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HEADER HYDROLASE 05-MAY-17 5XK2
TITLE CRYSTAL STRUCTURE OF MONO- AND DIACYLGLYCEROL LIPASE FROM ASPERGILLUS
TITLE 2 ORYZAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MONO-/DI-ACYLGLYCEROL LIPASE,N-TERMINAL;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;
SOURCE 3 ORGANISM_COMMON: YELLOW KOJI MOLD;
SOURCE 4 ORGANISM_TAXID: 5062;
SOURCE 5 GENE: MDLB, OAORY_01019780;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI-PICHIA PASTORIS SHUTTLE VECTOR
SOURCE 7 PPPARG4;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 1182032
KEYWDS CLOSED CONFORMATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.H.WANG,D.M.LAN
REVDAT 1 09-MAY-18 5XK2 0
JRNL AUTH Y.H.WANG,D.M.LAN
JRNL TITL CRYSTAL STRUCTURE OF MONO- AND DIACYLGLYCEROL LIPASE FROM
JRNL TITL 2 ASPERGILLUS ORYZAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX PHENIX.REFINE: 1.9_1692
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.420
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 61231
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890
REMARK 3 FREE R VALUE TEST SET COUNT : 2996
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 33.9799 - 4.6732 1.00 2895 160 0.1429 0.1488
REMARK 3 2 4.6732 - 3.7107 1.00 2851 136 0.1204 0.1470
REMARK 3 3 3.7107 - 3.2421 1.00 2833 158 0.1370 0.1455
REMARK 3 4 3.2421 - 2.9459 1.00 2792 140 0.1454 0.1794
REMARK 3 5 2.9459 - 2.7348 1.00 2846 148 0.1509 0.1675
REMARK 3 6 2.7348 - 2.5736 1.00 2818 130 0.1457 0.1834
REMARK 3 7 2.5736 - 2.4448 1.00 2845 127 0.1459 0.1960
REMARK 3 8 2.4448 - 2.3384 1.00 2785 161 0.1463 0.1766
REMARK 3 9 2.3384 - 2.2484 1.00 2814 137 0.1383 0.1787
REMARK 3 10 2.2484 - 2.1708 1.00 2815 146 0.1366 0.1609
REMARK 3 11 2.1708 - 2.1029 1.00 2776 155 0.1417 0.1737
REMARK 3 12 2.1029 - 2.0428 1.00 2809 151 0.1430 0.1825
REMARK 3 13 2.0428 - 1.9891 1.00 2804 145 0.1436 0.1820
REMARK 3 14 1.9891 - 1.9405 1.00 2801 170 0.1389 0.1779
REMARK 3 15 1.9405 - 1.8964 1.00 2768 147 0.1427 0.1531
REMARK 3 16 1.8964 - 1.8561 1.00 2826 146 0.1485 0.1849
REMARK 3 17 1.8561 - 1.8189 1.00 2750 162 0.1485 0.1804
REMARK 3 18 1.8189 - 1.7846 1.00 2847 134 0.1415 0.1803
REMARK 3 19 1.7846 - 1.7528 0.98 2737 116 0.1494 0.2176
REMARK 3 20 1.7528 - 1.7230 0.94 2656 122 0.1505 0.1773
REMARK 3 21 1.7230 - 1.6953 0.77 2167 105 0.1537 0.2115
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.50
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 4300
REMARK 3 ANGLE : 1.236 5875
REMARK 3 CHIRALITY : 0.059 662
REMARK 3 PLANARITY : 0.008 759
REMARK 3 DIHEDRAL : 12.374 1488
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8899 22.2701 103.6045
REMARK 3 T TENSOR
REMARK 3 T11: 0.0567 T22: 0.0624
REMARK 3 T33: 0.0582 T12: -0.0100
REMARK 3 T13: 0.0007 T23: -0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 0.0956 L22: 0.2687
REMARK 3 L33: 0.0831 L12: -0.0380
REMARK 3 L13: 0.0033 L23: -0.1307
