HEADER IMMUNE SYSTEM 03-MAR-98 1A6V
TITLE B1-8 FV FRAGMENT COMPLEXED WITH A (4-HYDROXY-3-NITROPHENYL) ACETATE
TITLE 2 COMPOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: B1-8 FV (LIGHT CHAIN);
COMPND 3 CHAIN: L, M, N;
COMPND 4 FRAGMENT: FV FRAGMENT;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: B1-8 FV (HEAVY CHAIN);
COMPND 8 CHAIN: H, I, J;
COMPND 9 FRAGMENT: FV FRAGMENT;
COMPND 10 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 STRAIN: C57BL/6;
SOURCE 6 CELL_LINE: J558L;
SOURCE 7 ORGAN: TAIL;
SOURCE 8 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: J558L;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR: PEC-GAMMA3;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 15 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 16 ORGANISM_TAXID: 10090;
SOURCE 17 STRAIN: C57BL/6;
SOURCE 18 CELL_LINE: J558L;
SOURCE 19 ORGAN: TAIL;
SOURCE 20 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 21 EXPRESSION_SYSTEM_COMMON: HOUSE MOUSE;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 23 EXPRESSION_SYSTEM_CELL_LINE: J558L;
SOURCE 24 EXPRESSION_SYSTEM_VECTOR: PEC-GAMMA3
KEYWDS IMMUNOGLOBULIN, HAPTEN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SIMON,K.HENRICK,M.HIRSHBERG,G.WINTER
REVDAT 4 14-JUN-23 1A6V 1 REMARK SEQADV ATOM
REVDAT 3 14-AUG-13 1A6V 1 HEADER HET HETATM KEYWDS
REVDAT 3 2 1 LINK REMARK SITE VERSN
REVDAT 2 24-FEB-09 1A6V 1 VERSN
REVDAT 1 15-JUL-98 1A6V 0
JRNL AUTH T.SIMON,K.HENRICK,M.HIRSHBERG,G.WINTER
JRNL TITL X-RAY STRUCTURES OF FV FRAGMENT AND ITS
JRNL TITL 2 (4-HYDROXY-3-NITROPHENYL)ACETATE COMPLEX OF MURINE B1-8
JRNL TITL 3 ANTIBODY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.SIMON,K.RAJEWSKY
REMARK 1 TITL A FUNCTIONAL ANTIBODY MUTANT WITH AN INSERTION IN THE
REMARK 1 TITL 2 FRAMEWORK REGION 3 LOOP OF THE VH DOMAIN: IMPLICATIONS FOR
REMARK 1 TITL 3 ANTIBODY ENGINEERING
REMARK 1 REF PROTEIN ENG. V. 5 229 1992
REMARK 1 REFN ISSN 0269-2139
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 59954
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.296
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2960
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5222
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 478
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.012 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.040 ; 0.030
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.010 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.148 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 1.800 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 22.500; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.400 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.100 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.900 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.300 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE HAS THREE MOLECULES PER
REMARK 3 EQUIVALENT POSITION ARRANGED AS A TRANSLATION ALONG THE Z-AXIS
REMARK 3 SUCH THAT OVERALL THE DIFFRACTION DATA SHOWS WEAK INTENSITIES
REMARK 3 FOR HKL, L=2N AND THIS TRANSLATIONAL NON-CRYSTALLOGRAPHIC
REMARK 3 SYMMETRY IS ON CLEARLY BROKEN BY THE DIFFERENT CONFORMATION OF
REMARK 3 THE TAIL O HAPTEN LIGAND ADOPTED IN EACH OF THE THREE
REMARK 3 INDEPENDENTLY DETERMINED MOLECULES. THERE ARE ALSO TWO
REMARK 3 CONFORMATIONS FOUND FOR THE HAPTEN BOUND TO CHAINS L AND H.
