| content |
HEADER HYDROLASE 16-NOV-14 4WY8
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, C, D;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOMUCOR MIEHEI CAU432;
SOURCE 3 ORGANISM_TAXID: 1031333;
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 4WY8 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. 2.27 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) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 55905
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2792
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 46.6544 - 6.1572 0.94 2785 139 0.1729 0.1726
REMARK 3 2 6.1572 - 4.8889 0.97 2791 148 0.1825 0.1919
REMARK 3 3 4.8889 - 4.2714 0.96 2744 156 0.1583 0.2170
REMARK 3 4 4.2714 - 3.8811 0.97 2763 142 0.1665 0.2069
REMARK 3 5 3.8811 - 3.6030 0.98 2760 146 0.1782 0.2333
REMARK 3 6 3.6030 - 3.3906 0.99 2790 168 0.1853 0.2640
REMARK 3 7 3.3906 - 3.2209 0.99 2773 151 0.1861 0.2222
REMARK 3 8 3.2209 - 3.0807 1.00 2812 133 0.1965 0.2081
REMARK 3 9 3.0807 - 2.9621 1.00 2778 160 0.1988 0.2566
REMARK 3 10 2.9621 - 2.8599 1.00 2799 150 0.2029 0.3054
REMARK 3 11 2.8599 - 2.7705 1.00 2803 139 0.2036 0.2439
REMARK 3 12 2.7705 - 2.6913 1.00 2821 137 0.2182 0.2750
REMARK 3 13 2.6913 - 2.6205 1.00 2741 143 0.2060 0.2458
REMARK 3 14 2.6205 - 2.5565 1.00 2851 132 0.2132 0.2899
REMARK 3 15 2.5565 - 2.4984 0.98 2705 142 0.2081 0.2671
REMARK 3 16 2.4984 - 2.4453 0.94 2652 143 0.2086 0.2671
REMARK 3 17 2.4453 - 2.3964 0.89 2458 135 0.2080 0.2638
REMARK 3 18 2.3964 - 2.3511 0.84 2316 111 0.2054 0.2828
REMARK 3 19 2.3511 - 2.3091 0.76 2134 106 0.1982 0.2676
REMARK 3 20 2.3091 - 2.2700 0.68 1837 111 0.2124 0.2841
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.260
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 : 0.009 10409
REMARK 3 ANGLE : 1.212 14180
REMARK 3 CHIRALITY : 0.049 1648
REMARK 3 PLANARITY : 0.007 1808
REMARK 3 DIHEDRAL : 12.951 3817
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 4WY8 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_1000204752.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
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 : 55910
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
REMARK 200 RESOLUTION RANGE LOW (A) : 46.650
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.0800
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: PHENIX
REMARK 200 STARTING MODEL: 1JJI
