 13
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
REMARK 465 VAL B 5
REMARK 465 SER B 6
REMARK 465 LYS B 7
REMARK 465 ASN B 8
REMARK 465 LEU B 9
REMARK 465 SER B 10
REMARK 465 GLU B 11
REMARK 465 THR B 12
REMARK 465 LEU B 13
REMARK 465 PHE B 14
REMARK 465 VAL B 15
REMARK 465 LYS B 16
REMARK 465 HIS B 17
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 118 -118.76 54.73
REMARK 500 PHE A 175 118.63 -170.71
REMARK 500 LYS A 177 -7.64 70.92
REMARK 500 HIS A 216 -67.95 -134.51
REMARK 500 SER A 231 -10.21 89.26
REMARK 500 ARG A 272 -137.44 48.79
REMARK 500 HIS A 300 -53.78 -153.57
REMARK 500 SER A 351 -48.82 -142.60
REMARK 500 LEU A 414 42.21 -89.53
REMARK 500 GLN B 19 35.15 -96.82
REMARK 500 PHE B 175 121.98 -173.84
REMARK 500 HIS B 216 -65.23 -131.35
REMARK 500 LYS B 219 -19.80 -49.41
REMARK 500 SER B 231 -5.40 82.56
REMARK 500 THR B 241 -164.11 -109.07
REMARK 500 ASP B 243 63.81 -100.58
REMARK 500 ARG B 272 -130.52 47.79
REMARK 500 HIS B 300 -56.54 -151.39
REMARK 500 SER B 350 -52.81 -124.56
REMARK 500 SER B 351 -53.59 -143.27
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 1PG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6NA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6NA B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MVE RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER LIGANDS
REMARK 900 RELATED ID: 3OUR RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ANOTHER PROTEIN
DBREF 4I4C A 1 415 UNP D9IR22 D9IR22_VIBVL 1 415
DBREF 4I4C B 1 415 UNP D9IR22 D9IR22_VIBVL 1 415
SEQRES 1 A 415 MET SER GLU GLU VAL SER LYS ASN LEU SER GLU THR LEU
SEQRES 2 A 415 PHE VAL LYS HIS LYS GLN ALA LYS GLU THR SER ALA LEU
SEQRES 3 A 415 THR GLN TYR MET PRO THR SER GLN SER LEU LEU ASP GLU
SEQRES 4 A 415 ILE LYS GLU LYS ASN GLY PHE SER TRP TYR ARG ASN LEU
SEQRES 5 A 415 ARG ARG LEU GLN TRP VAL TRP GLN GLY VAL ASP PRO ILE
SEQRES 6 A 415 GLU GLN GLU GLN VAL LEU ALA ARG ILE ALA SER SER LYS
SEQRES 7 A 415 HIS SER ARG THR ASP GLU GLN TRP LEU ASP THR VAL MET
SEQRES 8 A 415 GLY TYR HIS SER GLY ASN TRP ALA TYR GLU TRP THR ARG
SEQRES 9 A 415 LEU GLY MET GLU HIS GLN LYS ARG ALA GLY GLU MET THR
SEQRES 10 A 415 ASN GLU ALA ALA SER GLU ALA LEU PHE SER ALA SER LEU
SEQRES 11 A 415 CYS TYR SER ILE ALA GLY TYR PRO HIS LEU LYS SER ASP
SEQRES 12 A 415 ASN LEU ALA ILE GLN ALA GLN VAL LEU ALA ASN SER ALA
