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HEADER HYDROLASE 04-JUN-17 5W1U
TITLE CULEX QUINQUEFASCIATUS CARBOXYLESTERASE B2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CULEX QUINQUEFASCIATUS;
SOURCE 3 ORGANISM_COMMON: SOUTHERN HOUSE MOSQUITO;
SOURCE 4 ORGANISM_TAXID: 7176;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CARBOXYLESTERASE, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.HOPKINS,C.J.JACKSON
REVDAT 1 16-AUG-17 5W1U 0
JRNL AUTH D.H.HOPKINS,C.J.JACKSON
JRNL TITL STRUCTURE OF CULEX QUINQUEFASCIATUS CARBOXYLESTERASE B2 AT
JRNL TITL 2 2.5 ANGSTROMS RESOLUTION.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 53336
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.870
REMARK 3 FREE R VALUE TEST SET COUNT : 2599
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 45.5886 - 6.6645 1.00 2844 159 0.1491 0.2097
REMARK 3 2 6.6645 - 5.2923 1.00 2732 137 0.1513 0.2290
REMARK 3 3 5.2923 - 4.6241 1.00 2717 132 0.1461 0.2136
REMARK 3 4 4.6241 - 4.2016 1.00 2691 139 0.1547 0.2465
REMARK 3 5 4.2016 - 3.9006 1.00 2644 183 0.1653 0.2442
REMARK 3 6 3.9006 - 3.6708 1.00 2630 167 0.1769 0.2258
REMARK 3 7 3.6708 - 3.4870 1.00 2673 131 0.1947 0.2925
REMARK 3 8 3.4870 - 3.3353 1.00 2722 86 0.2071 0.2993
REMARK 3 9 3.3353 - 3.2069 1.00 2647 132 0.2159 0.2775
REMARK 3 10 3.2069 - 3.0963 1.00 2668 116 0.2256 0.3177
REMARK 3 11 3.0963 - 2.9995 1.00 2652 136 0.2436 0.3317
REMARK 3 12 2.9995 - 2.9138 1.00 2630 151 0.2452 0.3128
REMARK 3 13 2.9138 - 2.8371 1.00 2628 149 0.2501 0.3362
REMARK 3 14 2.8371 - 2.7678 1.00 2650 131 0.2503 0.3608
REMARK 3 15 2.7678 - 2.7049 1.00 2660 139 0.2617 0.3243
REMARK 3 16 2.7049 - 2.6474 1.00 2665 115 0.2599 0.3412
REMARK 3 17 2.6474 - 2.5944 1.00 2633 119 0.2737 0.3809
REMARK 3 18 2.5944 - 2.5455 1.00 2622 152 0.2857 0.3648
REMARK 3 19 2.5455 - 2.5000 1.00 2629 125 0.3024 0.3788
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) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.890
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 : 0.016 8741
REMARK 3 ANGLE : 1.646 11842
REMARK 3 CHIRALITY : 0.064 1261
REMARK 3 PLANARITY : 0.008 1548
REMARK 3 DIHEDRAL : 17.692 3254
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 5W1U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000227961.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95370
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53392
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 91.160
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.16100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.90
REMARK 200 R MERGE FOR SHELL (I) : 1.22600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, 0.1 M HEPES,
REMARK 280 PH 7, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.54067