REMARK 4
REMARK 4 1A6V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170466.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : AUG-95
REMARK 200 TEMPERATURE (KELVIN) : 269
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, AGROVATA/ROTAVATA
REMARK 200 DATA SCALING SOFTWARE : AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 367775
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 9.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.36100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN USING AMMONIUM
REMARK 280 SULPHATE AS PRECIPITANT
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 35.88000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.75550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.09500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.75550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.88000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.09500
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, 3
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 APPLY THE FOLLOWING TO CHAINS: L, H
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 APPLY THE FOLLOWING TO CHAINS: M, I
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, J
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 SER H 419
REMARK 465 SER H 420
REMARK 465 GLU M 110
REMARK 465 SER I 420
REMARK 465 GLU N 110
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 GLN L 1 CB CG CD OE1 NE2
REMARK 470 ARG L 23 CG CD NE CZ NH1 NH2
REMARK 470 SER L 24 OG
REMARK 470 LYS L 105 CG CD CE NZ
REMARK 470 GLU L 110 CB CG CD OE1 OE2
REMARK 470 GLN N 1 CB CG CD OE1 NE2
REMARK 470 PRO N 58 CB CG CD
REMARK 470 ASN N 96 CG OD1 ND2
REMARK 470 LYS J 313 CG CD CE NZ
REMARK 470 SER J 404 OG
REMARK 470 ASP J 408 CG OD1 OD2
REMARK 470 SER J 420 CB OG
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 THR N 82 C THR N 82 O 0.122
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 ASP L 43 C - N - CA ANGL. DEV. = 16.0 DEGREES
REMARK 500 ARG L 63 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG L 63 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ALA L 91 N - CA - CB ANGL. DEV. = 9.5 DEGREES
REMARK 500 VAL H 318 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 MET H 334 CG - SD - CE ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG H 340 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG H 343 C - N - CA ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG H 343 N - CA - CB ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG H 343 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 ARG H 343 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG H 343 NE - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 GLU H 346 N - CA - CB ANGL. DEV. = 11.3 DEGREES
REMARK 500 ARG H 350 CA - CB - CG ANGL. DEV. = 17.8 DEGREES
REMARK 500 ARG H 350 CG - CD - NE ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG H 350 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 LYS H 359 CA - CB - CG ANGL. DEV. = 23.4 DEGREES
REMARK 500 ASP H 373 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 SER H 388 N - CA - CB ANGL. DEV. = 9.9 DEGREES
REMARK 500 GLU H 389 CA - C - O ANGL. DEV. = 14.0 DEGREES
REMARK 500 ASP H 390 C - N - CA ANGL. DEV. = 29.6 DEGREES
REMARK 500 ASP H 390 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 GLY H 403 N - CA - C ANGL. DEV. = 26.0 DEGREES
REMARK 500 TYR H 406 CA - CB - CG ANGL. DEV. = 11.9 DEGREES
REMARK 500 ASP H 408 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ALA M 2 N - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 GLU M 16 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 GLU M 16 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ARG M 23 CA - CB - CG ANGL. DEV. = 13.6 DEGREES
REMARK 500 ARG M 23 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP M 43 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 LEU M 45 CB - CA - C ANGL. DEV. = 14.6 DEGREES
REMARK 500 ARG M 56 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 ARG M 56 CD - NE - CZ ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG M 56 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG M 63 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 GLN M 81 CB - CG - CD ANGL. DEV. = 15.9 DEGREES
REMARK 500 CYS M 90 N - CA - CB ANGL. DEV. = 9.5 DEGREES
REMARK 500 ALA M 91 N - CA - CB ANGL. DEV. = -9.4 DEGREES
REMARK 500 ARG I 340 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG I 340 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG I 350 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 GLU I 389 CA - CB - CG ANGL. DEV. = 16.7 DEGREES
REMARK 500 TYR I 395 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP I 408 CB - CG - OD1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 THR I 415 CA - CB - CG2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 VAL N 4 CA - CB - CG1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 VAL N 18 N - CA - CB ANGL. DEV. = 13.9 DEGREES
REMARK 500 LEU N 20 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 ARG N 23 CD - NE - CZ ANGL. DEV. = 11.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 90 ANGLE DEVIATIONS.
