HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-MAY-11 3S4O
TITLE PROTEIN TYROSINE PHOSPHATASE (PUTATIVE) FROM LEISHMANIA MAJOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TYROSINE PHOSPHATASE-LIKE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 4-167;
COMPND 5 EC: 3.1.3.48;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MAJOR;
SOURCE 3 ORGANISM_TAXID: 5664;
SOURCE 4 STRAIN: FRIEDLIN;
SOURCE 5 GENE: LMJF16.0230, LMJF_16_0230;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS STRUCTURAL GENOMICS, MEDICAL STRUCTURAL GENOMICS OF PATHOGENIC
KEYWDS 2 PROTOZOA, MSGPP, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR E.A.MERRITT,T.ARAKAKI,MEDICAL STRUCTURAL GENOMICS OF PATHOGENIC
AUTHOR 2 PROTOZOA (MSGPP),STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA
AUTHOR 3 CONSORTIUM (SGPP)
REVDAT 2 08-NOV-17 3S4O 1 REMARK
REVDAT 1 15-JUN-11 3S4O 0
JRNL AUTH E.A.MERRITT,T.ARAKAKI,H.NEELY,E.PHIZICKY,E.QUARTLEY,
JRNL AUTH 2 W.C.VAN VOORHIS,F.S.BUCKNER,E.FAN,F.ZUCKER,C.L.M.J.VERLINDE,
JRNL AUTH 3 W.G.J.HOL
JRNL TITL PROTEIN TYROSINE PHOSPHATASE FROM LEISHMANIA MAJOR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 45.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 15341
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 777
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) : 729
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 43
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2548
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : 0.29000
REMARK 3 B33 (A**2) : -0.16000
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): 0.409
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.254
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.187
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.730
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2649 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1826 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3593 ; 1.205 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4464 ; 1.189 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 330 ; 7.244 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 414 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2769 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 503 ; 0.003 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 6
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 1 A 16
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0260 -0.4210 -20.4360
REMARK 3 T TENSOR
REMARK 3 T11: 0.7237 T22: 0.2308
REMARK 3 T33: 0.2351 T12: 0.0015
REMARK 3 T13: -0.0566 T23: 0.1178
REMARK 3 L TENSOR
REMARK 3 L11: 23.3988 L22: 9.6606
REMARK 3 L33: 15.7948 L12: 3.2601
REMARK 3 L13: -10.7430 L23: -3.3698
REMARK 3 S TENSOR
REMARK 3 S11: -0.0028 S12: 1.1907 S13: 1.2971
REMARK 3 S21: -0.8580 S22: -0.0916 S23: -0.2517
REMARK 3 S31: -1.1790 S32: -0.1557 S33: 0.0944
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 17 A 133
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6600 -13.5630 -14.8290
REMARK 3 T TENSOR
REMARK 3 T11: 0.3270 T22: 0.1110
REMARK 3 T33: 0.0488 T12: -0.0180
REMARK 3 T13: 0.0084 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 2.3349 L22: 2.5000
REMARK 3 L33: 3.9564 L12: -0.3820
REMARK 3 L13: 0.9658 L23: -0.2513
