HEADER HYDROLASE/HYDROLASE INHIBITOR 20-SEP-14 4WH9
TITLE STRUCTURE OF THE CDC25B PHOSPHATASE CATALYTIC DOMAIN WITH BOUND
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: M-PHASE INDUCER PHOSPHATASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (UNP RESIDUES 386-565);
COMPND 5 SYNONYM: DUAL SPECIFICITY PHOSPHATASE CDC25B;
COMPND 6 EC: 3.1.3.48;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CDC25B, CDC25HU2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PHOSPHATASE, INHIBITOR, FRAGMENT, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.L.LUND,S.DUDKIN,D.BORKIN,W.NI,J.GREMBECKA,T.CIERPICKI
REVDAT 5 27-SEP-23 4WH9 1 REMARK
REVDAT 4 04-DEC-19 4WH9 1 REMARK
REVDAT 3 27-SEP-17 4WH9 1 SOURCE REMARK
REVDAT 2 04-MAR-15 4WH9 1 JRNL
REVDAT 1 10-DEC-14 4WH9 0
JRNL AUTH G.LUND,S.DUDKIN,D.BORKIN,W.NI,J.GREMBECKA,T.CIERPICKI
JRNL TITL INHIBITION OF CDC25B PHOSPHATASE THROUGH DISRUPTION OF
JRNL TITL 2 PROTEIN-PROTEIN INTERACTION.
JRNL REF ACS CHEM.BIOL. V. 10 390 2015
JRNL REFN ESSN 1554-8937
JRNL PMID 25423142
JRNL DOI 10.1021/CB500883H
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 42329
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.127
REMARK 3 R VALUE (WORKING SET) : 0.126
REMARK 3 FREE R VALUE : 0.152
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2226
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3109
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1730
REMARK 3 BIN FREE R VALUE SET COUNT : 146
REMARK 3 BIN FREE R VALUE : 0.2110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1472
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 296
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.050
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.049
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.032
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.650
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.975
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1621 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1505 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2197 ; 1.928 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3479 ; 1.422 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 191 ; 6.891 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 83 ;30.937 ;22.530
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 281 ;12.318 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;22.274 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 225 ; 0.130 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1791 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 397 ; 0.010 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 732 ; 3.031 ; 1.454
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 731 ; 3.033 ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 921 ; 3.407 ; 2.200
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 922 ; 3.405 ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 889 ; 6.465 ; 1.955
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 889 ; 6.465 ; 1.955
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1272 ; 6.783 ; 2.759
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2127 ; 6.167 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1943 ; 5.433 ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1578 ; 8.932 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1528 ;19.020 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4WH9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000203805.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.25-7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63905
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.330
REMARK 200 RESOLUTION RANGE LOW (A) : 51.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: 2A2K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: (NH4)2SO4, TRIS, TCEP, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 25.83000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.97000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.73500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.97000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.83000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.73500