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 L 43 73.17 72.65
REMARK 500 HIS L 44 29.28 41.10
REMARK 500 THR L 53 -54.73 61.24
REMARK 500 SER L 67 -171.74 170.16
REMARK 500 ALA L 80 121.60 -39.74
REMARK 500 ALA L 86 178.04 175.76
REMARK 500 SER L 95 -98.61 34.97
REMARK 500 LEU L 109 88.00 60.87
REMARK 500 PHE H 329 -77.86 -38.61
REMARK 500 ARG H 340 110.55 174.66
REMARK 500 PRO H 341 137.38 -23.50
REMARK 500 ARG H 343 -60.63 148.80
REMARK 500 LYS H 367 -76.85 -119.77
REMARK 500 SER H 384 -88.59 -67.35
REMARK 500 LEU H 386 91.68 -61.69
REMARK 500 SER H 388 58.08 119.81
REMARK 500 ASP H 390 -21.35 -30.54
REMARK 500 SER H 391 91.14 -59.74
REMARK 500 TYR H 402 41.16 -99.89
REMARK 500 TYR M 34 57.07 37.52
REMARK 500 PRO M 42 115.56 -20.61
REMARK 500 ASP M 43 59.92 70.50
REMARK 500 HIS M 44 73.51 31.36
REMARK 500 THR M 53 -49.56 78.82
REMARK 500 ASN M 54 19.21 -142.52
REMARK 500 ALA M 62 -7.85 -39.82
REMARK 500 ALA M 86 -170.60 175.22
REMARK 500 TYR M 94 55.78 -116.23
REMARK 500 SER M 95 -8.22 65.39
REMARK 500 ASN M 96 4.37 -166.78
REMARK 500 ARG I 343 -93.10 -21.14
REMARK 500 SER I 366 -7.77 163.55
REMARK 500 SER I 385 52.45 35.02
REMARK 500 SER I 404 -16.18 -46.50
REMARK 500 ALA N 2 107.39 -173.57
REMARK 500 THR N 12 -158.68 -111.23
REMARK 500 PRO N 14 130.67 -35.85
REMARK 500 THR N 30 -154.12 -92.82
REMARK 500 SER N 32 2.31 -65.96
REMARK 500 TYR N 34 89.29 16.07
REMARK 500 ASP N 43 32.00 100.60
REMARK 500 THR N 53 -44.58 66.37
REMARK 500 ALA N 57 121.33 -23.81
REMARK 500 PRO N 58 136.46 -33.88
REMARK 500 VAL N 60 123.49 -39.24
REMARK 500 ALA N 62 -0.49 -53.38
REMARK 500 ALA N 80 140.49 -27.91
REMARK 500 THR N 82 -19.17 -40.33
REMARK 500 ALA N 86 -166.39 176.78
REMARK 500 SER N 95 -27.60 49.32
REMARK 500
REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: NULL
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: NULL
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: NULL
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: NULL
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1A6V L 1 109 UNP P01724 LV1B_MOUSE 20 128
DBREF 1A6V H 301 420 UNP P01751 HV07_MOUSE 20 139
DBREF 1A6V M 1 109 UNP P01724 LV1B_MOUSE 20 128
DBREF 1A6V I 301 420 UNP P01751 HV07_MOUSE 20 139
DBREF 1A6V N 1 109 UNP P01724 LV1B_MOUSE 20 128
DBREF 1A6V J 301 420 UNP P01751 HV07_MOUSE 20 139
SEQADV 1A6V GLU L 40 UNP P01724 GLN 59 VARIANT