REMARK 3 S TENSOR
REMARK 3 S11: -0.0296 S12: 0.0089 S13: 0.0650
REMARK 3 S21: 0.0288 S22: 0.0618 S23: 0.1827
REMARK 3 S31: 0.0871 S32: -0.2281 S33: -0.0321
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 134 A 163
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0760 -2.7320 -4.2940
REMARK 3 T TENSOR
REMARK 3 T11: 0.5125 T22: 0.1608
REMARK 3 T33: 0.0969 T12: -0.0531
REMARK 3 T13: -0.0345 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 6.5934 L22: 12.9379
REMARK 3 L33: 8.2075 L12: -0.8898
REMARK 3 L13: -1.6955 L23: -2.0206
REMARK 3 S TENSOR
REMARK 3 S11: -0.3658 S12: -0.1643 S13: 0.2860
REMARK 3 S21: 0.6314 S22: 0.3945 S23: 0.1029
REMARK 3 S31: -0.8485 S32: 0.4381 S33: -0.0288
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 16
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3160 2.0340 -32.5590
REMARK 3 T TENSOR
REMARK 3 T11: 0.5437 T22: 0.4040
REMARK 3 T33: 0.1943 T12: -0.0004
REMARK 3 T13: -0.0323 T23: 0.0384
REMARK 3 L TENSOR
REMARK 3 L11: 8.5953 L22: 33.2603
REMARK 3 L33: 27.2162 L12: -6.2257
REMARK 3 L13: 0.7331 L23: 13.5770
REMARK 3 S TENSOR
REMARK 3 S11: -0.0697 S12: -0.9516 S13: 0.9573
REMARK 3 S21: 1.5435 S22: 0.3831 S23: -1.3495
REMARK 3 S31: -0.8121 S32: 0.3976 S33: -0.3134
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 17 B 118
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9790 -8.1720 -36.5390
REMARK 3 T TENSOR
REMARK 3 T11: 0.4249 T22: 0.2444
REMARK 3 T33: 0.1353 T12: -0.0568
REMARK 3 T13: -0.0757 T23: 0.0895
REMARK 3 L TENSOR
REMARK 3 L11: 3.0724 L22: 3.8764
REMARK 3 L33: 5.8600 L12: -0.8118
REMARK 3 L13: 0.7901 L23: -1.3003
REMARK 3 S TENSOR
REMARK 3 S11: 0.1459 S12: 0.1717 S13: -0.2346
REMARK 3 S21: -0.4271 S22: 0.0711 S23: 0.3778
REMARK 3 S31: 0.4766 S32: -0.4424 S33: -0.2170
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 119 B 163
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6210 4.1000 -46.1380
REMARK 3 T TENSOR
REMARK 3 T11: 0.4265 T22: 0.1639
REMARK 3 T33: 0.0476 T12: 0.0681
REMARK 3 T13: 0.0038 T23: 0.0747
REMARK 3 L TENSOR
REMARK 3 L11: 3.7672 L22: 7.9655
REMARK 3 L33: 8.3616 L12: 1.2030
REMARK 3 L13: -1.7987 L23: -1.8866
REMARK 3 S TENSOR
REMARK 3 S11: -0.1047 S12: 0.0639 S13: -0.0862
REMARK 3 S21: -0.1358 S22: 0.2549 S23: 0.3253
REMARK 3 S31: 0.0440 S32: -0.2651 S33: -0.1503
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: RIDING HYDROGEN ATOMS
REMARK 4
REMARK 4 3S4O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065756.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97955, 0.97967, 0.95369
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17137
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.160
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.6
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX + PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER 25 MM HEPES PH 7.5, 500
REMARK 280 MM NACL, CRYSTALLIZATION BUFFER 100 MM SODIUM THIOSULFATE
REMARK 280 PENTAHYDRATE, 100 MM HEPES PH 7.0, 35% PEG 4000, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 293K, PH 5.0
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 21.25900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.46550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.71000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.46550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.25900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.71000
