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HEADER HYDROLASE 15-NOV-14 4WY5
TITLE STRUCTURAL ANALYSIS OF TWO FUNGAL ESTERASES FROM RHIZOMUCOR MIEHEI
TITLE 2 EXPLAINING THEIR SUBSTRATE SPECIFICITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOMUCOR MIEHEI;
SOURCE 3 ORGANISM_TAXID: 4839;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS RHIZOMUCOR MIEHEI, ESTERASE, SUBSTRATE SPECIFICITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.QIN,S.YANG,X.DUAN,Q.YAN,Z.JIANG
REVDAT 1 01-JUL-15 4WY5 0
JRNL AUTH Z.QIN,S.YANG,X.DUAN,Q.YAN,Z.JIANG
JRNL TITL STRUCTURAL INSIGHTS INTO THE SUBSTRATE SPECIFICITY OF TWO
JRNL TITL 2 ESTERASES FROM THE THERMOPHILIC RHIZOMUCOR MIEHEI
JRNL REF J.LIPID RES.
JRNL REFN ISSN 0022-2275
REMARK 2
REMARK 2 RESOLUTION. 2.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 26738
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.450
REMARK 3 FREE R VALUE TEST SET COUNT : 1992
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 31.8550 - 5.8007 0.99 1806 144 0.1705 0.1879
REMARK 3 2 5.8007 - 4.6087 0.99 1800 143 0.1557 0.1935
REMARK 3 3 4.6087 - 4.0274 0.99 1793 141 0.1430 0.1896
REMARK 3 4 4.0274 - 3.6597 0.99 1840 147 0.1502 0.2057
REMARK 3 5 3.6597 - 3.3978 0.99 1745 146 0.1800 0.2103
REMARK 3 6 3.3978 - 3.1976 0.99 1812 143 0.1904 0.2532
REMARK 3 7 3.1976 - 3.0376 0.99 1799 151 0.1987 0.2244
REMARK 3 8 3.0376 - 2.9055 0.98 1791 143 0.2049 0.2489
REMARK 3 9 2.9055 - 2.7937 0.98 1759 142 0.1969 0.2880
REMARK 3 10 2.7937 - 2.6973 0.98 1760 143 0.2004 0.2523
REMARK 3 11 2.6973 - 2.6130 0.98 1843 147 0.1979 0.2702
REMARK 3 12 2.6130 - 2.5384 0.98 1769 140 0.2090 0.2943
REMARK 3 13 2.5384 - 2.4716 0.97 1718 140 0.2131 0.3155
REMARK 3 14 2.4716 - 2.4113 0.82 1511 122 0.2513 0.3216
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.560
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 : 0.010 4981
REMARK 3 ANGLE : 1.242 6803
REMARK 3 CHIRALITY : 0.050 806
REMARK 3 PLANARITY : 0.007 872
REMARK 3 DIHEDRAL : 13.816 1781
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: SF FILE CONTAINS FRIEDEL PAIRS UNDER
REMARK 3 I/F_MINUS AND I/F_PLUS COLUMNS.
REMARK 4
REMARK 4 4WY5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000204643.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BSRF
REMARK 200 BEAMLINE : 3W1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26738
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.430
REMARK 200 RESOLUTION RANGE LOW (A) : 31.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.9200
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: AUTOMAR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V)PEG3350; 0.2M (NH4)2SO4; 0.1M
REMARK 280 MES BUFFER PH6.0, PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 MET A 1
REMARK 465 THR A 2
REMARK 465 VAL A 3
REMARK 465 ALA A 324
REMARK 465 LEU A 325
REMARK 465 GLU A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
REMARK 465 HIS A 329
REMARK 465 HIS A 330
REMARK 465 HIS A 331