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 (%): 43.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG4000; 10% (V/V) 2
REMARK 280 -PROPANOL; 100MM HEPES BUFFER (PH7.5), PH 7.9, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
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 75.56250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.83750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 75.56250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.83750
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 ALA A 2
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 327
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 HIS C 326
REMARK 465 HIS C 327
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 HIS D 325
REMARK 465 HIS D 326
REMARK 465 HIS D 327
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 HIS B 322 CG ND1 CD2 CE1 NE2
REMARK 470 HIS C 322 CG ND1 CD2 CE1 NE2
REMARK 470 HIS C 324 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 6 CG CD CE NZ
REMARK 470 ILE D 20 CG1 CG2 CD1
REMARK 470 GLN D 24 CG CD OE1 NE2
REMARK 470 GLU D 28 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 OE1 GLU A 28 O HOH A 560 2.00
REMARK 500 O HOH D 420 O HOH D 463 2.06
REMARK 500 OE2 GLU A 133 O HOH A 557 2.11
REMARK 500 O ILE D 58 OG SER D 64 2.15
REMARK 500 NZ LYS C 316 O HOH C 443 2.17
REMARK 500 O HOH B 487 O HOH B 535 2.17
REMARK 500 OH TYR D 204 O HOH D 418 2.18
REMARK 500 OE1 GLN A 179 O HOH A 545 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 322 NE2 HIS A 322 CD2 -0.068
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 VAL A 94 -168.99 -125.90
REMARK 500 SER A 164 -118.76 62.03
REMARK 500 TYR A 192 70.20 22.32
REMARK 500 TYR A 212 -64.04 71.02
REMARK 500 ARG A 252 128.40 -38.77
REMARK 500 ALA A 260 76.36 -101.63
REMARK 500 HIS A 326 173.27 -54.06
REMARK 500 VAL B 94 -165.90 -126.17
REMARK 500 SER B 164 -115.54 60.83
REMARK 500 TYR B 192 70.92 20.72
REMARK 500 TYR B 212 -64.37 71.70
REMARK 500 ARG B 252 128.11 -38.85
REMARK 500 ALA B 260 74.88 -101.55
REMARK 500 ALA C 17 126.74 72.85
REMARK 500 VAL C 94 -167.09 -124.91
REMARK 500 SER C 164 -115.50 61.95
REMARK 500 ASN C 183 51.70 -117.24
REMARK 500 TYR C 192 70.84 21.99
REMARK 500 TYR C 211 52.72 -117.01
REMARK 500 TYR C 212 -72.20 59.29
REMARK 500 VAL C 249 54.23 38.20
REMARK 500 ARG C 252 128.37 -38.95
REMARK 500 HIS C 322 30.50 -88.44
REMARK 500 THR D 19 -36.23 -131.11
REMARK 500 VAL D 94 -168.86 -124.74