REMARK 3 S TENSOR
REMARK 3 S11: 0.0147 S12: -0.0155 S13: 0.0493
REMARK 3 S21: 0.0444 S22: -0.0042 S23: 0.0102
REMARK 3 S31: -0.0214 S32: 0.0154 S33: 0.0046
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 5XK2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1300003594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978530
REMARK 200 MONOCHROMATOR : MD2
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61241
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.695
REMARK 200 RESOLUTION RANGE LOW (A) : 33.973
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.496
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 24.1600
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) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.13
REMARK 200 R MERGE FOR SHELL (I) : 0.11700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 9.350
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 45.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.5, 45%
REMARK 280 POLYPROPYLENE GLYCOL P 400, VAPOR DIFFUSION SITTING DROP,
REMARK 280 TEMPERATURE 293K, VAPOR DIFFUSION, SITTING DROP
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 33.63850
REMARK 290 SMTRY3 2 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: 2220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 31.06122
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 33.63850
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 178.40786
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 TYR A 1
REMARK 465 PRO A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 ILE A 5
REMARK 465 ASP A 6
REMARK 465 VAL A 7
REMARK 465 ARG A 8
REMARK 465 ASP A 9
REMARK 465 PRO A 281
REMARK 465 GLY A 282
REMARK 465 LEU A 283
REMARK 465 PRO A 284
REMARK 465 LEU A 285
REMARK 465 ARG A 286
REMARK 465 TYR B 1
REMARK 465 PRO B 2
REMARK 465 THR B 3
REMARK 465 ALA B 4
REMARK 465 ILE B 5
REMARK 465 ASP B 6
REMARK 465 VAL B 7
REMARK 465 ARG B 8
REMARK 465 ASP B 9
REMARK 465 ILE B 10
REMARK 465 GLY B 280
REMARK 465 PRO B 281
REMARK 465 GLY B 282
REMARK 465 LEU B 283
REMARK 465 PRO B 284
REMARK 465 LEU B 285
REMARK 465 ARG B 286
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 O HOH A 392 O HOH A 550 1.84
REMARK 500 O HOH A 536 O HOH A 540 1.96
REMARK 500 NZ LYS B 37 O HOH B 301 2.04
REMARK 500 O HOH B 416 O HOH B 481 2.07
REMARK 500 O HOH A 302 O HOH A 551 2.18
REMARK 500 O HOH A 548 O HOH A 623 2.18
REMARK 500 O HOH A 365 O HOH A 509 2.18
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 THR A 67 -63.01 -94.82
REMARK 500 SER A 153 -135.60 60.81
REMARK 500 ASN A 170 1.96 82.94
REMARK 500 ASN A 204 -126.89 44.64
REMARK 500 PHE A 272 -37.75 60.93
REMARK 500 ILE B 68 -63.77 -120.25
REMARK 500 SER B 153 -135.06 62.35
REMARK 500 ASN B 204 -124.64 45.96
REMARK 500 PHE B 272 -33.83 63.04
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 624 DISTANCE = 6.43 ANGSTROMS
DBREF 5XK2 A 1 286 UNP P78583 P78583_ASPOZ 21 306