SEQADV 1A6V VAL H 416 UNP P01751 LEU 135 VARIANT
SEQADV 1A6V GLU M 40 UNP P01724 GLN 59 VARIANT
SEQADV 1A6V VAL I 416 UNP P01751 LEU 135 VARIANT
SEQADV 1A6V GLU N 40 UNP P01724 GLN 59 VARIANT
SEQADV 1A6V VAL J 416 UNP P01751 LEU 135 VARIANT
SEQRES 1 L 110 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER
SEQRES 2 L 110 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR
SEQRES 3 L 110 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN
SEQRES 4 L 110 GLU LYS PRO ASP HIS LEU PHE THR GLY LEU ILE GLY GLY
SEQRES 5 L 110 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER
SEQRES 6 L 110 GLY SER LEU ILE GLY ASN LYS ALA ALA LEU THR ILE THR
SEQRES 7 L 110 GLY ALA GLN THR GLU ASP GLU ALA ILE TYR PHE CYS ALA
SEQRES 8 L 110 LEU TRP TYR SER ASN HIS TRP VAL PHE GLY GLY GLY THR
SEQRES 9 L 110 LYS LEU THR VAL LEU GLU
SEQRES 1 H 120 GLN VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS
SEQRES 2 H 120 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 H 120 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN
SEQRES 4 H 120 ARG PRO GLY ARG GLY LEU GLU TRP ILE GLY ARG ILE ASP
SEQRES 5 H 120 PRO ASN SER GLY GLY THR LYS TYR ASN GLU LYS PHE LYS
SEQRES 6 H 120 SER LYS ALA THR LEU THR VAL ASP LYS PRO SER SER THR
SEQRES 7 H 120 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER
SEQRES 8 H 120 ALA VAL TYR TYR CYS ALA ARG TYR ASP TYR TYR GLY SER
SEQRES 9 H 120 SER TYR PHE ASP TYR TRP GLY GLN GLY THR THR VAL THR
SEQRES 10 H 120 VAL SER SER
SEQRES 1 M 110 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER
SEQRES 2 M 110 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR
SEQRES 3 M 110 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN
SEQRES 4 M 110 GLU LYS PRO ASP HIS LEU PHE THR GLY LEU ILE GLY GLY
SEQRES 5 M 110 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER
SEQRES 6 M 110 GLY SER LEU ILE GLY ASN LYS ALA ALA LEU THR ILE THR
SEQRES 7 M 110 GLY ALA GLN THR GLU ASP GLU ALA ILE TYR PHE CYS ALA
SEQRES 8 M 110 LEU TRP TYR SER ASN HIS TRP VAL PHE GLY GLY GLY THR
SEQRES 9 M 110 LYS LEU THR VAL LEU GLU
SEQRES 1 I 120 GLN VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS
SEQRES 2 I 120 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 I 120 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN
SEQRES 4 I 120 ARG PRO GLY ARG GLY LEU GLU TRP ILE GLY ARG ILE ASP
SEQRES 5 I 120 PRO ASN SER GLY GLY THR LYS TYR ASN GLU LYS PHE LYS