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 56.27033
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 56.27033
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 112.54067
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 LEU A 3
REMARK 465 GLU A 4
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LEU B 3
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 OD1 ASP B 124 HG SER B 451 1.45
REMARK 500 H VAL B 8 O VAL B 15 1.49
REMARK 500 H THR A 502 OE2 GLU B 538 1.53
REMARK 500 HH11 ARG A 360 O HOH A 707 1.55
REMARK 500 HH TYR B 199 O SER B 225 1.55
REMARK 500 HH TYR B 121 O HOH B 709 1.55
REMARK 500 H THR A 462 O HOH A 715 1.55
REMARK 500 H GLY A 325 OG SER A 390 1.57
REMARK 500 HD1 HIS B 190 O HOH B 712 1.57
REMARK 500 HH21 ARG B 307 O HOH B 701 1.60
REMARK 500 O HOH B 793 O HOH B 824 2.04
REMARK 500 O HOH A 792 O HOH A 820 2.04
REMARK 500 O THR A 454 O HOH A 701 2.06
REMARK 500 O ASN A 513 O HOH A 702 2.12
REMARK 500 NH2 ARG B 307 O HOH B 701 2.12
REMARK 500 OE1 GLU B 82 O HOH B 702 2.13
REMARK 500 O VAL B 479 O HOH B 703 2.15
REMARK 500 OE2 GLU A 445 O HOH A 703 2.16
REMARK 500 O TYR A 521 O HOH A 704 2.16
REMARK 500 OG SER B 356 O HOH B 704 2.17
REMARK 500 O PRO A 342 O HOH A 705 2.17
REMARK 500 O8 MLI A 601 O HOH A 706 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ARG B 526 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
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 LEU A 6 25.08 -160.56
REMARK 500 SER A 22 171.42 -57.27
REMARK 500 PRO A 40 72.90 -65.88
REMARK 500 PHE A 46 -13.60 91.44
REMARK 500 CYS A 81 145.63 -170.04
REMARK 500 PRO A 96 5.91 -63.46
REMARK 500 PHE A 111 -3.19 63.74
REMARK 500 TYR A 121 67.56 -116.88
REMARK 500 PHE A 145 25.41 -142.39
REMARK 500 ASN A 174 -41.48 -131.81
REMARK 500 PRO A 182 -7.77 -52.50
REMARK 500 SER A 191 -127.61 50.49
REMARK 500 ASP A 208 30.82 33.66
REMARK 500 ASN A 231 38.87 70.60
REMARK 500 GLN A 267 -99.40 -32.58
REMARK 500 LYS A 269 -84.97 -40.53
REMARK 500 LEU A 271 -73.40 -157.05
REMARK 500 GLN A 274 -26.41 84.00
REMARK 500 ASP A 279 95.62 -54.35
REMARK 500 GLN A 335 71.59 70.47
REMARK 500 PRO A 336 -166.15 -57.45
REMARK 500 GLU A 337 -5.90 61.33
REMARK 500 TYR A 372 58.57 -157.53
REMARK 500 ASP A 374 88.39 -151.53
REMARK 500 SER A 375 165.98 173.45
REMARK 500 PHE A 394 -56.50 -130.09
REMARK 500 ILE A 433 -69.49 -109.33
REMARK 500 ASP A 434 131.13 -170.99
REMARK 500 ALA A 443 2.53 82.47
REMARK 500 VAL A 457 116.04 -160.30
REMARK 500 LYS A 460 -10.86 78.45
REMARK 500 LYS A 491 23.98 -78.81
REMARK 500 ASP A 514 32.15 -87.53
REMARK 500 TYR A 534 47.44 -97.81
REMARK 500 SER B 20 -172.74 -171.65
REMARK 500 SER B 30 102.65 -166.90
REMARK 500 PHE B 46 -12.83 77.87
