HEADER HYDROLASE 10-APR-15 4Z99
TITLE CRYSTAL STRUCTURE OF THE APO LOW MOLECULAR WEIGHT PROTEIN TYROSINE
TITLE 2 PHOSPHATASE ISOFORM A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LMW-PTPASE,ADIPOCYTE ACID PHOSPHATASE,LOW MOLECULAR WEIGHT
COMPND 5 CYTOSOLIC ACID PHOSPHATASE,RED CELL ACID PHOSPHATASE 1;
COMPND 6 EC: 3.1.3.48,3.1.3.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ACP1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS LMW-PTPASE, LMW-PTP, LOW MOLECULAR WEIGHT CYTOSOLIC ACID PHOSPHATASE,
KEYWDS 2 RED CELL ACID PHOSPHATASE 1, ADIPOCYTE ACID PHOSPHATASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.B.FONSECA,V.SCORSATO,M.P.DIAS,F.L.DE OLIVERIA,P.C.M.L.MIRANDA,
AUTHOR 2 R.APARICIO
REVDAT 7 27-SEP-23 4Z99 1 REMARK
REVDAT 6 01-JAN-20 4Z99 1 REMARK
REVDAT 5 17-APR-19 4Z99 1 REMARK
REVDAT 4 07-MAR-18 4Z99 1 REMARK
REVDAT 3 17-JAN-18 4Z99 1 JRNL REMARK
REVDAT 2 05-AUG-15 4Z99 1 JRNL
REVDAT 1 15-JUL-15 4Z99 0
JRNL AUTH E.M.FONSECA,D.B.TRIVELLA,V.SCORSATO,M.P.DIAS,N.L.BAZZO,
JRNL AUTH 2 K.R.MANDAPATI,F.L.DE OLIVEIRA,C.V.FERREIRA-HALDER,R.A.PILLI,
JRNL AUTH 3 P.C.MIRANDA,R.APARICIO
JRNL TITL CRYSTAL STRUCTURES OF THE APO FORM AND A COMPLEX OF HUMAN
JRNL TITL 2 LMW-PTP WITH A PHOSPHONIC ACID PROVIDE NEW EVIDENCE OF A
JRNL TITL 3 SECONDARY SITE POTENTIALLY RELATED TO THE ANCHORAGE OF
JRNL TITL 4 NATURAL SUBSTRATES.
JRNL REF BIOORG.MED.CHEM. V. 23 4462 2015
JRNL REFN ESSN 1464-3391
JRNL PMID 26117648
JRNL DOI 10.1016/J.BMC.2015.06.017
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 7967
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 385
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 586
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 30
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1294
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 122
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.26000
REMARK 3 B22 (A**2) : 1.41000
REMARK 3 B33 (A**2) : -0.15000
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): 0.349
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.283
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.211
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.951
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.865
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1319 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1211 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1782 ; 1.487 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2784 ; 0.880 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 163 ; 7.220 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 67 ;34.479 ;24.179
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 226 ;13.601 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;21.342 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 192 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1526 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 316 ; 0.001 ; 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): 655 ; 1.228 ; 1.847
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 654 ; 1.223 ; 1.843
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 817 ; 2.056 ; 2.760
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 818 ; 2.057 ; 2.765
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 664 ; 1.323 ; 1.988
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 664 ; 1.323 ; 1.987
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 965 ; 2.205 ; 2.929
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1539 ; 4.868 ;15.312
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1506 ; 4.634 ;15.021
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -6 A 0
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3088 -1.9182 40.4125
REMARK 3 T TENSOR
REMARK 3 T11: 0.1236 T22: 0.0928
REMARK 3 T33: 0.1047 T12: -0.0107
REMARK 3 T13: -0.0797 T23: 0.0737
REMARK 3 L TENSOR
REMARK 3 L11: 13.1171 L22: 3.1271
REMARK 3 L33: 13.2363 L12: 5.3803
REMARK 3 L13: -11.8906 L23: -3.3735
REMARK 3 S TENSOR
REMARK 3 S11: 0.6273 S12: 0.1295 S13: -0.0560
REMARK 3 S21: 0.4733 S22: -0.1752 S23: -0.3324
REMARK 3 S31: -0.2109 S32: -0.4950 S33: -0.4521
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 157
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2385 5.3406 12.0708
REMARK 3 T TENSOR
REMARK 3 T11: 0.0818 T22: 0.0269
REMARK 3 T33: 0.0162 T12: 0.0103