SEQRES 6 I 120 SER LYS ALA THR LEU THR VAL ASP LYS PRO SER SER THR
SEQRES 7 I 120 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER
SEQRES 8 I 120 ALA VAL TYR TYR CYS ALA ARG TYR ASP TYR TYR GLY SER
SEQRES 9 I 120 SER TYR PHE ASP TYR TRP GLY GLN GLY THR THR VAL THR
SEQRES 10 I 120 VAL SER SER
SEQRES 1 N 110 GLN ALA VAL VAL THR GLN GLU SER ALA LEU THR THR SER
SEQRES 2 N 110 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR
SEQRES 3 N 110 GLY ALA VAL THR THR SER ASN TYR ALA ASN TRP VAL GLN
SEQRES 4 N 110 GLU LYS PRO ASP HIS LEU PHE THR GLY LEU ILE GLY GLY
SEQRES 5 N 110 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER
SEQRES 6 N 110 GLY SER LEU ILE GLY ASN LYS ALA ALA LEU THR ILE THR
SEQRES 7 N 110 GLY ALA GLN THR GLU ASP GLU ALA ILE TYR PHE CYS ALA
SEQRES 8 N 110 LEU TRP TYR SER ASN HIS TRP VAL PHE GLY GLY GLY THR
SEQRES 9 N 110 LYS LEU THR VAL LEU GLU
SEQRES 1 J 120 GLN VAL GLN LEU GLN GLN PRO GLY ALA GLU LEU VAL LYS
SEQRES 2 J 120 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY
SEQRES 3 J 120 TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN
SEQRES 4 J 120 ARG PRO GLY ARG GLY LEU GLU TRP ILE GLY ARG ILE ASP
SEQRES 5 J 120 PRO ASN SER GLY GLY THR LYS TYR ASN GLU LYS PHE LYS
SEQRES 6 J 120 SER LYS ALA THR LEU THR VAL ASP LYS PRO SER SER THR
SEQRES 7 J 120 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER
SEQRES 8 J 120 ALA VAL TYR TYR CYS ALA ARG TYR ASP TYR TYR GLY SER
SEQRES 9 J 120 SER TYR PHE ASP TYR TRP GLY GLN GLY THR THR VAL THR
SEQRES 10 J 120 VAL SER SER
HET NPC H 430 44
HET NPC I 430 22
HET NPC J 430 22
HETNAM NPC 4-HYDROXY-3-NITROPHENYLACETYL-EPSILON-AMINOCAPROIC ACID
HETNAM 2 NPC ANION
FORMUL 7 NPC 3(C14 H17 N2 O6 1-)
FORMUL 10 HOH *478(H2 O)
HELIX 1 1 THR L 82 ASP L 84 5 3
HELIX 2 2 PHE H 329 SER H 331 5 3
HELIX 3 3 GLU H 362 PHE H 364 5 3
HELIX 4 4 THR M 31 ASN M 33 5 3
HELIX 5 5 GLU I 362 PHE I 364 5 3
HELIX 6 6 SER J 388 ASP J 390 5 3
SHEET 1 A 4 VAL L 4 GLN L 6 0
SHEET 2 A 4 THR L 17 SER L 24 -1 N ARG L 23 O THR L 5
SHEET 3 A 4 LYS L 72 THR L 78 -1 N ILE L 77 O VAL L 18
SHEET 4 A 4 PHE L 64 ILE L 69 -1 N ILE L 69 O LYS L 72
SHEET 1 B 5 ALA L 9 THR L 11 0
SHEET 2 B 5 THR L 104 THR L 107 1 N LYS L 105 O LEU L 10
SHEET 3 B 5 ALA L 86 ALA L 91 -1 N TYR L 88 O THR L 104
SHEET 4 B 5 ASN L 36 LYS L 41 -1 N GLU L 40 O ILE L 87
SHEET 5 B 5 LEU L 45 ILE L 50 -1 N ILE L 50 O TRP L 37