SEQRES 13 A 415 TYR LEU GLU ALA ALA LYS LYS SER LYS TYR ILE ILE LYS
SEQRES 14 A 415 GLN LEU GLU ILE PRO PHE GLU LYS GLY LYS ILE THR ALA
SEQRES 15 A 415 HIS LEU HIS LEU THR ASN THR ASP LYS PRO HIS PRO VAL
SEQRES 16 A 415 VAL ILE VAL SER ALA GLY LEU ASP SER LEU GLN THR ASP
SEQRES 17 A 415 MET TRP ARG LEU PHE ARG ASP HIS LEU ALA LYS HIS ASP
SEQRES 18 A 415 ILE ALA MET LEU THR VAL ASP MET PRO SER VAL GLY TYR
SEQRES 19 A 415 SER SER LYS TYR PRO LEU THR GLU ASP TYR SER ARG LEU
SEQRES 20 A 415 HIS GLN ALA VAL LEU ASN GLU LEU PHE SER ILE PRO TYR
SEQRES 21 A 415 VAL ASP HIS HIS ARG VAL GLY LEU ILE GLY PHE ARG PHE
SEQRES 22 A 415 GLY GLY ASN ALA MET VAL ARG LEU SER PHE LEU GLU GLN
SEQRES 23 A 415 GLU LYS ILE LYS ALA CYS VAL ILE LEU GLY ALA PRO ILE
SEQRES 24 A 415 HIS ASP ILE PHE ALA SER PRO GLN LYS LEU GLN GLN MET
SEQRES 25 A 415 PRO LYS MET TYR LEU ASP VAL LEU ALA SER ARG LEU GLY
SEQRES 26 A 415 LYS SER VAL VAL ASP ILE TYR SER LEU SER GLY GLN MET
SEQRES 27 A 415 ALA ALA TRP SER LEU LYS VAL GLN GLY PHE LEU SER SER
SEQRES 28 A 415 ARG LYS THR LYS VAL PRO ILE LEU ALA MET SER LEU GLU
SEQRES 29 A 415 GLY ASP PRO VAL SER PRO TYR SER ASP ASN GLN MET VAL
SEQRES 30 A 415 ALA PHE PHE SER THR TYR GLY LYS ALA LYS LYS ILE SER
SEQRES 31 A 415 SER LYS THR ILE THR GLN GLY TYR GLU GLN SER LEU ASP
SEQRES 32 A 415 LEU ALA ILE LYS TRP LEU GLU ASP GLU LEU LEU ARG
SEQRES 1 B 415 MET SER GLU GLU VAL SER LYS ASN LEU SER GLU THR LEU
SEQRES 2 B 415 PHE VAL LYS HIS LYS GLN ALA LYS GLU THR SER ALA LEU
SEQRES 3 B 415 THR GLN TYR MET PRO THR SER GLN SER LEU LEU ASP GLU
SEQRES 4 B 415 ILE LYS GLU LYS ASN GLY PHE SER TRP TYR ARG ASN LEU
SEQRES 5 B 415 ARG ARG LEU GLN TRP VAL TRP GLN GLY VAL ASP PRO ILE
SEQRES 6 B 415 GLU GLN GLU GLN VAL LEU ALA ARG ILE ALA SER SER LYS
SEQRES 7 B 415 HIS SER ARG THR ASP GLU GLN TRP LEU ASP THR VAL MET
SEQRES 8 B 415 GLY TYR HIS SER GLY ASN TRP ALA TYR GLU TRP THR ARG
SEQRES 9 B 415 LEU GLY MET GLU HIS GLN LYS ARG ALA GLY GLU MET THR
SEQRES 10 B 415 ASN GLU ALA ALA SER GLU ALA LEU PHE SER ALA SER LEU
SEQRES 11 B 415 CYS TYR SER ILE ALA GLY TYR PRO HIS LEU LYS SER ASP
SEQRES 12 B 415 ASN LEU ALA ILE GLN ALA GLN VAL LEU ALA ASN SER ALA
SEQRES 13 B 415 TYR LEU GLU ALA ALA LYS LYS SER LYS TYR ILE ILE LYS
SEQRES 14 B 415 GLN LEU GLU ILE PRO PHE GLU LYS GLY LYS ILE THR ALA
SEQRES 15 B 415 HIS LEU HIS LEU THR ASN THR ASP LYS PRO HIS PRO VAL