REMARK 465 HIS A 332
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 VAL B 3
REMARK 465 ALA B 324
REMARK 465 LEU B 325
REMARK 465 GLU B 326
REMARK 465 HIS B 327
REMARK 465 HIS B 328
REMARK 465 HIS B 329
REMARK 465 HIS B 330
REMARK 465 HIS B 331
REMARK 465 HIS B 332
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 20 CG CD CE NZ
REMARK 470 GLU A 21 CG CD OE1 OE2
REMARK 470 ARG A 22 CG CD NE CZ NH1 NH2
REMARK 470 SER A 36 OG
REMARK 470 SER A 37 OG
REMARK 470 ARG A 40 CG CD NE CZ NH1 NH2
REMARK 470 SER B 36 OG
REMARK 470 SER B 37 OG
REMARK 470 ASN B 45 CG OD1 ND2
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 GLU B 249 CG CD OE1 OE2
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 VAL A 32 CB SER A 36 1.01
REMARK 500 C VAL A 32 CB SER A 36 2.10
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 ASN A 5 21.18 -155.58
REMARK 500 THR A 27 51.39 -114.49
REMARK 500 LEU A 30 11.32 -67.80
REMARK 500 ASN A 111 64.17 63.97
REMARK 500 SER A 161 -114.72 52.11
REMARK 500 LEU A 179 53.33 -113.41
REMARK 500 TYR A 190 68.81 36.44
REMARK 500 SER A 261 79.87 -105.92
REMARK 500 ASN B 5 23.18 -142.66
REMARK 500 LYS B 31 32.56 -86.97
REMARK 500 SER B 36 73.52 -67.84
REMARK 500 ASN B 111 63.96 63.12
REMARK 500 SER B 161 -114.68 51.76
REMARK 500 LEU B 179 51.84 -112.04
REMARK 500 TYR B 190 68.70 36.76
REMARK 500 SER B 261 79.72 -106.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 35 SER A 36 -144.82
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WY8 RELATED DB: PDB
DBREF 4WY5 A 1 324 UNP V5J5W4 V5J5W4_RHIMI 1 324
DBREF 4WY5 B 1 324 UNP V5J5W4 V5J5W4_RHIMI 1 324
SEQADV 4WY5 LEU A 325 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 GLU A 326 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS A 327 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS A 328 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS A 329 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS A 330 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS A 331 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS A 332 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 LEU B 325 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 GLU B 326 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS B 327 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS B 328 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS B 329 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS B 330 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS B 331 UNP V5J5W4 EXPRESSION TAG
SEQADV 4WY5 HIS B 332 UNP V5J5W4 EXPRESSION TAG
SEQRES 1 A 332 MET THR VAL GLY ASN PRO PRO ILE HIS PRO VAL TYR ALA
SEQRES 2 A 332 ALA ALA PHE ALA ALA MET LYS GLU ARG PRO PRO ILE HIS
SEQRES 3 A 332 THR LEU ASP LEU LYS VAL VAL ARG GLU SER SER GLU ALA
SEQRES 4 A 332 ARG GLN LEU ALA ALA ASN ILE LYS LEU PRO GLU VAL ILE
SEQRES 5 A 332 GLU GLU ASP LYS VAL VAL GLU SER ASP GLY LYS THR LEU
SEQRES 6 A 332 LYS LEU THR ILE VAL ARG PRO PRO GLY THR GLU ASP GLN