REMARK 500 THR B 58 117.77 -37.78
REMARK 500 LEU B 85 70.61 -62.63
REMARK 500 ASN B 95 75.79 -117.59
REMARK 500 PRO B 96 -1.91 -58.32
REMARK 500 LYS B 98 69.40 -173.36
REMARK 500 PHE B 145 19.32 -152.99
REMARK 500 SER B 191 -121.60 60.77
REMARK 500 ASP B 208 19.41 48.01
REMARK 500 ARG B 230 59.07 -143.99
REMARK 500 ILE B 263 -70.16 -77.05
REMARK 500 PHE B 281 -70.14 -69.42
REMARK 500 PRO B 336 -175.63 -58.85
REMARK 500 TYR B 372 54.05 -153.35
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
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 EPE A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI B 601
DBREF 5W1U A 1 540 UNP Q23734 Q23734_CULQU 1 540
DBREF 5W1U B 1 540 UNP Q23734 Q23734_CULQU 1 540
SEQRES 1 A 540 MET SER LEU GLU SER LEU THR VAL GLN THR LYS TYR GLY
SEQRES 2 A 540 PRO VAL ARG GLY LYS ARG SER VAL SER LEU LEU GLY GLN
SEQRES 3 A 540 GLU TYR VAL SER PHE GLN GLY ILE PRO TYR ALA ARG ALA
SEQRES 4 A 540 PRO GLU GLY GLU LEU ARG PHE LYS ALA PRO VAL PRO PRO
SEQRES 5 A 540 GLN ASN TRP THR GLU THR LEU ASP CYS SER GLN GLN CYS
SEQRES 6 A 540 GLU PRO CYS TYR HIS PHE ASP ARG ARG LEU GLN LYS ILE
SEQRES 7 A 540 VAL GLY CYS GLU ASP SER LEU LYS ILE ASN VAL PHE ALA
SEQRES 8 A 540 LYS GLU ILE ASN PRO SER LYS PRO LEU PRO VAL MET LEU
SEQRES 9 A 540 TYR ILE TYR GLY GLY GLY PHE THR GLU GLY THR SER GLY
SEQRES 10 A 540 THR GLU LEU TYR GLY PRO ASP PHE LEU VAL GLN LYS ASP
SEQRES 11 A 540 ILE VAL LEU VAL SER PHE ASN TYR ARG ILE GLY ALA LEU
SEQRES 12 A 540 GLY PHE LEU CYS CYS GLN SER GLU GLN ASP GLY VAL PRO
SEQRES 13 A 540 GLY ASN ALA GLY LEU LYS ASP GLN ASN LEU ALA ILE ARG
SEQRES 14 A 540 TRP VAL LEU GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO
SEQRES 15 A 540 LYS ARG VAL THR LEU VAL GLY HIS SER ALA GLY ALA ALA
SEQRES 16 A 540 SER VAL GLN TYR HIS LEU ILE SER ASP ALA SER LYS ASP
SEQRES 17 A 540 LEU PHE GLN ARG ALA ILE VAL MET SER GLY SER THR TYR
SEQRES 18 A 540 ASN SER TRP SER LEU THR ARG GLN ARG ASN TRP VAL GLU
SEQRES 19 A 540 LYS LEU ALA LYS ALA ILE GLY TRP ASP GLY GLN GLY GLY
SEQRES 20 A 540 GLU SER GLY ALA LEU ARG PHE LEU LYS ALA ALA LYS PRO
SEQRES 21 A 540 GLU ASP ILE VAL ALA ASN GLN GLU LYS LEU LEU THR ASP
SEQRES 22 A 540 GLN ASP MET GLN ASP ASP ILE PHE THR PRO PHE GLY PRO
SEQRES 23 A 540 THR VAL GLU PRO TYR LEU THR GLU GLN CYS MET ILE PRO
SEQRES 24 A 540 LYS GLU PRO PHE GLU MET ALA ARG THR ALA TRP GLY ASP
SEQRES 25 A 540 LYS ILE ASP ILE MET ILE GLY GLY THR SER GLU GLU GLY
SEQRES 26 A 540 LEU LEU LEU LEU GLN LYS ILE LYS LEU GLN PRO GLU LEU
SEQRES 27 A 540 LEU SER HIS PRO HIS LEU PHE LEU GLY ASN VAL PRO PRO
SEQRES 28 A 540 ASN LEU LYS ILE SER MET GLU LYS ARG ILE GLU PHE ALA
SEQRES 29 A 540 ALA LYS LEU LYS GLN ARG TYR TYR PRO ASP SER SER PRO
SEQRES 30 A 540 SER MET GLU ASN ASN LEU GLY TYR VAL HIS MET MET SER