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: 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 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
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 HIS B 41 O3S EPE A 164 2.05
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 2 54.85 22.71
REMARK 500 TRP A 70 72.62 -119.97
REMARK 500 CYS A 112 -103.55 -131.51
REMARK 500 VAL A 113 -75.73 -120.55
REMARK 500 ILE A 150 110.39 77.92
REMARK 500 CYS B 112 -123.19 -105.51
REMARK 500 ILE B 150 93.20 53.66
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 MSE A 1 ASN A 2 107.82
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 THJ A 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 164
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: LMAJ002537BAD RELATED DB: TARGETDB
DBREF 3S4O A 2 163 UNP Q4QEZ7 Q4QEZ7_LEIMA 4 165
DBREF 3S4O B 2 163 UNP Q4QEZ7 Q4QEZ7_LEIMA 4 165
SEQADV 3S4O GLY A -3 UNP Q4QEZ7 EXPRESSION TAG
SEQADV 3S4O PRO A -2 UNP Q4QEZ7 EXPRESSION TAG
SEQADV 3S4O GLY A -1 UNP Q4QEZ7 EXPRESSION TAG
SEQADV 3S4O SER A 0 UNP Q4QEZ7 EXPRESSION TAG
SEQADV 3S4O MSE A 1 UNP Q4QEZ7 EXPRESSION TAG
SEQADV 3S4O GLY B -3 UNP Q4QEZ7 EXPRESSION TAG
SEQADV 3S4O PRO B -2 UNP Q4QEZ7 EXPRESSION TAG
SEQADV 3S4O GLY B -1 UNP Q4QEZ7 EXPRESSION TAG
SEQADV 3S4O SER B 0 UNP Q4QEZ7 EXPRESSION TAG
SEQADV 3S4O MSE B 1 UNP Q4QEZ7 EXPRESSION TAG
SEQRES 1 A 167 GLY PRO GLY SER MSE ASN ALA THR LEU ILE ASP CYS CYS
SEQRES 2 A 167 ASP PRO GLN LYS PRO SER ARG VAL LEU PHE HIS PHE LEU
SEQRES 3 A 167 ILE LEU ASP ALA PRO SER PRO SER ASN LEU PRO THR TYR
SEQRES 4 A 167 ILE LYS GLU LEU GLN HIS ARG GLY VAL ARG HIS LEU VAL
SEQRES 5 A 167 ARG VAL CYS GLY PRO THR TYR ASP ALA THR LEU VAL LYS
SEQRES 6 A 167 SER ARG GLY ILE ASP VAL HIS SER TRP PRO PHE ASP ASP
SEQRES 7 A 167 GLY ALA PRO PRO THR ARG ALA VAL LEU ASP SER TRP LEU
SEQRES 8 A 167 LYS LEU LEU ASP THR GLU LEU ALA ARG GLN GLN GLU ASP
SEQRES 9 A 167 PRO SER VAL PRO PRO PRO THR ILE GLY VAL HIS CYS VAL
SEQRES 10 A 167 ALA GLY LEU GLY ARG ALA PRO ILE LEU VAL ALA LEU ALA
SEQRES 11 A 167 LEU VAL GLU TYR GLY ASN VAL SER ALA LEU ASP ALA ILE
SEQRES 12 A 167 ALA LEU ILE ARG GLU LYS ARG LYS GLY ALA ILE ASN GLN
SEQRES 13 A 167 THR GLN MSE HIS TRP ILE THR LYS TYR LYS ARG
SEQRES 1 B 167 GLY PRO GLY SER MSE ASN ALA THR LEU ILE ASP CYS CYS
SEQRES 2 B 167 ASP PRO GLN LYS PRO SER ARG VAL LEU PHE HIS PHE LEU
SEQRES 3 B 167 ILE LEU ASP ALA PRO SER PRO SER ASN LEU PRO THR TYR
SEQRES 4 B 167 ILE LYS GLU LEU GLN HIS ARG GLY VAL ARG HIS LEU VAL
SEQRES 5 B 167 ARG VAL CYS GLY PRO THR TYR ASP ALA THR LEU VAL LYS
SEQRES 6 B 167 SER ARG GLY ILE ASP VAL HIS SER TRP PRO PHE ASP ASP
SEQRES 7 B 167 GLY ALA PRO PRO THR ARG ALA VAL LEU ASP SER TRP LEU
SEQRES 8 B 167 LYS LEU LEU ASP THR GLU LEU ALA ARG GLN GLN GLU ASP
SEQRES 9 B 167 PRO SER VAL PRO PRO PRO THR ILE GLY VAL HIS CYS VAL
SEQRES 10 B 167 ALA GLY LEU GLY ARG ALA PRO ILE LEU VAL ALA LEU ALA
SEQRES 11 B 167 LEU VAL GLU TYR GLY ASN VAL SER ALA LEU ASP ALA ILE
SEQRES 12 B 167 ALA LEU ILE ARG GLU LYS ARG LYS GLY ALA ILE ASN GLN
SEQRES 13 B 167 THR GLN MSE HIS TRP ILE THR LYS TYR LYS ARG
MODRES 3S4O MSE A 1 MET SELENOMETHIONINE