DBREF 5XK2 B 1 286 UNP P78583 P78583_ASPOZ 21 306
SEQRES 1 A 286 TYR PRO THR ALA ILE ASP VAL ARG ASP ILE PRO THR THR
SEQRES 2 A 286 GLN LEU GLU ASP PHE LYS PHE TRP VAL GLN TYR ALA ALA
SEQRES 3 A 286 ALA THR TYR CYS PRO ASN ASN TYR VAL ALA LYS ASP GLY
SEQRES 4 A 286 GLU LYS LEU ASN CYS SER VAL GLY ASN CYS PRO ASP VAL
SEQRES 5 A 286 GLU ALA ALA GLY SER THR VAL LYS LEU SER PHE SER ASP
SEQRES 6 A 286 ASP THR ILE THR ASP THR ALA GLY PHE VAL ALA VAL ASP
SEQRES 7 A 286 ASN THR ASN LYS ALA ILE VAL VAL ALA PHE ARG GLY SER
SEQRES 8 A 286 TYR SER ILE ARG ASN TRP VAL THR ASP ALA THR PHE PRO
SEQRES 9 A 286 GLN THR ASP PRO GLY LEU CYS ASP GLY CYS LYS ALA GLU
SEQRES 10 A 286 LEU GLY PHE TRP THR ALA TRP LYS VAL VAL ARG ASP ARG
SEQRES 11 A 286 ILE ILE LYS THR LEU ASP GLU LEU LYS PRO GLU HIS SER
SEQRES 12 A 286 ASP TYR LYS ILE VAL VAL VAL GLY HIS SER LEU GLY ALA
SEQRES 13 A 286 ALA ILE ALA SER LEU ALA ALA ALA ASP LEU ARG THR LYS
SEQRES 14 A 286 ASN TYR ASP ALA ILE LEU TYR ALA TYR ALA ALA PRO ARG
SEQRES 15 A 286 VAL ALA ASN LYS PRO LEU ALA GLU PHE ILE THR ASN GLN
SEQRES 16 A 286 GLY ASN ASN TYR ARG PHE THR HIS ASN ASP ASP PRO VAL
SEQRES 17 A 286 PRO LYS LEU PRO LEU LEU THR MET GLY TYR VAL HIS ILE
SEQRES 18 A 286 SER PRO GLU TYR TYR ILE THR ALA PRO ASP ASN THR THR
SEQRES 19 A 286 VAL THR ASP ASN GLN VAL THR VAL LEU ASP GLY TYR VAL
SEQRES 20 A 286 ASN PHE LYS GLY ASN THR GLY THR SER GLY GLY LEU PRO
SEQRES 21 A 286 ASP LEU LEU ALA PHE HIS SER HIS VAL TRP TYR PHE ILE
SEQRES 22 A 286 HIS ALA ASP ALA CYS LYS GLY PRO GLY LEU PRO LEU ARG
SEQRES 1 B 286 TYR PRO THR ALA ILE ASP VAL ARG ASP ILE PRO THR THR
SEQRES 2 B 286 GLN LEU GLU ASP PHE LYS PHE TRP VAL GLN TYR ALA ALA
SEQRES 3 B 286 ALA THR TYR CYS PRO ASN ASN TYR VAL ALA LYS ASP GLY
SEQRES 4 B 286 GLU LYS LEU ASN CYS SER VAL GLY ASN CYS PRO ASP VAL
SEQRES 5 B 286 GLU ALA ALA GLY SER THR VAL LYS LEU SER PHE SER ASP
SEQRES 6 B 286 ASP THR ILE THR ASP THR ALA GLY PHE VAL ALA VAL ASP
SEQRES 7 B 286 ASN THR ASN LYS ALA ILE VAL VAL ALA PHE ARG GLY SER
SEQRES 8 B 286 TYR SER ILE ARG ASN TRP VAL THR ASP ALA THR PHE PRO
SEQRES 9 B 286 GLN THR ASP PRO GLY LEU CYS ASP GLY CYS LYS ALA GLU
SEQRES 10 B 286 LEU GLY PHE TRP THR ALA TRP LYS VAL VAL ARG ASP ARG
SEQRES 11 B 286 ILE ILE LYS THR LEU ASP GLU LEU LYS PRO GLU HIS SER
SEQRES 12 B 286 ASP TYR LYS ILE VAL VAL VAL GLY HIS SER LEU GLY ALA
SEQRES 13 B 286 ALA ILE ALA SER LEU ALA ALA ALA ASP LEU ARG THR LYS
SEQRES 14 B 286 ASN TYR ASP ALA ILE LEU TYR ALA TYR ALA ALA PRO ARG
SEQRES 15 B 286 VAL ALA ASN LYS PRO LEU ALA GLU PHE ILE THR ASN GLN
SEQRES 16 B 286 GLY ASN ASN TYR ARG PHE THR HIS ASN ASP ASP PRO VAL
SEQRES 17 B 286 PRO LYS LEU PRO LEU LEU THR MET GLY TYR VAL HIS ILE
SEQRES 18 B 286 SER PRO GLU TYR TYR ILE THR ALA PRO ASP ASN THR THR
SEQRES 19 B 286 VAL THR ASP ASN GLN VAL THR VAL LEU ASP GLY TYR VAL
SEQRES 20 B 286 ASN PHE LYS GLY ASN THR GLY THR SER GLY GLY LEU PRO