SEQRES 16 B 415 VAL ILE VAL SER ALA GLY LEU ASP SER LEU GLN THR ASP
SEQRES 17 B 415 MET TRP ARG LEU PHE ARG ASP HIS LEU ALA LYS HIS ASP
SEQRES 18 B 415 ILE ALA MET LEU THR VAL ASP MET PRO SER VAL GLY TYR
SEQRES 19 B 415 SER SER LYS TYR PRO LEU THR GLU ASP TYR SER ARG LEU
SEQRES 20 B 415 HIS GLN ALA VAL LEU ASN GLU LEU PHE SER ILE PRO TYR
SEQRES 21 B 415 VAL ASP HIS HIS ARG VAL GLY LEU ILE GLY PHE ARG PHE
SEQRES 22 B 415 GLY GLY ASN ALA MET VAL ARG LEU SER PHE LEU GLU GLN
SEQRES 23 B 415 GLU LYS ILE LYS ALA CYS VAL ILE LEU GLY ALA PRO ILE
SEQRES 24 B 415 HIS ASP ILE PHE ALA SER PRO GLN LYS LEU GLN GLN MET
SEQRES 25 B 415 PRO LYS MET TYR LEU ASP VAL LEU ALA SER ARG LEU GLY
SEQRES 26 B 415 LYS SER VAL VAL ASP ILE TYR SER LEU SER GLY GLN MET
SEQRES 27 B 415 ALA ALA TRP SER LEU LYS VAL GLN GLY PHE LEU SER SER
SEQRES 28 B 415 ARG LYS THR LYS VAL PRO ILE LEU ALA MET SER LEU GLU
SEQRES 29 B 415 GLY ASP PRO VAL SER PRO TYR SER ASP ASN GLN MET VAL
SEQRES 30 B 415 ALA PHE PHE SER THR TYR GLY LYS ALA LYS LYS ILE SER
SEQRES 31 B 415 SER LYS THR ILE THR GLN GLY TYR GLU GLN SER LEU ASP
SEQRES 32 B 415 LEU ALA ILE LYS TRP LEU GLU ASP GLU LEU LEU ARG
HET 1PG A 501 17
HET 6NA A 502 8
HET 1PG B 501 17
HET GOL B 502 6
HET 6NA B 503 8
HETNAM 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-
HETNAM 2 1PG ETHANOL
HETNAM 6NA HEXANOIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 1PG 2(C11 H24 O6)
FORMUL 4 6NA 2(C6 H12 O2)
FORMUL 6 GOL C3 H8 O3
FORMUL 8 HOH *274(H2 O)
HELIX 1 1 PHE A 14 LYS A 18 5 5
HELIX 2 2 GLU A 22 LEU A 26 5 5
HELIX 3 3 MET A 30 GLY A 45 1 16
HELIX 4 4 ARG A 53 GLY A 61 1 9
HELIX 5 5 ASP A 63 SER A 76 1 14
HELIX 6 6 ASN A 97 GLU A 115 1 19
HELIX 7 7 ALA A 120 TYR A 137 1 18
HELIX 8 8 ASP A 143 SER A 164 1 22
HELIX 9 9 LEU A 205 ASP A 208 5 4
HELIX 10 10 MET A 209 HIS A 216 1 8
HELIX 11 11 LEU A 217 ASP A 221 5 5
HELIX 12 12 VAL A 232 SER A 236 5 5
HELIX 13 13 SER A 245 LEU A 255 1 11
HELIX 14 14 PHE A 256 ILE A 258 5 3
HELIX 15 15 ARG A 272 GLU A 285 1 14
HELIX 16 16 SER A 305 GLN A 310 1 6
HELIX 17 17 PRO A 313 LEU A 324 1 12
HELIX 18 18 ASP A 330 MET A 338 1 9
HELIX 19 19 ALA A 339 SER A 342 5 4
HELIX 20 20 PRO A 370 PHE A 380 1 11
HELIX 21 21 THR A 393 LEU A 414 1 22
HELIX 22 22 GLU B 22 LEU B 26 5 5
HELIX 23 23 MET B 30 GLY B 45 1 16
HELIX 24 24 ARG B 53 GLY B 61 1 9
HELIX 25 25 ASP B 63 SER B 76 1 14
