HEADER PEPTIDE BINDING PROTEIN 15-AUG-14 4UWX
TITLE STRUCTURE OF LIPRIN-ALPHA3 IN COMPLEX WITH MDIA1 DIAPHANOUS-
TITLE 2 INHIBITORY DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DIAPHANOUS HOMOLOG 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DIAPHANOUS-INHIBITORY DOMAIN, RESIDUES 135-369;
COMPND 5 SYNONYM: DIAPHANOUS-RELATED FORMIN-1, DRF1, P140MDIA, MDIA1, MDIA1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LIPRIN-ALPHA-3;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: COILED-COIL DOMAIN;
COMPND 11 SYNONYM: PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE F POLYPEPTIDE-IN
COMPND 12 TERACTING PROTEIN ALPHA-3, PTPRF-INTERACTING PROTEIN ALPHA-3, LIPR
COMPND 13 IN-ALPHA3;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 9 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 10 ORGANISM_TAXID: 10090;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS PEPTIDE-BINDING PROTEIN, ACTIN POLYMERISATION, RHOGNBPS, SYNAPE
KEYWDS 2 MATURATION, CELL MOTILITY, FH1, FH2 DOMAIN, ACTIN-NUCLEATION FACTOR
KEYWDS 3 - DIAPHANOUS-RELATED FORMIN, PEPTIDE BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BRENIG,S.DE BOOR,P.KNYPHAUSEN,N.KUHLMANN,S.WROBLOWSKI,L.BALDUS,
AUTHOR 2 L.SCISLOWSKI,O.ARTZ,P.TRAUSCHIES,U.BAUMANN,I.NEUNDORF,M.LAMMERS
REVDAT 4 10-JAN-24 4UWX 1 REMARK LINK
REVDAT 3 17-JUN-15 4UWX 1 JRNL
REVDAT 2 13-MAY-15 4UWX 1 JRNL
REVDAT 1 06-MAY-15 4UWX 0
JRNL AUTH J.BRENIG,S.DE BOOR,P.KNYPHAUSEN,N.KUHLMANN,S.WROBLOWSKI,
JRNL AUTH 2 L.BALDUS,L.SCISLOWSKI,O.ARTZ,P.TRAUSCHIES,U.BAUMANN,
JRNL AUTH 3 I.NEUNDORF,M.LAMMERS
JRNL TITL STRUCTURAL AND BIOCHEMICAL BASIS FOR THE INHIBITORY EFFECT
JRNL TITL 2 OF LIPRIN-ALPHA3 ON MOUSE DIAPHANOUS 1 (MDIA1) FUNCTION.
JRNL REF J.BIOL.CHEM. V. 290 14314 2015
JRNL REFN ISSN 0021-9258
JRNL PMID 25911102
JRNL DOI 10.1074/JBC.M114.621946
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 75028
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3777
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5223
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.3210
REMARK 3 BIN FREE R VALUE SET COUNT : 275
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3926
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 393
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06400
REMARK 3 B22 (A**2) : 2.16000
REMARK 3 B33 (A**2) : -2.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.13600
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.084
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.093
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3985 ; 0.022 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3965 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5354 ; 2.005 ; 1.997
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9117 ; 1.316 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 489 ; 5.220 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 192 ;34.109 ;24.740
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 782 ;13.749 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;19.444 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 617 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4428 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 850 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1439 ; 0.308 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 61 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2037 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 59 ; 0.195 ; 0.200