SHEET 1 C 2 ALA L 91 TYR L 94 0
SHEET 2 C 2 HIS L 97 PHE L 100 -1 N VAL L 99 O LEU L 92
SHEET 1 D 4 GLN H 303 GLN H 305 0
SHEET 2 D 4 VAL H 318 SER H 325 -1 N SER H 325 O GLN H 303
SHEET 3 D 4 THR H 378 LEU H 383 -1 N LEU H 383 O VAL H 318
SHEET 4 D 4 ALA H 368 ASP H 373 -1 N ASP H 373 O THR H 378
SHEET 1 E 6 ALA H 309 LEU H 311 0
SHEET 2 E 6 THR H 414 THR H 417 1 N THR H 415 O GLU H 310
SHEET 3 E 6 ALA H 392 TYR H 399 -1 N TYR H 394 O THR H 414
SHEET 4 E 6 TRP H 333 GLN H 339 -1 N GLN H 339 O VAL H 393
SHEET 5 E 6 GLU H 346 ASP H 352 -1 N ILE H 351 O MET H 334
SHEET 6 E 6 GLY H 357 TYR H 360 -1 N LYS H 359 O ARG H 350
SHEET 1 F 5 ALA M 9 SER M 13 0
SHEET 2 F 5 THR M 104 LEU M 109 1 N LYS M 105 O LEU M 10
SHEET 3 F 5 ALA M 86 ALA M 91 -1 N TYR M 88 O THR M 104
SHEET 4 F 5 ASN M 36 LYS M 41 -1 N GLU M 40 O ILE M 87
SHEET 5 F 5 LEU M 45 ILE M 50 -1 N ILE M 50 O TRP M 37
SHEET 1 G 3 VAL M 18 CYS M 22 0
SHEET 2 G 3 LYS M 72 ILE M 77 -1 N ILE M 77 O VAL M 18
SHEET 3 G 3 PHE M 64 ILE M 69 -1 N ILE M 69 O LYS M 72
SHEET 1 H 2 ALA M 91 TRP M 93 0
SHEET 2 H 2 TRP M 98 PHE M 100 -1 N VAL M 99 O LEU M 92
SHEET 1 I 4 GLN I 303 GLN I 305 0
SHEET 2 I 4 VAL I 318 SER I 325 -1 N SER I 325 O GLN I 303
SHEET 3 I 4 THR I 378 LEU I 383 -1 N LEU I 383 O VAL I 318
SHEET 4 I 4 ALA I 368 ASP I 373 -1 N ASP I 373 O THR I 378
SHEET 1 J 6 ALA I 309 VAL I 312 0
SHEET 2 J 6 THR I 414 VAL I 418 1 N THR I 415 O GLU I 310
SHEET 3 J 6 ALA I 392 TYR I 399 -1 N TYR I 394 O THR I 414
SHEET 4 J 6 TRP I 333 GLN I 339 -1 N GLN I 339 O VAL I 393
SHEET 5 J 6 LEU I 345 ASP I 352 -1 N ILE I 351 O MET I 334
SHEET 6 J 6 THR I 358 TYR I 360 -1 N LYS I 359 O ARG I 350
SHEET 1 K 2 ALA I 397 TYR I 399 0
SHEET 2 K 2 PHE I 407 TRP I 410 -1 N TYR I 409 O ARG I 398
SHEET 1 L 5 ALA N 9 SER N 13 0
SHEET 2 L 5 THR N 104 LEU N 109 1 N LYS N 105 O LEU N 10
SHEET 3 L 5 ALA N 86 ALA N 91 -1 N TYR N 88 O THR N 104
SHEET 4 L 5 ASN N 36 LYS N 41 -1 N GLU N 40 O ILE N 87
SHEET 5 L 5 LEU N 45 ILE N 50 -1 N ILE N 50 O TRP N 37
SHEET 1 M 3 VAL N 18 ARG N 23 0
SHEET 2 M 3 LYS N 72 ILE N 77 -1 N ILE N 77 O VAL N 18
SHEET 3 M 3 PHE N 64 ILE N 69 -1 N ILE N 69 O LYS N 72
SHEET 1 N 2 ALA N 91 TYR N 94 0
SHEET 2 N 2 HIS N 97 PHE N 100 -1 N VAL N 99 O LEU N 92
SHEET 1 O 2 GLN J 303 GLN J 306 0
SHEET 2 O 2 CYS J 322 SER J 325 -1 N SER J 325 O GLN J 303
SHEET 1 P 5 ALA J 309 LEU J 311 0