HELIX 26 26 ASN B 97 GLY B 114 1 18
HELIX 27 27 THR B 117 TYR B 137 1 21
HELIX 28 28 ASP B 143 SER B 164 1 22
HELIX 29 29 LEU B 205 ASP B 208 5 4
HELIX 30 30 MET B 209 HIS B 216 1 8
HELIX 31 31 LEU B 217 ASP B 221 5 5
HELIX 32 32 VAL B 232 SER B 236 5 5
HELIX 33 33 SER B 245 ASN B 253 1 9
HELIX 34 34 ARG B 272 GLU B 285 1 14
HELIX 35 35 SER B 305 GLN B 310 1 6
HELIX 36 36 PRO B 313 LEU B 324 1 12
HELIX 37 37 ASP B 330 MET B 338 1 9
HELIX 38 38 ALA B 339 SER B 342 5 4
HELIX 39 39 PRO B 370 PHE B 380 1 11
HELIX 40 40 THR B 393 LEU B 414 1 22
SHEET 1 A 2 GLN A 28 TYR A 29 0
SHEET 2 A 2 VAL A 328 VAL A 329 1 O VAL A 329 N GLN A 28
SHEET 1 B 8 ILE A 167 PHE A 175 0
SHEET 2 B 8 GLY A 178 LEU A 186 -1 O LEU A 186 N ILE A 167
SHEET 3 B 8 ALA A 223 THR A 226 -1 O MET A 224 N HIS A 185
SHEET 4 B 8 HIS A 193 SER A 199 1 N PRO A 194 O ALA A 223
SHEET 5 B 8 VAL A 261 PHE A 271 1 O GLY A 267 N VAL A 195
SHEET 6 B 8 ALA A 291 LEU A 295 1 O VAL A 293 N LEU A 268
SHEET 7 B 8 ILE A 358 LEU A 363 1 O LEU A 359 N CYS A 292
SHEET 8 B 8 LYS A 385 ILE A 389 1 O LYS A 385 N ALA A 360
SHEET 1 C 8 ILE B 167 PHE B 175 0
SHEET 2 C 8 GLY B 178 LEU B 186 -1 O ILE B 180 N ILE B 173
SHEET 3 C 8 ALA B 223 VAL B 227 -1 O MET B 224 N HIS B 185
SHEET 4 C 8 HIS B 193 SER B 199 1 N VAL B 196 O LEU B 225
SHEET 5 C 8 VAL B 261 PHE B 271 1 O GLY B 267 N VAL B 195
SHEET 6 C 8 ILE B 289 LEU B 295 1 O LYS B 290 N VAL B 266
SHEET 7 C 8 ILE B 358 LEU B 363 1 O LEU B 359 N ILE B 294
SHEET 8 C 8 LYS B 385 ILE B 389 1 O LYS B 385 N ALA B 360
CISPEP 1 TYR A 137 PRO A 138 0 5.52
CISPEP 2 TYR B 137 PRO B 138 0 6.55
SITE 1 AC1 7 GLN A 56 TRP A 59 GLN A 60 MET A 209
SITE 2 AC1 7 LEU A 295 TYR A 398 LEU A 402
SITE 1 AC2 6 GLY A 201 LEU A 202 ARG A 272 PHE A 273
SITE 2 AC2 6 HOH A 652 HOH A 703
SITE 1 AC3 8 TRP B 59 GLN B 60 LEU B 212 ARG B 272
SITE 2 AC3 8 LEU B 295 TYR B 398 LEU B 402 HOH B 626
SITE 1 AC4 2 LYS B 308 MET B 312
SITE 1 AC5 6 GLY B 201 LEU B 202 ARG B 272 PHE B 273
SITE 2 AC5 6 LEU B 320 HOH B 664
CRYST1 42.659 104.542 82.302 90.00 91.18 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 0.023442 0.000000 0.000483 0.00000
SCALE2 0.000000 0.009566 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012153 0.00000
TER 3212 ARG A 415
TER 6407 ARG B 415
MASTER 341 0 5 40 18 0 9 6 6715 2 56 64
END
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