REMARK 500 SER D 164 -111.87 62.25
REMARK 500 TYR D 192 62.81 28.07
REMARK 500 VAL D 249 50.99 36.83
REMARK 500 ARG D 252 126.35 -38.88
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 HIS A 325 HIS A 326 110.78
REMARK 500 GLY D 63 SER D 64 -143.45
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 567 DISTANCE = 6.36 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN DOES NOT CURRENTLY
REMARK 999 EXIST.
DBREF 4WY8 A 1 327 PDB 4WY8 4WY8 1 327
DBREF 4WY8 B 1 327 PDB 4WY8 4WY8 1 327
DBREF 4WY8 C 1 327 PDB 4WY8 4WY8 1 327
DBREF 4WY8 D 1 327 PDB 4WY8 4WY8 1 327
SEQRES 1 A 327 MET ALA PRO THR VAL LYS LEU LYS PRO TYR CYS GLN ASN
SEQRES 2 A 327 ILE ALA ASP ALA ALA THR ILE ASP SER THR GLN TYR PRO
SEQRES 3 A 327 PRO GLU VAL VAL ARG LYS ALA GLU ALA ALA SER ILE ILE
SEQRES 4 A 327 ASP ASP PRO LYS ALA LEU GLU GLY LEU PRO ASP VAL TYR
SEQRES 5 A 327 LEU GLU GLU LYS THR ILE ASN ARG LYS ASN GLY SER LYS
SEQRES 6 A 327 ILE GLU LEU THR ILE THR ARG PRO LEU ASP THR GLU ASN
SEQRES 7 A 327 GLN VAL LEU PRO PRO ILE VAL PHE PHE HIS GLY GLY GLY
SEQRES 8 A 327 TRP VAL VAL GLY SER LYS LEU THR HIS ARG ARG THR VAL
SEQRES 9 A 327 TYR GLU LEU THR VAL ARG ALA ARG ALA ALA VAL ILE PHE
SEQRES 10 A 327 VAL ASN TYR SER LEU SER PRO GLU VAL ARG PHE PRO THR
SEQRES 11 A 327 ALA LEU GLU GLU CYS LEU ASP ALA VAL VAL TRP VAL ALA
SEQRES 12 A 327 LYS GLU GLU ASN ALA LYS SER ILE ASN VAL ASP PRO THR
SEQRES 13 A 327 LYS LEU VAL VAL ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 14 A 327 SER ALA VAL VAL CYS ILE ARG ALA LYS GLN LEU GLY LEU
SEQRES 15 A 327 ASN ILE ILE LYS GLY GLN VAL LEU ILE TYR PRO VAL THR
SEQRES 16 A 327 ASP ASP ASN PHE GLU THR ASP SER TYR LYS GLN PHE ALA
SEQRES 17 A 327 GLU ASN TYR TYR LEU THR ARG LYS LEU MET VAL TRP PHE
SEQRES 18 A 327 PHE ASP HIS TYR ILE PRO ASP LYS LYS ASP ARG GLN SER
SEQRES 19 A 327 ILE PHE ALA CYS PRO LEU LYS ALA SER ILE ASP ASP LEU
SEQRES 20 A 327 ARG VAL LEU PRO ARG ALA LEU VAL ILE THR ALA GLU ALA
SEQRES 21 A 327 ASP VAL LEU ARG GLU GLU GLY GLU ALA TYR ALA ARG LYS
SEQRES 22 A 327 LEU ILE GLU ALA GLY ASN ASP VAL THR ALA VAL ARG TYR
SEQRES 23 A 327 LEU GLY ILE ILE HIS GLY ILE PHE ASN LEU ALA THR LEU
SEQRES 24 A 327 SER PRO THR GLY SER GLU ILE LEU ASP HIS ILE VAL ALA
SEQRES 25 A 327 TRP LEU GLN LYS THR TRP LYS LEU GLU HIS HIS HIS HIS
SEQRES 26 A 327 HIS HIS
SEQRES 1 B 327 MET ALA PRO THR VAL LYS LEU LYS PRO TYR CYS GLN ASN
SEQRES 2 B 327 ILE ALA ASP ALA ALA THR ILE ASP SER THR GLN TYR PRO