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): 3985 ; 2.967 ; 1.891
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3965 ; 0.751 ; 1.975
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5354 ; 4.505 ; 2.759
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 516 ; 8.871 ; 6.067
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3395 ; 8.458 ;18.692
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 : 4
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 131 A 368
REMARK 3 ORIGIN FOR THE GROUP (A): 119.4759 -2.1112 136.3159
REMARK 3 T TENSOR
REMARK 3 T11: 0.0739 T22: 0.0503
REMARK 3 T33: 0.0960 T12: 0.0165
REMARK 3 T13: -0.0030 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.3261 L22: 0.1150
REMARK 3 L33: 0.5068 L12: -0.0494
REMARK 3 L13: -0.3266 L23: 0.1858
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: -0.0359 S13: 0.0021
REMARK 3 S21: -0.0007 S22: 0.0098 S23: -0.0154
REMARK 3 S31: 0.0013 S32: 0.0249 S33: -0.0133
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 : B 135 B 369
REMARK 3 ORIGIN FOR THE GROUP (A): 86.3814 3.8452 127.5499
REMARK 3 T TENSOR
REMARK 3 T11: 0.0744 T22: 0.0427
REMARK 3 T33: 0.0984 T12: 0.0121
REMARK 3 T13: 0.0044 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.3282 L22: 0.0217
REMARK 3 L33: 0.5409 L12: -0.0178
REMARK 3 L13: 0.3739 L23: 0.0034
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: -0.0234 S13: -0.0192
REMARK 3 S21: -0.0022 S22: 0.0087 S23: 0.0080
REMARK 3 S31: 0.0157 S32: 0.0076 S33: -0.0080
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 : C 567 C 581
REMARK 3 ORIGIN FOR THE GROUP (A): 124.8173 11.6560 148.5679
REMARK 3 T TENSOR
REMARK 3 T11: 0.0794 T22: 0.1110
REMARK 3 T33: 0.1457 T12: -0.0635
REMARK 3 T13: 0.0440 T23: -0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 2.9638 L22: 4.6836
REMARK 3 L33: 5.7423 L12: -1.0686
REMARK 3 L13: -4.0612 L23: 1.3529
REMARK 3 S TENSOR
REMARK 3 S11: 0.1839 S12: -0.2995 S13: 0.0995
REMARK 3 S21: -0.0214 S22: 0.1066 S23: -0.0010
REMARK 3 S31: -0.3603 S32: 0.4948 S33: -0.2904
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 : D 567 D 581
REMARK 3 ORIGIN FOR THE GROUP (A): 81.3074 -9.8234 116.0037
REMARK 3 T TENSOR
REMARK 3 T11: 0.1297 T22: 0.0107
REMARK 3 T33: 0.1269 T12: 0.0209
REMARK 3 T13: -0.0014 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 4.8297 L22: 1.0115
REMARK 3 L33: 3.4735 L12: 0.2248
REMARK 3 L13: 2.4264 L23: -0.0010
REMARK 3 S TENSOR
REMARK 3 S11: 0.0906 S12: 0.1354 S13: -0.0339
REMARK 3 S21: 0.0649 S22: -0.0471 S23: -0.0298
REMARK 3 S31: 0.2419 S32: 0.1019 S33: -0.0434
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PLUS 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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4UWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-AUG-14.
REMARK 100 THE DEPOSITION ID IS D_1290060651.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : BARTELS SI (111)
REMARK 200 OPTICS : MIRRORS TOROIDAL FOCUSSING
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : TRUNCATE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75030
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 105.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.130