REMARK 290 SMTRY3 4 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: 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 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 GLY A 369
REMARK 465 SER A 370
REMARK 465 SER A 371
REMARK 465 ASP A 372
REMARK 465 SER A 373
REMARK 465 ASP A 374
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 770 O HOH A 773 1.91
REMARK 500 OE1 GLU A 478 O HOH A 892 1.93
REMARK 500 OE2 GLU A 524 O HOH A 939 2.04
REMARK 500 O HOH A 802 O HOH A 944 2.19
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 439 -11.03 85.65
REMARK 500 SER A 473 -150.21 -137.43
REMARK 500 GLU A 478 -55.74 -129.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 HIS A 375 -10.53
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 799 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A 986 DISTANCE = 6.03 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3M8 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 606
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WH7 RELATED DB: PDB
DBREF 4WH9 A 372 551 UNP P30305 MPIP2_HUMAN 386 565
SEQADV 4WH9 GLY A 369 UNP P30305 EXPRESSION TAG
SEQADV 4WH9 SER A 370 UNP P30305 EXPRESSION TAG
SEQADV 4WH9 SER A 371 UNP P30305 EXPRESSION TAG
SEQADV 4WH9 SER A 473 UNP P30305 CYS 487 ENGINEERED MUTATION
SEQRES 1 A 183 GLY SER SER ASP SER ASP HIS ARG GLU LEU ILE GLY ASP
SEQRES 2 A 183 TYR SER LYS ALA PHE LEU LEU GLN THR VAL ASP GLY LYS
SEQRES 3 A 183 HIS GLN ASP LEU LYS TYR ILE SER PRO GLU THR MET VAL
SEQRES 4 A 183 ALA LEU LEU THR GLY LYS PHE SER ASN ILE VAL ASP LYS
SEQRES 5 A 183 PHE VAL ILE VAL ASP CYS ARG TYR PRO TYR GLU TYR GLU
SEQRES 6 A 183 GLY GLY HIS ILE LYS THR ALA VAL ASN LEU PRO LEU GLU
SEQRES 7 A 183 ARG ASP ALA GLU SER PHE LEU LEU LYS SER PRO ILE ALA
SEQRES 8 A 183 PRO CYS SER LEU ASP LYS ARG VAL ILE LEU ILE PHE HIS
SEQRES 9 A 183 SER GLU PHE SER SER GLU ARG GLY PRO ARG MET CYS ARG
SEQRES 10 A 183 PHE ILE ARG GLU ARG ASP ARG ALA VAL ASN ASP TYR PRO
SEQRES 11 A 183 SER LEU TYR TYR PRO GLU MET TYR ILE LEU LYS GLY GLY
SEQRES 12 A 183 TYR LYS GLU PHE PHE PRO GLN HIS PRO ASN PHE CYS GLU
SEQRES 13 A 183 PRO GLN ASP TYR ARG PRO MET ASN HIS GLU ALA PHE LYS
SEQRES 14 A 183 ASP GLU LEU LYS THR PHE ARG LEU LYS THR ARG SER TRP
SEQRES 15 A 183 ALA
HET 3M8 A 601 17
HET SO4 A 602 5
HET SO4 A 603 5
HET SO4 A 604 5
HET SO4 A 605 5
HET GOL A 606 12
HETNAM 3M8 2-[(2-CYANO-3-FLUORO-5-HYDROXYPHENYL)
HETNAM 2 3M8 SULFANYL]ETHANESULFONIC ACID
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 3M8 C9 H8 F N O4 S2
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 HOH *296(H2 O)
HELIX 1 AA1 SER A 402 THR A 411 1 10
HELIX 2 AA2 TYR A 428 GLY A 434 1 7
HELIX 3 AA3 LEU A 445 LYS A 455 1 11
HELIX 4 AA4 GLU A 478 ASN A 495 1 18
HELIX 5 AA5 GLY A 510 HIS A 519 1 10
HELIX 6 AA6 PHE A 536 LEU A 545 1 10
SHEET 1 AA1 5 TYR A 400 ILE A 401 0
SHEET 2 AA1 5 MET A 505 LEU A 508 1 O ILE A 507 N ILE A 401
SHEET 3 AA1 5 ARG A 466 HIS A 472 1 N PHE A 471 O TYR A 506
SHEET 4 AA1 5 VAL A 418 ASP A 425 1 N VAL A 424 O ILE A 470
SHEET 5 AA1 5 VAL A 441 ASN A 442 1 O VAL A 441 N ILE A 423
SHEET 1 AA2 2 HIS A 436 ILE A 437 0
SHEET 2 AA2 2 CYS A 523 GLU A 524 -1 O GLU A 524 N HIS A 436
CISPEP 1 TYR A 497 PRO A 498 0 7.91
CISPEP 2 GLU A 524 PRO A 525 0 -22.09
SITE 1 AC1 15 ASP A 397 LEU A 398 CYS A 484 ARG A 485
SITE 2 AC1 15 ARG A 488 ARG A 492 MET A 505 HOH A 714
SITE 3 AC1 15 HOH A 723 HOH A 763 HOH A 808 HOH A 821
SITE 4 AC1 15 HOH A 831 HOH A 861 HOH A 876
SITE 1 AC2 8 GLY A 393 LYS A 394 LYS A 509 HOH A 820
SITE 2 AC2 8 HOH A 829 HOH A 879 HOH A 890 HOH A 894
SITE 1 AC3 3 ILE A 417 ARG A 466 HOH A 886
SITE 1 AC4 9 SER A 473 GLU A 474 PHE A 475 SER A 476
SITE 2 AC4 9 SER A 477 GLU A 478 ARG A 479 HOH A 825
SITE 3 AC4 9 HOH A 958
SITE 1 AC5 4 ARG A 482 HOH A 839 HOH A 963 HOH A 968
SITE 1 AC6 6 LEU A 445 GLU A 446 ARG A 447 ARG A 482
SITE 2 AC6 6 THR A 547 ARG A 548
CRYST1 51.660 71.470 73.940 90.00 90.00 90.00 P 21 21 21 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 0.019357 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013992 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013524 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