SEQRES 3 B 327 PRO GLU VAL VAL ARG LYS ALA GLU ALA ALA SER ILE ILE
SEQRES 4 B 327 ASP ASP PRO LYS ALA LEU GLU GLY LEU PRO ASP VAL TYR
SEQRES 5 B 327 LEU GLU GLU LYS THR ILE ASN ARG LYS ASN GLY SER LYS
SEQRES 6 B 327 ILE GLU LEU THR ILE THR ARG PRO LEU ASP THR GLU ASN
SEQRES 7 B 327 GLN VAL LEU PRO PRO ILE VAL PHE PHE HIS GLY GLY GLY
SEQRES 8 B 327 TRP VAL VAL GLY SER LYS LEU THR HIS ARG ARG THR VAL
SEQRES 9 B 327 TYR GLU LEU THR VAL ARG ALA ARG ALA ALA VAL ILE PHE
SEQRES 10 B 327 VAL ASN TYR SER LEU SER PRO GLU VAL ARG PHE PRO THR
SEQRES 11 B 327 ALA LEU GLU GLU CYS LEU ASP ALA VAL VAL TRP VAL ALA
SEQRES 12 B 327 LYS GLU GLU ASN ALA LYS SER ILE ASN VAL ASP PRO THR
SEQRES 13 B 327 LYS LEU VAL VAL ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 14 B 327 SER ALA VAL VAL CYS ILE ARG ALA LYS GLN LEU GLY LEU
SEQRES 15 B 327 ASN ILE ILE LYS GLY GLN VAL LEU ILE TYR PRO VAL THR
SEQRES 16 B 327 ASP ASP ASN PHE GLU THR ASP SER TYR LYS GLN PHE ALA
SEQRES 17 B 327 GLU ASN TYR TYR LEU THR ARG LYS LEU MET VAL TRP PHE
SEQRES 18 B 327 PHE ASP HIS TYR ILE PRO ASP LYS LYS ASP ARG GLN SER
SEQRES 19 B 327 ILE PHE ALA CYS PRO LEU LYS ALA SER ILE ASP ASP LEU
SEQRES 20 B 327 ARG VAL LEU PRO ARG ALA LEU VAL ILE THR ALA GLU ALA
SEQRES 21 B 327 ASP VAL LEU ARG GLU GLU GLY GLU ALA TYR ALA ARG LYS
SEQRES 22 B 327 LEU ILE GLU ALA GLY ASN ASP VAL THR ALA VAL ARG TYR
SEQRES 23 B 327 LEU GLY ILE ILE HIS GLY ILE PHE ASN LEU ALA THR LEU
SEQRES 24 B 327 SER PRO THR GLY SER GLU ILE LEU ASP HIS ILE VAL ALA
SEQRES 25 B 327 TRP LEU GLN LYS THR TRP LYS LEU GLU HIS HIS HIS HIS
SEQRES 26 B 327 HIS HIS
SEQRES 1 C 327 MET ALA PRO THR VAL LYS LEU LYS PRO TYR CYS GLN ASN
SEQRES 2 C 327 ILE ALA ASP ALA ALA THR ILE ASP SER THR GLN TYR PRO
SEQRES 3 C 327 PRO GLU VAL VAL ARG LYS ALA GLU ALA ALA SER ILE ILE
SEQRES 4 C 327 ASP ASP PRO LYS ALA LEU GLU GLY LEU PRO ASP VAL TYR
SEQRES 5 C 327 LEU GLU GLU LYS THR ILE ASN ARG LYS ASN GLY SER LYS
SEQRES 6 C 327 ILE GLU LEU THR ILE THR ARG PRO LEU ASP THR GLU ASN
SEQRES 7 C 327 GLN VAL LEU PRO PRO ILE VAL PHE PHE HIS GLY GLY GLY
SEQRES 8 C 327 TRP VAL VAL GLY SER LYS LEU THR HIS ARG ARG THR VAL
SEQRES 9 C 327 TYR GLU LEU THR VAL ARG ALA ARG ALA ALA VAL ILE PHE
SEQRES 10 C 327 VAL ASN TYR SER LEU SER PRO GLU VAL ARG PHE PRO THR
SEQRES 11 C 327 ALA LEU GLU GLU CYS LEU ASP ALA VAL VAL TRP VAL ALA
SEQRES 12 C 327 LYS GLU GLU ASN ALA LYS SER ILE ASN VAL ASP PRO THR