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.24
REMARK 200 R MERGE FOR SHELL (I) : 0.73000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.330
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: PDB ENTRY 1Z2C
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NACL, 0.1 M TRIS/HCL PH 8.0, 20%
REMARK 280 PEG6000
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 60.54500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.69050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.54500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.69050
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: 1440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: 1510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 GLU A 194
REMARK 465 GLU A 195
REMARK 465 THR A 196
REMARK 465 SER A 197
REMARK 465 GLY A 369
REMARK 465 GLY B 131
REMARK 465 SER B 132
REMARK 465 GLU B 133
REMARK 465 PHE B 134
REMARK 465 GLU B 194
REMARK 465 GLU B 195
REMARK 465 THR B 196
REMARK 465 SER B 197
REMARK 465 GLY B 198
REMARK 465 LEU C 582
REMARK 465 GLN C 583
REMARK 465 ALA C 584
REMARK 465 GLY C 585
REMARK 465 SER C 586
REMARK 465 PRO C 587
REMARK 465 GLN D 583
REMARK 465 ALA D 584
REMARK 465 GLY D 585
REMARK 465 SER D 586
REMARK 465 PRO D 587
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 2060 O HOH A 2061 0.90
REMARK 500 O HOH A 2050 O HOH A 2051 0.95
REMARK 500 O HOH A 2121 O HOH A 2122 0.99
REMARK 500 O HOH B 2122 O HOH B 2155 1.12
REMARK 500 O HOH B 2140 O HOH B 2143 1.18
REMARK 500 O HOH B 2156 O HOH B 2157 1.53
REMARK 500 CB SER A 181 O HOH A 2047 1.55
REMARK 500 SD MET B 266 O HOH B 2110 1.87
REMARK 500 SD MET A 266 O HOH A 2120 1.91
REMARK 500 O3 144 B 1371 O HOH A 2160 2.09
REMARK 500 O HOH A 2017 O HOH A 2019 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2025 O HOH B 2114 3545 1.80
REMARK 500 O HOH A 2023 O HOH B 2125 3545 1.92
REMARK 500 O HOH A 2176 O HOH B 2008 2758 2.07
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 GLY A 131 C GLY A 131 O 0.125
REMARK 500 MET A 216 SD MET A 216 CE -0.500
REMARK 500 ARG B 160 CD ARG B 160 NE -0.124
REMARK 500 GLU B 318 CG GLU B 318 CD 0.092
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 A 160 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 MET A 216 CG - SD - CE ANGL. DEV. = -17.5 DEGREES
REMARK 500 ARG A 269 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 160 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG B 160 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 237 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 326 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 331 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG B 331 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG C 572 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG C 572 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG D 572 NE - CZ - NH1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ARG D 572 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 MET D 576 CG - SD - CE ANGL. DEV. = -10.1 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 ASP A 149 -129.01 58.12
REMARK 500 GLU A 192 49.41 -100.64
REMARK 500 ASP B 149 -134.85 58.81
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 B2038 DISTANCE = 6.44 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A1369 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 142 OE2