MODRES 3S4O MSE A 155 MET SELENOMETHIONINE
MODRES 3S4O MSE B 1 MET SELENOMETHIONINE
MODRES 3S4O MSE B 155 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 155 13
HET MSE B 1 8
HET MSE B 155 13
HET THJ A 170 5
HET EPE A 164 15
HETNAM MSE SELENOMETHIONINE
HETNAM THJ THIOSULFATE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 3 THJ O3 S2 2-
FORMUL 4 EPE C8 H18 N2 O4 S
FORMUL 5 HOH *88(H2 O)
HELIX 1 1 SER A 28 SER A 30 5 3
HELIX 2 2 ASN A 31 HIS A 41 1 11
HELIX 3 3 ALA A 57 SER A 62 1 6
HELIX 4 4 THR A 79 ASP A 100 1 22
HELIX 5 5 GLY A 117 TYR A 130 1 14
HELIX 6 6 SER A 134 ARG A 146 1 13
HELIX 7 7 ASN A 151 TYR A 161 1 11
HELIX 8 8 SER B 28 SER B 30 5 3
HELIX 9 9 ASN B 31 HIS B 41 1 11
HELIX 10 10 ALA B 57 SER B 62 1 6
HELIX 11 11 THR B 79 ASP B 100 1 22
HELIX 12 12 ARG B 118 TYR B 130 1 13
HELIX 13 13 SER B 134 ARG B 146 1 13
HELIX 14 14 ASN B 151 TYR B 161 1 11
SHEET 1 A 5 ALA A 3 CYS A 9 0
SHEET 2 A 5 VAL A 17 LEU A 24 -1 O PHE A 21 N ILE A 6
SHEET 3 A 5 THR A 107 HIS A 111 1 O ILE A 108 N HIS A 20
SHEET 4 A 5 VAL A 44 ARG A 49 1 N HIS A 46 O GLY A 109
SHEET 5 A 5 ASP A 66 SER A 69 1 O ASP A 66 N LEU A 47
SHEET 1 B 5 THR B 4 CYS B 9 0
SHEET 2 B 5 VAL B 17 LEU B 24 -1 O PHE B 21 N ILE B 6
SHEET 3 B 5 THR B 107 HIS B 111 1 O ILE B 108 N HIS B 20
SHEET 4 B 5 VAL B 44 ARG B 49 1 N HIS B 46 O GLY B 109
SHEET 5 B 5 ASP B 66 SER B 69 1 O ASP B 66 N LEU B 47
SSBOND 1 CYS A 51 CYS A 112 1555 1555 2.04
SSBOND 2 CYS B 51 CYS B 112 1555 1555 2.06
LINK C MSE A 1 N ASN A 2 1555 1555 1.33
LINK C GLN A 154 N MSE A 155 1555 1555 1.33
LINK C MSE A 155 N HIS A 156 1555 1555 1.32
LINK C MSE B 1 N ASN B 2 1555 1555 1.33
LINK C GLN B 154 N MSE B 155 1555 1555 1.33
LINK C MSE B 155 N HIS B 156 1555 1555 1.33
SITE 1 AC1 9 ASP A 74 CYS A 112 VAL A 113 ALA A 114
SITE 2 AC1 9 GLY A 115 LEU A 116 GLY A 117 ARG A 118
SITE 3 AC1 9 ALA A 119
SITE 1 AC2 20 HIS A 41 ARG A 42 GLY A 43 ARG A 45
SITE 2 AC2 20 ARG A 96 PRO A 104 PRO A 105 PRO A 106
SITE 3 AC2 20 THR A 107 HOH A 190 HOH A 193 HOH A 202
SITE 4 AC2 20 HIS B 41 ARG B 42 GLY B 43 ARG B 45
SITE 5 AC2 20 ARG B 96 PRO B 105 PRO B 106 THR B 107
CRYST1 42.518 69.420 118.931 90.00 90.00 90.00 P 21 21 21 8
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 0.023519 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014405 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008408 0.00000
HETATM 1 N MSE A 1 3.672 -5.228 -12.796 1.00 94.88 N
ANISOU 1 N MSE A 1 8052 15695 12303 1411 69 -229 N
HETATM 2 CA MSE A 1 5.012 -5.830 -12.543 1.00 87.70 C
ANISOU 2 CA MSE A 1 8190 13933 11199 1002 198 -544 C
HETATM 3 C MSE A 1 6.106 -4.795 -12.314 1.00 80.78 C
ANISOU 3 C MSE A 1 8142 12339 10209 1609 175 -435 C
HETATM 4 O MSE A 1 6.754 -4.333 -13.267 1.00 78.87 O
ANISOU 4 O MSE A 1 8174 12001 9790 1687 -249 -311 O
HETATM 5 CB MSE A 1 5.419 -6.752 -13.702 1.00 88.70 C
ANISOU 5 CB MSE A 1 8382 14234 11085 160 -157 -838 C
HETATM 6 CG MSE A 1 6.306 -7.913 -13.294 1.00 85.65 C
ANISOU 6 CG MSE A 1 8677 13077 10789 -415 277 -1140 C
HETATM 7 SE MSE A 1 7.624 -8.405 -14.680 1.00 85.10 SE
ANISOU 7 SE MSE A 1 9264 12664 10404 -953 -13 -1478 SE
HETATM 8 CE MSE A 1 7.471 -10.334 -14.505 1.00 87.87 C
ANISOU 8 CE MSE A 1 9634 12495 11256 -2042 776 -2017 C
(ATOM LINES ARE NOT SHOWN.)
END