REMARK 3 T13: 0.0220 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.4053 L22: 0.6051
REMARK 3 L33: 1.0705 L12: 0.3065
REMARK 3 L13: -0.0254 L23: 0.4031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: -0.0397 S13: -0.0420
REMARK 3 S21: -0.0610 S22: 0.0202 S23: -0.0285
REMARK 3 S31: 0.0446 S32: 0.0546 S33: 0.0078
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 4Z99 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208745.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : QUAZAR(TM) CU MULTILAYER OPTIC
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : APEX II CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : APEX
REMARK 200 DATA SCALING SOFTWARE : APEX
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8392
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 54.160
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 8.570
REMARK 200 R MERGE (I) : 0.22620
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.94
REMARK 200 R MERGE FOR SHELL (I) : 0.62100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 5PNT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% (W/V) PEG 2000, 0.1 M MALIC
REMARK 280 ACID:TRIS, MOLAR RATIO 1:2, PH 7.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
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 16.33350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.02500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.07850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.02500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.33350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.07850
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 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 GLU A 37 CD OE1 OE2
REMARK 470 LYS A 112 CG CD CE NZ
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 LYS A 155 CG CD CE NZ
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 CYS A 17 -91.96 -107.29
REMARK 500 LYS A 155 85.40 -165.42
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 321 DISTANCE = 6.96 ANGSTROMS
REMARK 525 HOH A 322 DISTANCE = 8.44 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5PNT RELATED DB: PDB
REMARK 900 5PNT CONTAINS THE SAME PROTEIN IN COMPLEX WITH MES
REMARK 900 RELATED ID: 3N8I RELATED DB: PDB
REMARK 900 3N8I CONTAINS THE SAME PROTEIN IN COMPLEX WITH NLA IN A SECONDARY
REMARK 900 BINDING SITE
REMARK 900 RELATED ID: 4Z9A RELATED DB: PDB
REMARK 900 RELATED ID: 4Z9B RELATED DB: PDB
DBREF 4Z99 A 0 157 UNP P24666 PPAC_HUMAN 1 158
SEQADV 4Z99 GLY A -6 UNP P24666 EXPRESSION TAG
SEQADV 4Z99 SER A -5 UNP P24666 EXPRESSION TAG
SEQADV 4Z99 HIS A -4 UNP P24666 EXPRESSION TAG
SEQADV 4Z99 MET A -3 UNP P24666 EXPRESSION TAG
SEQADV 4Z99 GLU A -2 UNP P24666 EXPRESSION TAG
SEQADV 4Z99 PHE A -1 UNP P24666 EXPRESSION TAG
SEQRES 1 A 164 GLY SER HIS MET GLU PHE MET ALA GLU GLN ALA THR LYS
SEQRES 2 A 164 SER VAL LEU PHE VAL CYS LEU GLY ASN ILE CYS ARG SER
SEQRES 3 A 164 PRO ILE ALA GLU ALA VAL PHE ARG LYS LEU VAL THR ASP
SEQRES 4 A 164 GLN ASN ILE SER GLU ASN TRP ARG VAL ASP SER ALA ALA
SEQRES 5 A 164 THR SER GLY TYR GLU ILE GLY ASN PRO PRO ASP TYR ARG
SEQRES 6 A 164 GLY GLN SER CYS MET LYS ARG HIS GLY ILE PRO MET SER
SEQRES 7 A 164 HIS VAL ALA ARG GLN ILE THR LYS GLU ASP PHE ALA THR
SEQRES 8 A 164 PHE ASP TYR ILE LEU CYS MET ASP GLU SER ASN LEU ARG
SEQRES 9 A 164 ASP LEU ASN ARG LYS SER ASN GLN VAL LYS THR CYS LYS
SEQRES 10 A 164 ALA LYS ILE GLU LEU LEU GLY SER TYR ASP PRO GLN LYS
SEQRES 11 A 164 GLN LEU ILE ILE GLU ASP PRO TYR TYR GLY ASN ASP SER
SEQRES 12 A 164 ASP PHE GLU THR VAL TYR GLN GLN CYS VAL ARG CYS CYS
SEQRES 13 A 164 ARG ALA PHE LEU GLU LYS ALA HIS
FORMUL 2 HOH *122(H2 O)
HELIX 1 AA1 CYS A 17 GLN A 33 1 17
HELIX 2 AA2 ILE A 35 GLU A 37 5 3
HELIX 3 AA3 ASP A 56 HIS A 66 1 11
HELIX 4 AA4 THR A 78 PHE A 85 1 8
HELIX 5 AA5 ASP A 92 ASN A 104 1 13
HELIX 6 AA6 GLY A 117 ASP A 120 5 4
HELIX 7 AA7 ASN A 134 LYS A 155 1 22
SHEET 1 AA1 4 TRP A 39 ALA A 45 0
SHEET 2 AA1 4 LYS A 6 CYS A 12 1 N LYS A 6 O ARG A 40
SHEET 3 AA1 4 TYR A 87 CYS A 90 1 O TYR A 87 N LEU A 9
SHEET 4 AA1 4 LYS A 112 LEU A 115 1 O GLU A 114 N CYS A 90
CRYST1 32.667 54.157 100.050 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 0.030612 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018465 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009995 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