SEQRES 31 A 540 ASP ARG VAL PHE TRP HIS GLY LEU HIS ARG THR ILE LEU
SEQRES 32 A 540 ALA ARG ALA ALA ARG SER ARG ALA ARG THR PHE VAL TYR
SEQRES 33 A 540 ARG ILE CYS LEU ASP SER GLU PHE TYR ASN HIS TYR ARG
SEQRES 34 A 540 ILE MET MET ILE ASP PRO LYS LEU ARG GLY THR ALA HIS
SEQRES 35 A 540 ALA ASP GLU LEU SER TYR LEU PHE SER ASN PHE THR GLN
SEQRES 36 A 540 GLN VAL PRO GLY LYS GLU THR PHE GLU TYR ARG GLY LEU
SEQRES 37 A 540 GLN THR LEU VAL ASP VAL PHE THR ALA PHE VAL ILE ASN
SEQRES 38 A 540 GLY ASP PRO ASN CYS GLY MET THR ALA LYS SER GLY VAL
SEQRES 39 A 540 VAL PHE GLU PRO ASN ALA GLN THR LYS PRO THR PHE LYS
SEQRES 40 A 540 CYS LEU ASN ILE ALA ASN ASP GLY VAL ALA PHE VAL ASP
SEQRES 41 A 540 TYR PRO ASP ALA ASP ARG LEU ASP MET TRP ASP ALA MET
SEQRES 42 A 540 TYR VAL ASN ASP GLU LEU PHE
SEQRES 1 B 540 MET SER LEU GLU SER LEU THR VAL GLN THR LYS TYR GLY
SEQRES 2 B 540 PRO VAL ARG GLY LYS ARG SER VAL SER LEU LEU GLY GLN
SEQRES 3 B 540 GLU TYR VAL SER PHE GLN GLY ILE PRO TYR ALA ARG ALA
SEQRES 4 B 540 PRO GLU GLY GLU LEU ARG PHE LYS ALA PRO VAL PRO PRO
SEQRES 5 B 540 GLN ASN TRP THR GLU THR LEU ASP CYS SER GLN GLN CYS
SEQRES 6 B 540 GLU PRO CYS TYR HIS PHE ASP ARG ARG LEU GLN LYS ILE
SEQRES 7 B 540 VAL GLY CYS GLU ASP SER LEU LYS ILE ASN VAL PHE ALA
SEQRES 8 B 540 LYS GLU ILE ASN PRO SER LYS PRO LEU PRO VAL MET LEU
SEQRES 9 B 540 TYR ILE TYR GLY GLY GLY PHE THR GLU GLY THR SER GLY
SEQRES 10 B 540 THR GLU LEU TYR GLY PRO ASP PHE LEU VAL GLN LYS ASP
SEQRES 11 B 540 ILE VAL LEU VAL SER PHE ASN TYR ARG ILE GLY ALA LEU
SEQRES 12 B 540 GLY PHE LEU CYS CYS GLN SER GLU GLN ASP GLY VAL PRO
SEQRES 13 B 540 GLY ASN ALA GLY LEU LYS ASP GLN ASN LEU ALA ILE ARG
SEQRES 14 B 540 TRP VAL LEU GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO
SEQRES 15 B 540 LYS ARG VAL THR LEU VAL GLY HIS SER ALA GLY ALA ALA
SEQRES 16 B 540 SER VAL GLN TYR HIS LEU ILE SER ASP ALA SER LYS ASP
SEQRES 17 B 540 LEU PHE GLN ARG ALA ILE VAL MET SER GLY SER THR TYR
SEQRES 18 B 540 ASN SER TRP SER LEU THR ARG GLN ARG ASN TRP VAL GLU
SEQRES 19 B 540 LYS LEU ALA LYS ALA ILE GLY TRP ASP GLY GLN GLY GLY
SEQRES 20 B 540 GLU SER GLY ALA LEU ARG PHE LEU LYS ALA ALA LYS PRO
SEQRES 21 B 540 GLU ASP ILE VAL ALA ASN GLN GLU LYS LEU LEU THR ASP
SEQRES 22 B 540 GLN ASP MET GLN ASP ASP ILE PHE THR PRO PHE GLY PRO
SEQRES 23 B 540 THR VAL GLU PRO TYR LEU THR GLU GLN CYS MET ILE PRO
SEQRES 24 B 540 LYS GLU PRO PHE GLU MET ALA ARG THR ALA TRP GLY ASP
SEQRES 25 B 540 LYS ILE ASP ILE MET ILE GLY GLY THR SER GLU GLU GLY
SEQRES 26 B 540 LEU LEU LEU LEU GLN LYS ILE LYS LEU GLN PRO GLU LEU
SEQRES 27 B 540 LEU SER HIS PRO HIS LEU PHE LEU GLY ASN VAL PRO PRO
SEQRES 28 B 540 ASN LEU LYS ILE SER MET GLU LYS ARG ILE GLU PHE ALA
