HEADER STRUCTURAL PROTEIN 28-NOV-11 3UUM
TITLE CRYSTAL STRUCTURE OF N-TERMINAL FIRST SPECTRIN REPEAT OF UTROPHIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UTROPHIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL FIRST SPECTRIN REPEAT, RESIDUES 308-430;
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 GENE: UTRN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEXHTB
KEYWDS TRIPLE HELICAL, STRUCTURAL STABILITY, CYTOSKELETAL, STRUCTURAL
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MUTHU,K.A.RICHARDSON,A.J.SUTHERLAND-SMITH
REVDAT 1 19-SEP-12 3UUM 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. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0109
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 14759
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 774
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 966
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.3680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1969
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 51
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28000
REMARK 3 B22 (A**2) : 3.22000
REMARK 3 B33 (A**2) : -3.50000
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): 0.204
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.147
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.176
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2014 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1304 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2721 ; 1.590 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3218 ; 1.021 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 251 ; 5.781 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 117 ;35.687 ;26.923
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 387 ;15.034 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;18.277 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 307 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2273 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 359 ; 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 312 A 334 5
REMARK 3 1 B 312 B 334 5
REMARK 3 2 A 342 A 430 5
REMARK 3 2 B 342 B 430 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 667 ; 0.260 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 833 ; 0.630 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 667 ; 3.970 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 833 ; 4.370 ;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 : B 308 B 430
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8548 -4.3201 -35.5972
REMARK 3 T TENSOR
REMARK 3 T11: 0.0635 T22: 0.0528
REMARK 3 T33: 0.1272 T12: 0.0084
REMARK 3 T13: -0.0062 T23: -0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 0.1666 L22: 0.3647
REMARK 3 L33: 4.0643 L12: 0.2374
REMARK 3 L13: 0.6636 L23: 0.8007
REMARK 3 S TENSOR
REMARK 3 S11: -0.0085 S12: -0.0269 S13: 0.0532
REMARK 3 S21: -0.0499 S22: -0.0472 S23: 0.0677
REMARK 3 S31: 0.1488 S32: 0.0872 S33: 0.0556
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 309 A 430
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8605 -5.8059 -19.6680
REMARK 3 T TENSOR
REMARK 3 T11: 0.1085 T22: 0.0183
REMARK 3 T33: 0.1296 T12: 0.0002
REMARK 3 T13: -0.0088 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.4892 L22: 0.1459
REMARK 3 L33: 4.5353 L12: -0.2307
REMARK 3 L13: 0.8864 L23: -0.5459
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S12: 0.0868 S13: 0.0048
REMARK 3 S21: 0.0587 S22: -0.0281 S23: -0.0039
REMARK 3 S31: 0.1396 S32: 0.0819 S33: 0.0506
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 3UUM 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 RCSB ID CODE IS RCSB069228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.5
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 : 14759
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 35.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.300
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : 0.72000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.14100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.1M NA CACODYLATE, 0.2M
REMARK 280 MAGNESIUM ACETATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294.15K
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 21.37000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.63995
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.00995
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.63995
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.37000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.00995
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 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 MET A 309 CG SD CE
REMARK 470 LEU A 430 CG CD1 CD2
REMARK 470 ASP B 308 CG OD1 OD2
REMARK 470 MET B 309 CG SD CE
REMARK 470 LEU B 430 CG CD1 CD2
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 MG MG A 1 O HOH A 27 1.53
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 VAL A 321 CB VAL A 321 CG1 0.130
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 B 405 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 405 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 414 NE - CZ - NH1 ANGL. DEV. = 3.1 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 MET B 309 15.46 57.90
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 MET B 309 ASP B 310 145.83
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 HOH A 24 O
REMARK 620 2 HOH A 26 O 121.6
REMARK 620 3 HOH A 25 O 74.1 116.5
REMARK 620 N 1 2
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: 3UUL RELATED DB: PDB
REMARK 900 RELATED ID: 3UUN RELATED DB: PDB
DBREF 3UUM A 308 430 UNP O55147 O55147_RAT 308 430
DBREF 3UUM B 308 430 UNP O55147 O55147_RAT 308 430
SEQRES 1 A 123 ASP MET ASP LEU ASP SER TYR GLN ILE ALA LEU GLU GLU
SEQRES 2 A 123 VAL LEU THR TRP LEU LEU SER ALA GLU ASP THR PHE GLN
SEQRES 3 A 123 GLU GLN ASP ASP ILE SER ASP ASP VAL GLU ASP VAL LYS
SEQRES 4 A 123 GLU GLN PHE ALA THR HIS GLU THR PHE MET MET GLU LEU
SEQRES 5 A 123 SER ALA HIS GLN SER SER VAL GLY SER VAL LEU GLN ALA
SEQRES 6 A 123 GLY ASN GLN LEU MET THR GLN GLY THR LEU SER ASP GLU
SEQRES 7 A 123 GLU GLU PHE GLU ILE GLN GLU GLN MET THR LEU LEU ASN
SEQRES 8 A 123 ALA ARG TRP GLU ALA LEU ARG VAL GLU SER MET GLU ARG
SEQRES 9 A 123 GLN SER ARG LEU HIS ASP ALA LEU MET GLU LEU GLN LYS
SEQRES 10 A 123 LYS GLN LEU GLN GLN LEU
SEQRES 1 B 123 ASP MET ASP LEU ASP SER TYR GLN ILE ALA LEU GLU GLU
SEQRES 2 B 123 VAL LEU THR TRP LEU LEU SER ALA GLU ASP THR PHE GLN
SEQRES 3 B 123 GLU GLN ASP ASP ILE SER ASP ASP VAL GLU ASP VAL LYS
SEQRES 4 B 123 GLU GLN PHE ALA THR HIS GLU THR PHE MET MET GLU LEU
SEQRES 5 B 123 SER ALA HIS GLN SER SER VAL GLY SER VAL LEU GLN ALA
SEQRES 6 B 123 GLY ASN GLN LEU MET THR GLN GLY THR LEU SER ASP GLU
SEQRES 7 B 123 GLU GLU PHE GLU ILE GLN GLU GLN MET THR LEU LEU ASN
SEQRES 8 B 123 ALA ARG TRP GLU ALA LEU ARG VAL GLU SER MET GLU ARG
SEQRES 9 B 123 GLN SER ARG LEU HIS ASP ALA LEU MET GLU LEU GLN LYS
SEQRES 10 B 123 LYS GLN LEU GLN GLN LEU
HET MG A 1 1
HETNAM MG MAGNESIUM ION
FORMUL 3 MG MG 2+
FORMUL 4 HOH *51(H2 O)
HELIX 1 1 MET A 309 GLN A 335 1 27
HELIX 2 2 ASP A 341 GLY A 380 1 40
HELIX 3 3 SER A 383 GLN A 428 1 46
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 LEU B 430 1 48
LINK MG MG A 1 O HOH A 24 1555 1555 2.12
LINK MG MG A 1 O HOH A 26 1555 1555 2.16
LINK MG MG A 1 O HOH A 25 1555 1555 2.73
SITE 1 AC1 4 HOH A 24 HOH A 25 HOH A 26 HOH A 27
CRYST1 42.740 58.020 91.280 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 0.023397 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017235 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010955 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 -0.988802 -0.148351 -0.016192 20.33609 1
MTRIX2 2 -0.148230 0.988917 -0.008415 1.34866 1
MTRIX3 2 0.017261 -0.005921 -0.999834 -55.73369 1
(ATOM LINES ARE NOT SHOWN.)
END