REMARK 620 2 HIS A 151 NE2 93.8
REMARK 620 3 144 A1370 O2 91.9 89.1
REMARK 620 4 144 A1370 O3 89.9 173.3 85.2
REMARK 620 5 144 A1370 O4 168.0 96.1 81.6 79.6
REMARK 620 6 HIS B 324 ND1 88.6 97.8 173.0 87.8 96.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B1370 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 324 ND1
REMARK 620 2 GLU B 142 OE2 93.6
REMARK 620 3 HIS B 151 NE2 97.2 92.4
REMARK 620 4 144 B1371 O4 95.9 169.4 91.1
REMARK 620 5 144 B1371 O3 68.9 105.4 157.7 73.8
REMARK 620 6 144 B1371 C3 100.2 93.1 161.4 80.6 33.2
REMARK 620 7 144 B1371 O2 171.5 87.0 91.2 83.0 102.8 71.4
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1369
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 144 A 1370
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 1370
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 144 B 1371
DBREF 4UWX A 135 369 UNP O08808 DIAP1_MOUSE 135 369
DBREF 4UWX B 135 369 UNP O08808 DIAP1_MOUSE 135 369
DBREF 4UWX C 567 587 UNP P60469 LIPA3_MOUSE 567 587
DBREF 4UWX D 567 587 UNP P60469 LIPA3_MOUSE 567 587
SEQADV 4UWX GLY A 131 UNP O08808 EXPRESSION TAG
SEQADV 4UWX SER A 132 UNP O08808 EXPRESSION TAG
SEQADV 4UWX GLU A 133 UNP O08808 EXPRESSION TAG
SEQADV 4UWX PHE A 134 UNP O08808 EXPRESSION TAG
SEQADV 4UWX GLY B 131 UNP O08808 EXPRESSION TAG
SEQADV 4UWX SER B 132 UNP O08808 EXPRESSION TAG
SEQADV 4UWX GLU B 133 UNP O08808 EXPRESSION TAG
SEQADV 4UWX PHE B 134 UNP O08808 EXPRESSION TAG
SEQRES 1 A 239 GLY SER GLU PHE SER ALA MET MET TYR ILE GLN GLU LEU
SEQRES 2 A 239 ARG SER GLY LEU ARG ASP MET HIS LEU LEU SER CYS LEU
SEQRES 3 A 239 GLU SER LEU ARG VAL SER LEU ASN ASN ASN PRO VAL SER
SEQRES 4 A 239 TRP VAL GLN THR PHE GLY ALA GLU GLY LEU ALA SER LEU
SEQRES 5 A 239 LEU ASP ILE LEU LYS ARG LEU HIS ASP GLU LYS GLU GLU
SEQRES 6 A 239 THR SER GLY ASN TYR ASP SER ARG ASN GLN HIS GLU ILE
SEQRES 7 A 239 ILE ARG CYS LEU LYS ALA PHE MET ASN ASN LYS PHE GLY
SEQRES 8 A 239 ILE LYS THR MET LEU GLU THR GLU GLU GLY ILE LEU LEU
SEQRES 9 A 239 LEU VAL ARG ALA MET ASP PRO ALA VAL PRO ASN MET MET
SEQRES 10 A 239 ILE ASP ALA ALA LYS LEU LEU SER ALA LEU CYS ILE LEU
SEQRES 11 A 239 PRO GLN PRO GLU ASP MET ASN GLU ARG VAL LEU GLU ALA
SEQRES 12 A 239 MET THR GLU ARG ALA GLU MET ASP GLU VAL GLU ARG PHE
SEQRES 13 A 239 GLN PRO LEU LEU ASP GLY LEU LYS SER GLY THR SER ILE
SEQRES 14 A 239 ALA LEU LYS VAL GLY CYS LEU GLN LEU ILE ASN ALA LEU
SEQRES 15 A 239 ILE THR PRO ALA GLU GLU LEU ASP PHE ARG VAL HIS ILE
SEQRES 16 A 239 ARG SER GLU LEU MET ARG LEU GLY LEU HIS GLN VAL LEU
SEQRES 17 A 239 GLN GLU LEU ARG GLU ILE GLU ASN GLU ASP MET LYS VAL
SEQRES 18 A 239 GLN LEU CYS VAL PHE ASP GLU GLN GLY ASP GLU ASP PHE
SEQRES 19 A 239 PHE ASP LEU LYS GLY
SEQRES 1 B 239 GLY SER GLU PHE SER ALA MET MET TYR ILE GLN GLU LEU
SEQRES 2 B 239 ARG SER GLY LEU ARG ASP MET HIS LEU LEU SER CYS LEU
SEQRES 3 B 239 GLU SER LEU ARG VAL SER LEU ASN ASN ASN PRO VAL SER
SEQRES 4 B 239 TRP VAL GLN THR PHE GLY ALA GLU GLY LEU ALA SER LEU
SEQRES 5 B 239 LEU ASP ILE LEU LYS ARG LEU HIS ASP GLU LYS GLU GLU
SEQRES 6 B 239 THR SER GLY ASN TYR ASP SER ARG ASN GLN HIS GLU ILE
SEQRES 7 B 239 ILE ARG CYS LEU LYS ALA PHE MET ASN ASN LYS PHE GLY
SEQRES 8 B 239 ILE LYS THR MET LEU GLU THR GLU GLU GLY ILE LEU LEU
SEQRES 9 B 239 LEU VAL ARG ALA MET ASP PRO ALA VAL PRO ASN MET MET