SEQRES 29 B 540 ALA LYS LEU LYS GLN ARG TYR TYR PRO ASP SER SER PRO
SEQRES 30 B 540 SER MET GLU ASN ASN LEU GLY TYR VAL HIS MET MET SER
SEQRES 31 B 540 ASP ARG VAL PHE TRP HIS GLY LEU HIS ARG THR ILE LEU
SEQRES 32 B 540 ALA ARG ALA ALA ARG SER ARG ALA ARG THR PHE VAL TYR
SEQRES 33 B 540 ARG ILE CYS LEU ASP SER GLU PHE TYR ASN HIS TYR ARG
SEQRES 34 B 540 ILE MET MET ILE ASP PRO LYS LEU ARG GLY THR ALA HIS
SEQRES 35 B 540 ALA ASP GLU LEU SER TYR LEU PHE SER ASN PHE THR GLN
SEQRES 36 B 540 GLN VAL PRO GLY LYS GLU THR PHE GLU TYR ARG GLY LEU
SEQRES 37 B 540 GLN THR LEU VAL ASP VAL PHE THR ALA PHE VAL ILE ASN
SEQRES 38 B 540 GLY ASP PRO ASN CYS GLY MET THR ALA LYS SER GLY VAL
SEQRES 39 B 540 VAL PHE GLU PRO ASN ALA GLN THR LYS PRO THR PHE LYS
SEQRES 40 B 540 CYS LEU ASN ILE ALA ASN ASP GLY VAL ALA PHE VAL ASP
SEQRES 41 B 540 TYR PRO ASP ALA ASP ARG LEU ASP MET TRP ASP ALA MET
SEQRES 42 B 540 TYR VAL ASN ASP GLU LEU PHE
HET EPE A 600 32
HET MLI A 601 9
HET EPE B 600 32
HET MLI B 601 9
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETNAM MLI MALONATE ION
HETSYN EPE HEPES
FORMUL 3 EPE 2(C8 H18 N2 O4 S)
FORMUL 4 MLI 2(C3 H2 O4 2-)
FORMUL 7 HOH *260(H2 O)
HELIX 1 AA1 PHE A 125 LYS A 129 5 5
HELIX 2 AA2 GLY A 141 LEU A 146 1 6
HELIX 3 AA3 SER A 150 GLY A 154 5 5
HELIX 4 AA4 ASN A 158 ILE A 175 1 18
HELIX 5 AA5 ALA A 176 PHE A 178 5 3
HELIX 6 AA6 SER A 191 SER A 203 1 13
HELIX 7 AA7 ASP A 204 LYS A 207 5 4
HELIX 8 AA8 ASN A 222 LEU A 226 5 5
HELIX 9 AA9 ASN A 231 TRP A 242 1 12
HELIX 10 AB1 GLY A 246 LYS A 256 1 11
HELIX 11 AB2 LYS A 259 GLN A 267 1 9
HELIX 12 AB3 GLN A 274 ASP A 278 5 5
HELIX 13 AB4 GLU A 301 ALA A 306 1 6
HELIX 14 AB5 ARG A 307 ILE A 314 5 8
HELIX 15 AB6 GLU A 323 LEU A 327 5 5
HELIX 16 AB7 LEU A 328 LEU A 334 1 7
HELIX 17 AB8 SER A 356 TYR A 372 1 17
HELIX 18 AB9 ASN A 382 PHE A 394 1 13
HELIX 19 AC1 PHE A 394 SER A 409 1 16
HELIX 20 AC2 ASN A 426 MET A 432 1 7
HELIX 21 AC3 ALA A 443 LEU A 449 5 7
HELIX 22 AC4 THR A 462 GLY A 482 1 21
HELIX 23 AC5 CYS A 486 LYS A 491 1 6
HELIX 24 AC6 ASP A 523 TYR A 534 1 12
HELIX 25 AC7 PHE B 125 LYS B 129 5 5
HELIX 26 AC8 GLY B 141 LEU B 146 1 6
HELIX 27 AC9 SER B 150 GLY B 154 5 5
HELIX 28 AD1 ASN B 158 ILE B 175 1 18
HELIX 29 AD2 ALA B 176 PHE B 178 5 3
HELIX 30 AD3 SER B 191 SER B 203 1 13
HELIX 31 AD4 ASP B 204 LYS B 207 5 4
HELIX 32 AD5 ASN B 222 LEU B 226 5 5
HELIX 33 AD6 ASN B 231 GLY B 241 1 11
HELIX 34 AD7 GLY B 246 ALA B 258 1 13
HELIX 35 AD8 LYS B 259 GLU B 268 1 10
HELIX 36 AD9 GLU B 301 THR B 308 1 8
HELIX 37 AE1 ALA B 309 ILE B 314 5 6
HELIX 38 AE2 GLU B 323 LEU B 327 5 5
HELIX 39 AE3 LEU B 328 LYS B 333 1 6
HELIX 40 AE4 GLU B 337 HIS B 341 5 5
HELIX 41 AE5 PHE B 345 VAL B 349 5 5
HELIX 42 AE6 SER B 356 TYR B 372 1 17
HELIX 43 AE7 ASN B 382 PHE B 394 1 13