SEQRES 13 C 327 LYS LEU VAL VAL ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 14 C 327 SER ALA VAL VAL CYS ILE ARG ALA LYS GLN LEU GLY LEU
SEQRES 15 C 327 ASN ILE ILE LYS GLY GLN VAL LEU ILE TYR PRO VAL THR
SEQRES 16 C 327 ASP ASP ASN PHE GLU THR ASP SER TYR LYS GLN PHE ALA
SEQRES 17 C 327 GLU ASN TYR TYR LEU THR ARG LYS LEU MET VAL TRP PHE
SEQRES 18 C 327 PHE ASP HIS TYR ILE PRO ASP LYS LYS ASP ARG GLN SER
SEQRES 19 C 327 ILE PHE ALA CYS PRO LEU LYS ALA SER ILE ASP ASP LEU
SEQRES 20 C 327 ARG VAL LEU PRO ARG ALA LEU VAL ILE THR ALA GLU ALA
SEQRES 21 C 327 ASP VAL LEU ARG GLU GLU GLY GLU ALA TYR ALA ARG LYS
SEQRES 22 C 327 LEU ILE GLU ALA GLY ASN ASP VAL THR ALA VAL ARG TYR
SEQRES 23 C 327 LEU GLY ILE ILE HIS GLY ILE PHE ASN LEU ALA THR LEU
SEQRES 24 C 327 SER PRO THR GLY SER GLU ILE LEU ASP HIS ILE VAL ALA
SEQRES 25 C 327 TRP LEU GLN LYS THR TRP LYS LEU GLU HIS HIS HIS HIS
SEQRES 26 C 327 HIS HIS
SEQRES 1 D 327 MET ALA PRO THR VAL LYS LEU LYS PRO TYR CYS GLN ASN
SEQRES 2 D 327 ILE ALA ASP ALA ALA THR ILE ASP SER THR GLN TYR PRO
SEQRES 3 D 327 PRO GLU VAL VAL ARG LYS ALA GLU ALA ALA SER ILE ILE
SEQRES 4 D 327 ASP ASP PRO LYS ALA LEU GLU GLY LEU PRO ASP VAL TYR
SEQRES 5 D 327 LEU GLU GLU LYS THR ILE ASN ARG LYS ASN GLY SER LYS
SEQRES 6 D 327 ILE GLU LEU THR ILE THR ARG PRO LEU ASP THR GLU ASN
SEQRES 7 D 327 GLN VAL LEU PRO PRO ILE VAL PHE PHE HIS GLY GLY GLY
SEQRES 8 D 327 TRP VAL VAL GLY SER LYS LEU THR HIS ARG ARG THR VAL
SEQRES 9 D 327 TYR GLU LEU THR VAL ARG ALA ARG ALA ALA VAL ILE PHE
SEQRES 10 D 327 VAL ASN TYR SER LEU SER PRO GLU VAL ARG PHE PRO THR
SEQRES 11 D 327 ALA LEU GLU GLU CYS LEU ASP ALA VAL VAL TRP VAL ALA
SEQRES 12 D 327 LYS GLU GLU ASN ALA LYS SER ILE ASN VAL ASP PRO THR
SEQRES 13 D 327 LYS LEU VAL VAL ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 14 D 327 SER ALA VAL VAL CYS ILE ARG ALA LYS GLN LEU GLY LEU
SEQRES 15 D 327 ASN ILE ILE LYS GLY GLN VAL LEU ILE TYR PRO VAL THR
SEQRES 16 D 327 ASP ASP ASN PHE GLU THR ASP SER TYR LYS GLN PHE ALA
SEQRES 17 D 327 GLU ASN TYR TYR LEU THR ARG LYS LEU MET VAL TRP PHE
SEQRES 18 D 327 PHE ASP HIS TYR ILE PRO ASP LYS LYS ASP ARG GLN SER
SEQRES 19 D 327 ILE PHE ALA CYS PRO LEU LYS ALA SER ILE ASP ASP LEU
SEQRES 20 D 327 ARG VAL LEU PRO ARG ALA LEU VAL ILE THR ALA GLU ALA
SEQRES 21 D 327 ASP VAL LEU ARG GLU GLU GLY GLU ALA TYR ALA ARG LYS
SEQRES 22 D 327 LEU ILE GLU ALA GLY ASN ASP VAL THR ALA VAL ARG TYR
SEQRES 23 D 327 LEU GLY ILE ILE HIS GLY ILE PHE ASN LEU ALA THR LEU