SEQRES 7 A 332 ILE LEU PRO VAL LEU ILE PHE LEU HIS GLY GLY GLY PHE
SEQRES 8 A 332 VAL PHE GLY SER LYS TYR THR HIS ILE LYS PRO VAL ARG
SEQRES 9 A 332 ASP LEU THR VAL LYS ALA ASN VAL VAL THR VAL PHE VAL
SEQRES 10 A 332 ASP TYR SER LEU SER PRO GLU ALA LYS PHE PRO THR ALA
SEQRES 11 A 332 ILE GLU GLU ILE TYR ALA ALA ILE LEU TRP VAL ARG GLU
SEQRES 12 A 332 ASN ALA SER SER LEU ASN ILE ASN ALA GLU ALA LEU ALA
SEQRES 13 A 332 VAL ALA GLY ASP SER ALA GLY ALA THR LEU SER ALA ALA
SEQRES 14 A 332 VAL SER ILE TYR ALA LYS GLU LYS GLY LEU SER ALA ALA
SEQRES 15 A 332 ILE LYS THR GLN VAL LEU ILE TYR PRO ALA THR ALA VAL
SEQRES 16 A 332 SER HIS ALA LYS TYR GLU SER TYR LYS LEU PHE GLY ASN
SEQRES 17 A 332 GLY ASP TYR ILE LEU SER ALA GLU ASP LEU LYS PHE PHE
SEQRES 18 A 332 SER ASN ALA TYR LEU PRO ALA PRO ALA SER GLU LEU ASN
SEQRES 19 A 332 ASP LYS LEU ALA THR LEU GLU LEU ALA THR LYS ALA ASP
SEQRES 20 A 332 LEU GLU GLY LEU PRO PRO ALA LEU LEU PHE THR ALA GLU
SEQRES 21 A 332 SER ASP VAL LEU ARG ASP GLU GLY GLU LYS TYR ALA GLN
SEQRES 22 A 332 GLN LEU ALA GLU ALA GLY VAL ASP VAL ALA ALA VAL ARG
SEQRES 23 A 332 VAL LEU GLY ALA VAL HIS GLY PHE ILE THR VAL PRO VAL
SEQRES 24 A 332 GLU THR PRO GLN TYR ARG PHE THR ILE ASN THR ILE VAL
SEQRES 25 A 332 ALA HIS LEU ARG ASP ILE TYR ALA LYS TYR ASN ALA LEU
SEQRES 26 A 332 GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 332 MET THR VAL GLY ASN PRO PRO ILE HIS PRO VAL TYR ALA
SEQRES 2 B 332 ALA ALA PHE ALA ALA MET LYS GLU ARG PRO PRO ILE HIS
SEQRES 3 B 332 THR LEU ASP LEU LYS VAL VAL ARG GLU SER SER GLU ALA
SEQRES 4 B 332 ARG GLN LEU ALA ALA ASN ILE LYS LEU PRO GLU VAL ILE
SEQRES 5 B 332 GLU GLU ASP LYS VAL VAL GLU SER ASP GLY LYS THR LEU
SEQRES 6 B 332 LYS LEU THR ILE VAL ARG PRO PRO GLY THR GLU ASP GLN
SEQRES 7 B 332 ILE LEU PRO VAL LEU ILE PHE LEU HIS GLY GLY GLY PHE
SEQRES 8 B 332 VAL PHE GLY SER LYS TYR THR HIS ILE LYS PRO VAL ARG
SEQRES 9 B 332 ASP LEU THR VAL LYS ALA ASN VAL VAL THR VAL PHE VAL
SEQRES 10 B 332 ASP TYR SER LEU SER PRO GLU ALA LYS PHE PRO THR ALA
SEQRES 11 B 332 ILE GLU GLU ILE TYR ALA ALA ILE LEU TRP VAL ARG GLU
SEQRES 12 B 332 ASN ALA SER SER LEU ASN ILE ASN ALA GLU ALA LEU ALA
SEQRES 13 B 332 VAL ALA GLY ASP SER ALA GLY ALA THR LEU SER ALA ALA
SEQRES 14 B 332 VAL SER ILE TYR ALA LYS GLU LYS GLY LEU SER ALA ALA
SEQRES 15 B 332 ILE LYS THR GLN VAL LEU ILE TYR PRO ALA THR ALA VAL
SEQRES 16 B 332 SER HIS ALA LYS TYR GLU SER TYR LYS LEU PHE GLY ASN
SEQRES 17 B 332 GLY ASP TYR ILE LEU SER ALA GLU ASP LEU LYS PHE PHE
SEQRES 18 B 332 SER ASN ALA TYR LEU PRO ALA PRO ALA SER GLU LEU ASN
SEQRES 19 B 332 ASP LYS LEU ALA THR LEU GLU LEU ALA THR LYS ALA ASP
SEQRES 20 B 332 LEU GLU GLY LEU PRO PRO ALA LEU LEU PHE THR ALA GLU
SEQRES 21 B 332 SER ASP VAL LEU ARG ASP GLU GLY GLU LYS TYR ALA GLN
SEQRES 22 B 332 GLN LEU ALA GLU ALA GLY VAL ASP VAL ALA ALA VAL ARG
SEQRES 23 B 332 VAL LEU GLY ALA VAL HIS GLY PHE ILE THR VAL PRO VAL
SEQRES 24 B 332 GLU THR PRO GLN TYR ARG PHE THR ILE ASN THR ILE VAL
