HEADER STRUCTURAL PROTEIN 28-NOV-11 3UUL
TITLE CRYSTAL STRUCTURE OF FIRST N-TERMINAL UTROPHIN SPECTRIN REPEAT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UTROPHIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SPECTRIN REPEAT, RESIDUES 308-425;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 TISSUE: MUSCLE;
SOURCE 6 GENE: UTRN;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPROEXHTB
KEYWDS SPECTRIN REPEAT, STRUCTURAL PROTEIN, UTROPHIN, CYTOSKELETAL, TRIPLE
KEYWDS 2 HELICAL BUNDLE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MUTHU,K.A.RICHARDSON,A.J.SUTHERLAND-SMITH
REVDAT 2 25-DEC-19 3UUL 1 REMARK
REVDAT 1 19-SEP-12 3UUL 0
JRNL AUTH M.MUTHU,K.A.RICHARDSON,A.J.SUTHERLAND-SMITH
JRNL TITL THE CRYSTAL STRUCTURES OF DYSTROPHIN AND UTROPHIN SPECTRIN
JRNL TITL 2 REPEATS: IMPLICATIONS FOR DOMAIN BOUNDARIES
JRNL REF PLOS ONE V. 7 40066 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 22911693
JRNL DOI 10.1371/JOURNAL.PONE.0040066
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0101
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 16320
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 876
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1060
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 16320
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1851
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 206
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.64
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.11000
REMARK 3 B22 (A**2) : 3.65000
REMARK 3 B33 (A**2) : -2.55000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.168
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.141
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.606
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1878 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1202 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2540 ; 1.236 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2957 ; 0.954 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 234 ; 4.588 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;35.086 ;26.604
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 346 ;13.924 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;17.949 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 290 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2124 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 344 ; 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): 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 8
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 311 A 333 4
REMARK 3 1 B 311 B 333 4
REMARK 3 2 A 343 A 357 4
REMARK 3 2 B 343 B 357 4
REMARK 3 3 A 366 A 370 4
REMARK 3 3 B 366 B 370 4
REMARK 3 4 A 372 A 377 4
REMARK 3 4 B 372 B 377 4
REMARK 3 5 A 383 A 401 4
REMARK 3 5 B 383 B 401 4
REMARK 3 6 A 406 A 410 4
REMARK 3 6 B 406 B 410 4
REMARK 3 7 A 412 A 423 4
REMARK 3 7 B 412 B 423 4
REMARK 3 8 A 358 A 365 5
REMARK 3 8 B 358 B 365 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1165 ; 0.290 ; 0.800
REMARK 3 LOOSE POSITIONAL 1 A (A): 44 ; 0.730 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1165 ; 2.040 ;10.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 44 ; 1.810 ;10.000
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 310 A 424
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9353 5.1828 -22.6522
REMARK 3 T TENSOR
REMARK 3 T11: 0.0382 T22: 0.0080
REMARK 3 T33: 0.0519 T12: -0.0152
REMARK 3 T13: 0.0067 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.2507 L22: 0.0569
REMARK 3 L33: 2.3348 L12: -0.1188
REMARK 3 L13: -0.4328 L23: 0.1944
REMARK 3 S TENSOR
REMARK 3 S11: -0.0146 S12: -0.0046 S13: -0.0469
REMARK 3 S21: 0.0088 S22: 0.0004 S23: 0.0268
REMARK 3 S31: -0.1237 S32: 0.1009 S33: 0.0142
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 308 B 424
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6485 3.9545 -34.6668
REMARK 3 T TENSOR
REMARK 3 T11: 0.0272 T22: 0.0229
REMARK 3 T33: 0.0462 T12: 0.0220
REMARK 3 T13: 0.0041 T23: 0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 0.2920 L22: 0.1943
REMARK 3 L33: 1.7892 L12: 0.2381
REMARK 3 L13: -0.4863 L23: -0.3855
REMARK 3 S TENSOR
REMARK 3 S11: -0.0036 S12: 0.0010 S13: -0.0226