SEQRES 21 B 286 ASP LEU LEU ALA PHE HIS SER HIS VAL TRP TYR PHE ILE
SEQRES 22 B 286 HIS ALA ASP ALA CYS LYS GLY PRO GLY LEU PRO LEU ARG
FORMUL 3 HOH *544(H2 O)
HELIX 1 AA1 THR A 13 THR A 28 1 16
HELIX 2 AA2 CYS A 30 VAL A 35 1 6
HELIX 3 AA3 CYS A 49 GLY A 56 1 8
HELIX 4 AA4 SER A 93 THR A 99 1 7
HELIX 5 AA5 LEU A 118 LYS A 139 1 22
HELIX 6 AA6 PRO A 140 SER A 143 5 4
HELIX 7 AA7 SER A 153 LYS A 169 1 17
HELIX 8 AA8 ASN A 185 GLY A 196 1 12
HELIX 9 AA9 PRO A 207 LEU A 211 5 5
HELIX 10 AB1 LEU A 213 GLY A 217 5 5
HELIX 11 AB2 THR A 236 ASN A 238 5 3
HELIX 12 AB3 GLY A 251 LEU A 259 5 9
HELIX 13 AB4 ASP A 261 TRP A 270 5 10
HELIX 14 AB5 THR B 13 THR B 28 1 16
HELIX 15 AB6 CYS B 30 VAL B 35 1 6
HELIX 16 AB7 CYS B 49 GLY B 56 1 8
HELIX 17 AB8 SER B 93 THR B 99 1 7
HELIX 18 AB9 LEU B 118 SER B 143 1 26
HELIX 19 AC1 SER B 153 LYS B 169 1 17
HELIX 20 AC2 ASN B 185 GLY B 196 1 12
HELIX 21 AC3 PRO B 207 LEU B 211 5 5
HELIX 22 AC4 LEU B 213 GLY B 217 5 5
HELIX 23 AC5 THR B 236 ASN B 238 5 3
HELIX 24 AC6 GLY B 251 LEU B 259 5 9
HELIX 25 AC7 ASP B 261 TRP B 270 5 10
SHEET 1 AA1 8 THR A 58 ASP A 65 0
SHEET 2 AA1 8 THR A 71 ASP A 78 -1 O THR A 71 N ASP A 65
SHEET 3 AA1 8 ALA A 83 ARG A 89 -1 O ARG A 89 N ALA A 72
SHEET 4 AA1 8 LYS A 146 HIS A 152 1 O VAL A 148 N VAL A 86
SHEET 5 AA1 8 ALA A 173 TYR A 178 1 O ILE A 174 N VAL A 149
SHEET 6 AA1 8 ASN A 198 HIS A 203 1 O TYR A 199 N ALA A 177
SHEET 7 AA1 8 GLU A 224 ILE A 227 1 O ILE A 227 N THR A 202
SHEET 8 AA1 8 VAL A 240 LEU A 243 -1 O THR A 241 N TYR A 226
SHEET 1 AA2 2 GLN A 105 THR A 106 0
SHEET 2 AA2 2 ALA A 116 GLU A 117 -1 O ALA A 116 N THR A 106
SHEET 1 AA3 8 THR B 58 SER B 64 0
SHEET 2 AA3 8 ALA B 72 ASP B 78 -1 O VAL B 75 N LYS B 60
SHEET 3 AA3 8 ALA B 83 ARG B 89 -1 O ARG B 89 N ALA B 72
SHEET 4 AA3 8 LYS B 146 HIS B 152 1 O VAL B 148 N VAL B 86
SHEET 5 AA3 8 ALA B 173 TYR B 178 1 O ILE B 174 N VAL B 149
SHEET 6 AA3 8 ASN B 198 HIS B 203 1 O PHE B 201 N ALA B 177
SHEET 7 AA3 8 GLU B 224 ILE B 227 1 O ILE B 227 N THR B 202
SHEET 8 AA3 8 VAL B 240 LEU B 243 -1 O THR B 241 N TYR B 226
SHEET 1 AA4 2 GLN B 105 THR B 106 0
SHEET 2 AA4 2 ALA B 116 GLU B 117 -1 O ALA B 116 N THR B 106
SSBOND 1 CYS A 30 CYS A 278 1555 1555 2.07
SSBOND 2 CYS A 44 CYS A 49 1555 1555 2.05
SSBOND 3 CYS A 111 CYS A 114 1555 1555 2.02
SSBOND 4 CYS B 30 CYS B 278 1555 1555 2.06
SSBOND 5 CYS B 44 CYS B 49 1555 1555 2.06
SSBOND 6 CYS B 111 CYS B 114 1555 1555 2.03
CISPEP 1 LEU A 211 PRO A 212 0 -10.57
CISPEP 2 SER A 222 PRO A 223 0 0.15
CISPEP 3 LEU B 211 PRO B 212 0 -8.36
CISPEP 4 SER B 222 PRO B 223 0 -1.88
CRYST1 47.329 67.277 89.574 90.00 95.21 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 0.021129 0.000000 0.001927 0.00000
SCALE2 0.000000 0.014864 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011210 0.00000
TER 2098 GLY A 280
TER 4184 LYS B 279
MASTER 318 0 0 25 20 0 0 6 4726 2 12 44
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