SEQRES 25 B 332 ALA HIS LEU ARG ASP ILE TYR ALA LYS TYR ASN ALA LEU
SEQRES 26 B 332 GLU HIS HIS HIS HIS HIS HIS
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 B 401 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 6 HOH *269(H2 O)
HELIX 1 AA1 HIS A 9 LYS A 20 1 12
HELIX 2 AA2 PRO A 24 LEU A 28 5 5
HELIX 3 AA3 ASP A 29 VAL A 33 5 5
HELIX 4 AA4 GLU A 38 ALA A 43 1 6
HELIX 5 AA5 HIS A 99 ASN A 111 1 13
HELIX 6 AA6 PRO A 128 ASN A 144 1 17
HELIX 7 AA7 ASN A 144 ASN A 149 1 6
HELIX 8 AA8 SER A 161 LYS A 177 1 17
HELIX 9 AA9 SER A 196 LYS A 199 5 4
HELIX 10 AB1 TYR A 200 GLY A 207 1 8
HELIX 11 AB2 SER A 214 LEU A 226 1 13
HELIX 12 AB3 PRO A 229 ASN A 234 1 6
HELIX 13 AB4 THR A 239 ALA A 243 5 5
HELIX 14 AB5 THR A 244 GLU A 249 1 6
HELIX 15 AB6 LEU A 264 ALA A 278 1 15
HELIX 16 AB7 GLY A 293 VAL A 297 5 5
HELIX 17 AB8 THR A 301 ALA A 320 1 20
HELIX 18 AB9 LYS A 321 ASN A 323 5 3
HELIX 19 AC1 HIS B 9 GLU B 21 1 13
HELIX 20 AC2 GLU B 38 ALA B 43 1 6
HELIX 21 AC3 HIS B 99 ASN B 111 1 13
HELIX 22 AC4 PRO B 128 ASN B 144 1 17
HELIX 23 AC5 ASN B 144 ASN B 149 1 6
HELIX 24 AC6 SER B 161 LYS B 177 1 17
HELIX 25 AC7 SER B 196 LYS B 199 5 4
HELIX 26 AC8 TYR B 200 GLY B 207 1 8
HELIX 27 AC9 SER B 214 LEU B 226 1 13
HELIX 28 AD1 PRO B 229 ASN B 234 1 6
HELIX 29 AD2 THR B 239 ALA B 243 5 5
HELIX 30 AD3 THR B 244 GLU B 249 1 6
HELIX 31 AD4 LEU B 264 ALA B 278 1 15
HELIX 32 AD5 GLY B 293 VAL B 297 5 5
HELIX 33 AD6 THR B 301 LYS B 321 1 21
SHEET 1 AA116 ILE A 52 SER A 60 0
SHEET 2 AA116 LYS A 63 ARG A 71 -1 O ILE A 69 N GLU A 54
SHEET 3 AA116 VAL A 113 VAL A 117 -1 O PHE A 116 N THR A 68
SHEET 4 AA116 LEU A 80 LEU A 86 1 N LEU A 83 O VAL A 113
SHEET 5 AA116 ILE A 150 ASP A 160 1 O ALA A 156 N ILE A 84
SHEET 6 AA116 THR A 185 ILE A 189 1 O VAL A 187 N VAL A 157
SHEET 7 AA116 ALA A 254 SER A 261 1 O LEU A 255 N LEU A 188
SHEET 8 AA116 VAL A 282 VAL A 291 1 O VAL A 287 N THR A 258
SHEET 9 AA116 VAL B 282 VAL B 291 -1 O ALA B 284 N LEU A 288
SHEET 10 AA116 ALA B 254 SER B 261 1 N THR B 258 O VAL B 287
SHEET 11 AA116 GLN B 186 ILE B 189 1 N LEU B 188 O LEU B 255
SHEET 12 AA116 ILE B 150 ASP B 160 1 N VAL B 157 O VAL B 187
SHEET 13 AA116 LEU B 80 LEU B 86 1 N ILE B 84 O ALA B 156
SHEET 14 AA116 VAL B 113 VAL B 117 1 O VAL B 113 N LEU B 83
SHEET 15 AA116 LYS B 63 ARG B 71 -1 N THR B 68 O PHE B 116
SHEET 16 AA116 ILE B 52 SER B 60 -1 N GLU B 54 O ILE B 69
CISPEP 1 SER A 122 PRO A 123 0 7.90
CISPEP 2 PHE A 127 PRO A 128 0 4.28
CISPEP 3 SER B 122 PRO B 123 0 8.22
CISPEP 4 PHE B 127 PRO B 128 0 4.78
SITE 1 AC1 7 ARG A 265 ARG A 286 HOH A 590 HOH A 634
SITE 2 AC1 7 HOH A 646 ARG B 265 ARG B 286
SITE 1 AC2 1 ARG A 104
SITE 1 AC3 1 ARG B 104
CRYST1 56.691 64.528 64.792 106.81 116.37 103.64 P 1 2
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 0.017639 0.004280 0.011977 0.00000
SCALE2 0.000000 0.015947 0.008092 0.00000
SCALE3 0.000000 0.000000 0.019317 0.00000
TER 2426 ASN A 323
TER 4861 ASN B 323
MASTER 315 0 3 33 16 0 4 6 5143 2 15 52
END |