SEQRES 24 D 327 SER PRO THR GLY SER GLU ILE LEU ASP HIS ILE VAL ALA
SEQRES 25 D 327 TRP LEU GLN LYS THR TRP LYS LEU GLU HIS HIS HIS HIS
SEQRES 26 D 327 HIS HIS
FORMUL 5 HOH *529(H2 O)
HELIX 1 AA1 LYS A 8 ALA A 18 1 11
HELIX 2 AA2 ASP A 21 TYR A 25 5 5
HELIX 3 AA3 PRO A 26 ASP A 40 1 15
HELIX 4 AA4 HIS A 100 ARG A 112 1 13
HELIX 5 AA5 PRO A 129 LYS A 144 1 16
HELIX 6 AA6 LYS A 144 ILE A 151 1 8
HELIX 7 AA7 ASP A 154 LEU A 158 5 5
HELIX 8 AA8 SER A 164 LEU A 180 1 17
HELIX 9 AA9 THR A 201 PHE A 207 1 7
HELIX 10 AB1 THR A 214 ILE A 226 1 13
HELIX 11 AB2 ASP A 228 SER A 234 5 7
HELIX 12 AB3 CYS A 238 ALA A 242 5 5
HELIX 13 AB4 SER A 243 ARG A 248 1 6
HELIX 14 AB5 LEU A 263 ALA A 277 1 15
HELIX 15 AB6 SER A 300 HIS A 323 1 24
HELIX 16 AB7 LYS B 8 ALA B 17 1 10
HELIX 17 AB8 ASP B 21 TYR B 25 5 5
HELIX 18 AB9 PRO B 26 ASP B 40 1 15
HELIX 19 AC1 HIS B 100 ARG B 112 1 13
HELIX 20 AC2 PRO B 129 LYS B 144 1 16
HELIX 21 AC3 LYS B 144 ILE B 151 1 8
HELIX 22 AC4 ASP B 154 LEU B 158 5 5
HELIX 23 AC5 SER B 164 LEU B 180 1 17
HELIX 24 AC6 THR B 201 PHE B 207 1 7
HELIX 25 AC7 THR B 214 ILE B 226 1 13
HELIX 26 AC8 ASP B 228 SER B 234 5 7
HELIX 27 AC9 CYS B 238 ALA B 242 5 5
HELIX 28 AD1 ILE B 244 ARG B 248 5 5
HELIX 29 AD2 LEU B 263 ALA B 277 1 15
HELIX 30 AD3 SER B 300 HIS B 322 1 23
HELIX 31 AD4 LYS C 8 ALA C 17 1 10
HELIX 32 AD5 PRO C 26 ASP C 40 1 15
HELIX 33 AD6 HIS C 100 ARG C 112 1 13
HELIX 34 AD7 PRO C 129 LYS C 144 1 16
HELIX 35 AD8 LYS C 144 ILE C 151 1 8
HELIX 36 AD9 ASP C 154 LEU C 158 5 5
HELIX 37 AE1 SER C 164 LEU C 180 1 17
HELIX 38 AE2 THR C 201 ALA C 208 1 8
HELIX 39 AE3 THR C 214 ILE C 226 1 13
HELIX 40 AE4 LYS C 230 SER C 234 5 5
HELIX 41 AE5 CYS C 238 ALA C 242 5 5
HELIX 42 AE6 LEU C 263 ALA C 277 1 15
HELIX 43 AE7 SER C 300 HIS C 322 1 23
HELIX 44 AE8 LYS D 8 ALA D 18 1 11
HELIX 45 AE9 ASP D 21 TYR D 25 5 5
HELIX 46 AF1 PRO D 26 ASP D 41 1 16
HELIX 47 AF2 HIS D 100 ARG D 112 1 13
HELIX 48 AF3 PRO D 129 LYS D 144 1 16
HELIX 49 AF4 LYS D 144 ILE D 151 1 8
HELIX 50 AF5 ASP D 154 LEU D 158 5 5
HELIX 51 AF6 SER D 164 LEU D 180 1 17
HELIX 52 AF7 THR D 201 ALA D 208 1 8
HELIX 53 AF8 THR D 214 ILE D 226 1 13
HELIX 54 AF9 LYS D 230 SER D 234 5 5
HELIX 55 AG1 CYS D 238 ALA D 242 5 5
HELIX 56 AG2 LEU D 263 ALA D 277 1 15
HELIX 57 AG3 SER D 300 HIS D 324 1 25
SHEET 1 AA116 VAL A 51 ASN A 59 0
SHEET 2 AA116 LYS A 65 PRO A 73 -1 O ARG A 72 N TYR A 52
SHEET 3 AA116 ALA A 114 VAL A 118 -1 O PHE A 117 N THR A 69