HELIX 44 AE8 PHE B 394 SER B 409 1 16
HELIX 45 AE9 ASN B 426 ILE B 433 1 8
HELIX 46 AF1 ASP B 444 LEU B 449 5 6
HELIX 47 AF2 THR B 462 GLY B 482 1 21
HELIX 48 AF3 CYS B 486 SER B 492 1 7
HELIX 49 AF4 ASP B 523 TYR B 534 1 12
SHEET 1 AA1 3 THR A 7 THR A 10 0
SHEET 2 AA1 3 GLY A 13 ARG A 16 -1 O VAL A 15 N VAL A 8
SHEET 3 AA1 3 LEU A 59 ASP A 60 1 O LEU A 59 N PRO A 14
SHEET 1 AA211 LYS A 18 VAL A 21 0
SHEET 2 AA211 GLU A 27 PRO A 35 -1 O SER A 30 N LYS A 18
SHEET 3 AA211 LYS A 86 ALA A 91 -1 O ILE A 87 N ILE A 34
SHEET 4 AA211 VAL A 132 PHE A 136 -1 O SER A 135 N ASN A 88
SHEET 5 AA211 LEU A 100 ILE A 106 1 N TYR A 105 O VAL A 134
SHEET 6 AA211 GLY A 180 HIS A 190 1 O THR A 186 N LEU A 104
SHEET 7 AA211 ARG A 212 MET A 216 1 O ILE A 214 N LEU A 187
SHEET 8 AA211 ASP A 315 THR A 321 1 O MET A 317 N VAL A 215
SHEET 9 AA211 THR A 413 ILE A 418 1 O PHE A 414 N ILE A 318
SHEET 10 AA211 LYS A 507 ILE A 511 1 O LEU A 509 N VAL A 415
SHEET 11 AA211 PHE A 518 ASP A 520 -1 O VAL A 519 N CYS A 508
SHEET 1 AA3 2 HIS A 70 PHE A 71 0
SHEET 2 AA3 2 ILE A 78 VAL A 79 -1 O VAL A 79 N HIS A 70
SHEET 1 AA4 3 THR B 7 THR B 10 0
SHEET 2 AA4 3 GLY B 13 ARG B 16 -1 O VAL B 15 N VAL B 8
SHEET 3 AA4 3 LEU B 59 ASP B 60 1 O LEU B 59 N ARG B 16
SHEET 1 AA511 ARG B 19 VAL B 21 0
SHEET 2 AA511 GLU B 27 PRO B 35 -1 O TYR B 28 N SER B 20
SHEET 3 AA511 LYS B 86 ALA B 91 -1 O ILE B 87 N ILE B 34
SHEET 4 AA511 VAL B 132 PHE B 136 -1 O LEU B 133 N PHE B 90
SHEET 5 AA511 LEU B 100 ILE B 106 1 N TYR B 105 O VAL B 134
SHEET 6 AA511 GLY B 180 HIS B 190 1 O VAL B 188 N LEU B 104
SHEET 7 AA511 ARG B 212 MET B 216 1 O ARG B 212 N LEU B 187
SHEET 8 AA511 ASP B 315 THR B 321 1 O MET B 317 N VAL B 215
SHEET 9 AA511 THR B 413 ILE B 418 1 O PHE B 414 N ILE B 318
SHEET 10 AA511 LYS B 507 ALA B 512 1 O LEU B 509 N VAL B 415
SHEET 11 AA511 GLY B 515 ASP B 520 -1 O ALA B 517 N ASN B 510
SHEET 1 AA6 2 HIS B 70 PHE B 71 0
SHEET 2 AA6 2 ILE B 78 VAL B 79 -1 O VAL B 79 N HIS B 70
CISPEP 1 LYS A 503 PRO A 504 0 4.63
CISPEP 2 LYS B 503 PRO B 504 0 -2.59
SITE 1 AC1 7 GLY A 109 TYR A 121 TYR A 428 ALA A 443
SITE 2 AC1 7 HOH A 706 HOH A 722 HOH A 767
SITE 1 AC2 6 TRP A 224 PHE A 281 LEU A 327 LYS A 331
SITE 2 AC2 6 VAL A 393 HOH A 706
SITE 1 AC3 5 GLY B 109 TYR B 121 TYR B 428 ALA B 443
SITE 2 AC3 5 MLI B 601
SITE 1 AC4 5 TRP B 224 PHE B 281 LEU B 327 EPE B 600
SITE 2 AC4 5 HOH B 724
CRYST1 125.070 125.070 168.811 90.00 90.00 120.00 P 32 2 1 12
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 0.007996 0.004616 0.000000 0.00000
SCALE2 0.000000 0.009232 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005924 0.00000
TER 8410 PHE A 540
TER 16833 PHE B 540
MASTER 374 0 4 49 32 0 8 6 8793 2 82 84
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