REMARK 3 S21: -0.0035 S22: 0.0020 S23: -0.0189
REMARK 3 S31: -0.0697 S32: -0.0359 S33: 0.0016
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3UUL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000069227.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : OSMIC BLUE CONFOCAL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16320
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 35.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.40600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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: 1S35
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4000, 0.1M TRIS HCL, 0.2M
REMARK 280 MAGNESIUM CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 21.50000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.72500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.33000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.72500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.33000
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 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 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 ASP A 308
REMARK 465 MET A 309
REMARK 465 LYS A 425
REMARK 465 LYS B 425
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 421 CG CD OE1 OE2
REMARK 470 LYS A 424 CG CD CE NZ
REMARK 470 ASP B 308 CG OD1 OD2
REMARK 470 MET B 309 CG SD CE
REMARK 470 GLN B 335 CG CD OE1 NE2
REMARK 470 ASP B 340 CG OD1 OD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU B 385 CD OE1 OE2
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 CB ASP B 308 CB ALA B 372 1.91
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 MET B 309 -57.02 -23.89
REMARK 500 GLU B 334 34.42 -84.77
REMARK 500 ILE B 338 92.70 -68.93
REMARK 500 ASP B 340 30.57 -94.78
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 382 O
REMARK 620 2 HOH A 198 O 88.2
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UUM RELATED DB: PDB
REMARK 900 RELATED ID: 3UUN RELATED DB: PDB
DBREF 3UUL A 308 425 UNP O55147 O55147_RAT 308 425
DBREF 3UUL B 308 425 UNP O55147 O55147_RAT 308 425
SEQRES 1 A 118 ASP MET ASP LEU ASP SER TYR GLN ILE ALA LEU GLU GLU
SEQRES 2 A 118 VAL LEU THR TRP LEU LEU SER ALA GLU ASP THR PHE GLN
SEQRES 3 A 118 GLU GLN ASP ASP ILE SER ASP ASP VAL GLU ASP VAL LYS
SEQRES 4 A 118 GLU GLN PHE ALA THR HIS GLU THR PHE MET MET GLU LEU
SEQRES 5 A 118 SER ALA HIS GLN SER SER VAL GLY SER VAL LEU GLN ALA
SEQRES 6 A 118 GLY ASN GLN LEU MET THR GLN GLY THR LEU SER ASP GLU
SEQRES 7 A 118 GLU GLU PHE GLU ILE GLN GLU GLN MET THR LEU LEU ASN
SEQRES 8 A 118 ALA ARG TRP GLU ALA LEU ARG VAL GLU SER MET GLU ARG
SEQRES 9 A 118 GLN SER ARG LEU HIS ASP ALA LEU MET GLU LEU GLN LYS
SEQRES 10 A 118 LYS
SEQRES 1 B 118 ASP MET ASP LEU ASP SER TYR GLN ILE ALA LEU GLU GLU
SEQRES 2 B 118 VAL LEU THR TRP LEU LEU SER ALA GLU ASP THR PHE GLN
SEQRES 3 B 118 GLU GLN ASP ASP ILE SER ASP ASP VAL GLU ASP VAL LYS
SEQRES 4 B 118 GLU GLN PHE ALA THR HIS GLU THR PHE MET MET GLU LEU
SEQRES 5 B 118 SER ALA HIS GLN SER SER VAL GLY SER VAL LEU GLN ALA
SEQRES 6 B 118 GLY ASN GLN LEU MET THR GLN GLY THR LEU SER ASP GLU
SEQRES 7 B 118 GLU GLU PHE GLU ILE GLN GLU GLN MET THR LEU LEU ASN
SEQRES 8 B 118 ALA ARG TRP GLU ALA LEU ARG VAL GLU SER MET GLU ARG
SEQRES 9 B 118 GLN SER ARG LEU HIS ASP ALA LEU MET GLU LEU GLN LYS
SEQRES 10 B 118 LYS
HET MG A 1 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG MG 2+
FORMUL 4 HOH *206(H2 O)
HELIX 1 1 ASP A 310 GLU A 334 1 25
HELIX 2 2 ASP A 341 GLN A 379 1 39
HELIX 3 3 SER A 383 LYS A 424 1 42
HELIX 4 4 ASP B 310 GLU B 334 1 25
HELIX 5 5 ASP B 341 GLY B 380 1 40
HELIX 6 6 SER B 383 LYS B 424 1 42
LINK O LEU A 382 MG MG A 1 1555 1555 2.46
LINK MG MG A 1 O HOH A 198 1555 1555 2.30
SITE 1 AC1 4 HOH A 198 LEU A 382 ASP A 384 GLU A 387
CRYST1 43.000 58.660 91.450 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 0.023256 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017047 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010935 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.993654 -0.112395 -0.004367 -22.06544 1
MTRIX2 2 -0.112432 0.993614 0.009542 -0.92674 1
MTRIX3 2 0.003267 0.009973 -0.999945 -57.13296 1
(ATOM LINES ARE NOT SHOWN.)
END