SHEET 4 AA116 PRO A 83 PHE A 87 1 N ILE A 84 O ILE A 116
SHEET 5 AA116 VAL A 159 ASP A 163 1 O VAL A 159 N VAL A 85
SHEET 6 AA116 GLN A 188 ILE A 191 1 O ILE A 191 N GLY A 162
SHEET 7 AA116 ALA A 253 ALA A 260 1 O LEU A 254 N LEU A 190
SHEET 8 AA116 VAL A 281 ILE A 290 1 O THR A 282 N VAL A 255
SHEET 9 AA116 VAL B 281 ILE B 290 -1 O ALA B 283 N LEU A 287
SHEET 10 AA116 ALA B 253 ALA B 260 1 N VAL B 255 O THR B 282
SHEET 11 AA116 GLN B 188 ILE B 191 1 N LEU B 190 O LEU B 254
SHEET 12 AA116 VAL B 159 ASP B 163 1 N GLY B 162 O ILE B 191
SHEET 13 AA116 PRO B 83 PHE B 87 1 N PHE B 87 O ALA B 161
SHEET 14 AA116 ALA B 114 ASN B 119 1 O ILE B 116 N ILE B 84
SHEET 15 AA116 LYS B 65 PRO B 73 -1 N THR B 71 O VAL B 115
SHEET 16 AA116 VAL B 51 ASN B 59 -1 N LYS B 56 O LEU B 68
SHEET 1 AA216 TYR C 52 ASN C 59 0
SHEET 2 AA216 LYS C 65 ARG C 72 -1 O ILE C 70 N GLU C 54
SHEET 3 AA216 ALA C 114 ASN C 119 -1 O PHE C 117 N THR C 69
SHEET 4 AA216 PRO C 83 PHE C 87 1 N ILE C 84 O ILE C 116
SHEET 5 AA216 VAL C 159 ASP C 163 1 O VAL C 159 N VAL C 85
SHEET 6 AA216 GLN C 188 ILE C 191 1 O ILE C 191 N GLY C 162
SHEET 7 AA216 ALA C 253 ALA C 260 1 O LEU C 254 N LEU C 190
SHEET 8 AA216 VAL C 281 ILE C 290 1 O THR C 282 N VAL C 255
SHEET 9 AA216 VAL D 281 ILE D 290 -1 O ARG D 285 N ARG C 285
SHEET 10 AA216 ALA D 253 ALA D 260 1 N THR D 257 O TYR D 286
SHEET 11 AA216 GLN D 188 ILE D 191 1 N LEU D 190 O ILE D 256
SHEET 12 AA216 VAL D 159 ASP D 163 1 N GLY D 162 O ILE D 191
SHEET 13 AA216 PRO D 83 PHE D 87 1 N VAL D 85 O VAL D 159
SHEET 14 AA216 ALA D 114 ASN D 119 1 O ILE D 116 N ILE D 84
SHEET 15 AA216 ILE D 66 PRO D 73 -1 N THR D 69 O PHE D 117
SHEET 16 AA216 VAL D 51 ILE D 58 -1 N GLU D 54 O ILE D 70
CISPEP 1 SER A 123 PRO A 124 0 3.27
CISPEP 2 PHE A 128 PRO A 129 0 2.14
CISPEP 3 HIS A 323 HIS A 324 0 15.96
CISPEP 4 SER B 123 PRO B 124 0 3.49
CISPEP 5 PHE B 128 PRO B 129 0 3.39
CISPEP 6 SER C 123 PRO C 124 0 1.86
CISPEP 7 PHE C 128 PRO C 129 0 0.56
CISPEP 8 ASN D 62 GLY D 63 0 24.32
CISPEP 9 SER D 123 PRO D 124 0 3.62
CISPEP 10 PHE D 128 PRO D 129 0 1.62
CRYST1 151.125 49.675 183.214 90.00 111.57 90.00 C 1 2 1 16
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 0.006617 0.000000 0.002616 0.00000
SCALE2 0.000000 0.020131 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005869 0.00000
TER 2577 HIS A 327
TER 5135 HIS B 326
TER 7682 HIS C 325
TER 10210 HIS D 324
MASTER 371 0 0 57 32 0 0 610727 4 0 104
END |