SHEET 2 P 5 THR J 414 THR J 417 1 N THR J 415 O GLU J 310
SHEET 3 P 5 ALA J 392 TYR J 399 -1 N TYR J 394 O THR J 414
SHEET 4 P 5 TRP J 333 GLN J 339 -1 N GLN J 339 O VAL J 393
SHEET 5 P 5 LEU J 345 ARG J 350 -1 N GLY J 349 O TRP J 336
SHEET 1 Q 2 ALA J 397 TYR J 399 0
SHEET 2 Q 2 PHE J 407 TRP J 410 -1 N TYR J 409 O ARG J 398
SSBOND 1 CYS L 22 CYS L 90 1555 1555 2.02
SSBOND 2 CYS H 322 CYS H 396 1555 1555 2.05
SSBOND 3 CYS M 22 CYS M 90 1555 1555 2.02
SSBOND 4 CYS I 322 CYS I 396 1555 1555 2.03
SSBOND 5 CYS N 22 CYS N 90 1555 1555 2.05
SSBOND 6 CYS J 322 CYS J 396 1555 1555 2.04
SITE 1 AC1 10 HOH H 73 TRP H 333 HIS H 335 ARG H 350
SITE 2 AC1 10 LYS H 359 TYR H 401 SER H 405 TYR L 34
SITE 3 AC1 10 TRP L 93 TRP L 98
SITE 1 AC2 11 HOH H 73 HOH H 141 TRP H 333 HIS H 335
SITE 2 AC2 11 ARG H 350 LYS H 359 TYR H 399 TYR H 401
SITE 3 AC2 11 NPC H 430 TRP L 93 TRP L 98
SITE 1 AC3 13 TRP I 333 HIS I 335 ARG I 350 LYS I 359
SITE 2 AC3 13 TYR I 399 TYR I 401 TYR I 402 SER I 405
SITE 3 AC3 13 HOH I 512 HOH I 513 TYR M 34 TRP M 93
SITE 4 AC3 13 TRP M 98
SITE 1 AC4 12 TRP J 333 HIS J 335 ARG J 350 LYS J 359
SITE 2 AC4 12 TYR J 399 TYR J 401 HOH J 437 HOH J 514
SITE 3 AC4 12 THR N 31 SER N 32 TYR N 34 TRP N 93
CRYST1 71.760 86.190 111.511 90.00 90.00 90.00 P 21 21 21 12
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 0.013935 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011602 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008968 0.00000
MTRIX1 1 1.000000 -0.000240 0.002860 -0.21008 1
MTRIX2 1 0.000190 0.999840 0.017720 -1.86478 1
MTRIX3 1 -0.002860 -0.017720 0.999840 -36.92922 1
MTRIX1 2 0.999910 -0.013020 0.003260 -0.03115 1
MTRIX2 2 0.013080 0.999720 -0.019690 2.02331 1
MTRIX3 2 -0.003000 0.019730 0.999800 -37.68118 1
MTRIX1 3 0.999990 0.004500 0.000730 -0.17386 1
MTRIX2 3 -0.004540 0.998280 0.058440 -5.87130 1
MTRIX3 3 -0.000460 -0.058440 0.998290 -72.93678 1
MTRIX1 4 0.999940 -0.009680 -0.005540 0.71513 1
MTRIX2 4 0.009550 0.999690 -0.022940 1.84498 1
MTRIX3 4 0.005760 0.022890 0.999720 -74.76064 1
MTRIX1 5 0.999990 0.004870 -0.002210 -0.04107 1
MTRIX2 5 -0.004770 0.999130 0.041340 -2.53210 1
MTRIX3 5 0.002410 -0.041330 0.999140 -36.09732 1
MTRIX1 6 0.999960 0.003610 -0.008590 0.40194 1
MTRIX2 6 -0.003640 0.999990 -0.003230 -0.30156 1
MTRIX3 6 0.008570 0.003260 0.999960 -37.08856 1
(ATOM LINES ARE NOT SHOWN.)
END