SEQRES 10 B 239 ILE ASP ALA ALA LYS LEU LEU SER ALA LEU CYS ILE LEU
SEQRES 11 B 239 PRO GLN PRO GLU ASP MET ASN GLU ARG VAL LEU GLU ALA
SEQRES 12 B 239 MET THR GLU ARG ALA GLU MET ASP GLU VAL GLU ARG PHE
SEQRES 13 B 239 GLN PRO LEU LEU ASP GLY LEU LYS SER GLY THR SER ILE
SEQRES 14 B 239 ALA LEU LYS VAL GLY CYS LEU GLN LEU ILE ASN ALA LEU
SEQRES 15 B 239 ILE THR PRO ALA GLU GLU LEU ASP PHE ARG VAL HIS ILE
SEQRES 16 B 239 ARG SER GLU LEU MET ARG LEU GLY LEU HIS GLN VAL LEU
SEQRES 17 B 239 GLN GLU LEU ARG GLU ILE GLU ASN GLU ASP MET LYS VAL
SEQRES 18 B 239 GLN LEU CYS VAL PHE ASP GLU GLN GLY ASP GLU ASP PHE
SEQRES 19 B 239 PHE ASP LEU LYS GLY
SEQRES 1 C 21 THR PRO ARG SER ALA ARG LEU GLU ARG MET ALA GLN ALA
SEQRES 2 C 21 LEU ALA LEU GLN ALA GLY SER PRO
SEQRES 1 D 21 THR PRO ARG SER ALA ARG LEU GLU ARG MET ALA GLN ALA
SEQRES 2 D 21 LEU ALA LEU GLN ALA GLY SER PRO
HET NI A1369 1
HET 144 A1370 8
HET NI B1370 1
HET 144 B1371 8
HETNAM NI NICKEL (II) ION
HETNAM 144 TRIS-HYDROXYMETHYL-METHYL-AMMONIUM
FORMUL 5 NI 2(NI 2+)
FORMUL 6 144 2(C4 H12 N O3 1+)
FORMUL 9 HOH *393(H2 O)
HELIX 1 1 SER A 132 ARG A 144 1 13
HELIX 2 2 ARG A 148 ASN A 166 1 19
HELIX 3 3 PRO A 167 GLU A 192 1 26
HELIX 4 4 TYR A 200 MET A 216 1 17
HELIX 5 5 ASN A 218 GLU A 227 1 10
HELIX 6 6 GLU A 230 ALA A 238 1 9
HELIX 7 7 VAL A 243 ILE A 259 1 17
HELIX 8 8 ASP A 265 GLU A 282 1 18
HELIX 9 9 PHE A 286 LEU A 293 1 8
HELIX 10 10 SER A 298 THR A 314 1 17
HELIX 11 11 GLU A 318 GLY A 333 1 16
HELIX 12 12 GLY A 333 GLU A 343 1 11
HELIX 13 13 ASN A 346 LYS A 368 1 23
HELIX 14 14 SER B 135 SER B 145 1 11
HELIX 15 15 ARG B 148 ASN B 166 1 19
HELIX 16 16 PRO B 167 GLU B 192 1 26
HELIX 17 17 TYR B 200 MET B 216 1 17
HELIX 18 18 ASN B 218 THR B 228 1 11
HELIX 19 19 GLU B 230 ALA B 238 1 9
HELIX 20 20 VAL B 243 ILE B 259 1 17
HELIX 21 21 ASP B 265 GLU B 282 1 18
HELIX 22 22 PHE B 286 LEU B 293 1 8
HELIX 23 23 SER B 298 THR B 314 1 17
HELIX 24 24 GLU B 318 LEU B 332 1 15
HELIX 25 25 GLY B 333 ARG B 342 1 10
HELIX 26 26 ASN B 346 GLY B 369 1 24
HELIX 27 27 THR C 567 ALA C 581 1 15
HELIX 28 28 THR D 567 LEU D 582 1 16
LINK OE2 GLU A 142 NI NI A1369 1555 1555 2.10
LINK NE2 HIS A 151 NI NI A1369 1555 1555 2.19
LINK ND1 HIS A 324 NI NI B1370 1555 1555 2.17
LINK NI NI A1369 O2 144 A1370 1555 1555 2.18
LINK NI NI A1369 O3 144 A1370 1555 1555 2.14
LINK NI NI A1369 O4 144 A1370 1555 1555 2.18
LINK NI NI A1369 ND1 HIS B 324 1555 3545 2.24
LINK OE2 GLU B 142 NI NI B1370 1555 1555 2.05
LINK NE2 HIS B 151 NI NI B1370 1555 1555 2.11
LINK NI NI B1370 O4 144 B1371 1555 1555 2.23
LINK NI NI B1370 O3 144 B1371 1555 1555 2.47
LINK NI NI B1370 C3 144 B1371 1555 1555 2.28
LINK NI NI B1370 O2 144 B1371 1555 1555 2.24
CISPEP 1 GLY A 131 SER A 132 0 4.43
CISPEP 2 GLN A 262 PRO A 263 0 -9.94
CISPEP 3 GLN B 262 PRO B 263 0 -10.54
SITE 1 AC1 4 GLU A 142 HIS A 151 144 A1370 HIS B 324
SITE 1 AC2 5 GLU A 142 HIS A 151 NI A1369 HOH A2020
SITE 2 AC2 5 HIS B 324
SITE 1 AC3 4 HIS A 324 GLU B 142 HIS B 151 144 B1371
SITE 1 AC4 7 HIS A 324 ARG A 331 HOH A2157 HOH A2160
SITE 2 AC4 7 GLU B 142 HIS B 151 NI B1370
CRYST1 121.090 49.381 106.370 90.00 97.86 90.00 C 1 2 1 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 0.008258 0.000000 0.001140 0.00000
SCALE2 0.000000 0.020251 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009490 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
