HEADER OXIDOREDUCTASE 19-AUG-13 4MB8
TITLE EVOLUTIONARY HISTORY AND METABOLIC INSIGHTS OF ANCIENT MAMMALIAN
TITLE 2 URICASES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: URICASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 1.7.3.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCLASSIFIED MAMMALIA;
SOURCE 3 ORGANISM_TAXID: 1002697;
SOURCE 4 GENE: PHYLOGENETICALLY PREDICTED SEQUENCE FOR THE MAMMALIAN URICASE
SOURCE 5 ANCESTOR, UOX;
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: PET-21A
KEYWDS URIC ACID OXIDASE, LYSOZOME, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.O.ORTLUND,M.N.MURPHY
REVDAT 7 28-FEB-24 4MB8 1 REMARK
REVDAT 6 22-MAY-19 4MB8 1 COMPND SOURCE DBREF SEQADV
REVDAT 6 2 1 SHEET
REVDAT 5 15-NOV-17 4MB8 1 REMARK
REVDAT 4 02-JUL-14 4MB8 1 SOURCE
REVDAT 3 26-MAR-14 4MB8 1 JRNL
REVDAT 2 19-MAR-14 4MB8 1 JRNL
REVDAT 1 05-FEB-14 4MB8 0
JRNL AUTH J.T.KRATZER,M.A.LANASPA,M.N.MURPHY,C.CICERCHI,C.L.GRAVES,
JRNL AUTH 2 P.A.TIPTON,E.A.ORTLUND,R.J.JOHNSON,E.A.GAUCHER
JRNL TITL EVOLUTIONARY HISTORY AND METABOLIC INSIGHTS OF ANCIENT
JRNL TITL 2 MAMMALIAN URICASES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 3763 2014
JRNL REFN ISSN 0027-8424
JRNL PMID 24550457
JRNL DOI 10.1073/PNAS.1320393111
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1458
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 39.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 63465
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3220
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.7724 - 6.8170 0.99 2668 131 0.1460 0.1711
REMARK 3 2 6.8170 - 5.4152 1.00 2630 153 0.1959 0.2646
REMARK 3 3 5.4152 - 4.7319 1.00 2637 149 0.1423 0.1751
REMARK 3 4 4.7319 - 4.2998 1.00 2634 142 0.1339 0.1720
REMARK 3 5 4.2998 - 3.9920 1.00 2599 139 0.1508 0.1762
REMARK 3 6 3.9920 - 3.7568 1.00 2640 131 0.1576 0.2034
REMARK 3 7 3.7568 - 3.5688 1.00 2609 153 0.1597 0.2034
REMARK 3 8 3.5688 - 3.4135 1.00 2609 164 0.1696 0.2020
REMARK 3 9 3.4135 - 3.2822 1.00 2600 151 0.1824 0.2395
REMARK 3 10 3.2822 - 3.1689 1.00 2630 118 0.1750 0.2199
REMARK 3 11 3.1689 - 3.0699 1.00 2606 137 0.1901 0.2409
REMARK 3 12 3.0699 - 2.9822 1.00 2599 155 0.1994 0.2641
REMARK 3 13 2.9822 - 2.9037 1.00 2617 146 0.2018 0.2632
REMARK 3 14 2.9037 - 2.8329 1.00 2643 136 0.2131 0.2485
REMARK 3 15 2.8329 - 2.7685 1.00 2575 150 0.1996 0.2534
REMARK 3 16 2.7685 - 2.7096 1.00 2639 123 0.2212 0.3043
REMARK 3 17 2.7096 - 2.6554 1.00 2637 129 0.2252 0.2810
REMARK 3 18 2.6554 - 2.6053 1.00 2599 142 0.2376 0.3368
REMARK 3 19 2.6053 - 2.5588 1.00 2611 129 0.2245 0.2902
REMARK 3 20 2.5588 - 2.5154 1.00 2603 140 0.2304 0.2787
REMARK 3 21 2.5154 - 2.4748 1.00 2615 142 0.2357 0.3132
REMARK 3 22 2.4748 - 2.4368 1.00 2592 121 0.2419 0.3011
REMARK 3 23 2.4368 - 2.4009 1.00 2653 139 0.2475 0.2944
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.03
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 9495
REMARK 3 ANGLE : 1.240 12822
REMARK 3 CHIRALITY : 0.051 1420
REMARK 3 PLANARITY : 0.006 1619
REMARK 3 DIHEDRAL : 14.770 3533
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 33.4118 -63.8095 -25.8935
REMARK 3 T TENSOR
REMARK 3 T11: 0.2051 T22: 0.2434
REMARK 3 T33: 0.1502 T12: -0.0350
REMARK 3 T13: 0.0064 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 1.4312 L22: 0.7079
REMARK 3 L33: 0.1695 L12: 0.6711
REMARK 3 L13: 0.0690 L23: -0.1215
REMARK 3 S TENSOR
REMARK 3 S11: -0.0571 S12: -0.0785 S13: -0.0074
REMARK 3 S21: -0.0877 S22: 0.0369 S23: 0.0073
REMARK 3 S31: 0.0261 S32: -0.0530 S33: -0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4MB8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000081696.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63527
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% MPD, 40 MM MGCL2, AND 50 MM SODIUM
REMARK 280 CACODYLATE , PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.29000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 92.58000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 69.43500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 115.72500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 23.14500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -145.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 HIS A 3
REMARK 465 TYR A 4
REMARK 465 HIS A 5
REMARK 465 ASN A 6
REMARK 465 ASP A 7
REMARK 465 TYR A 8
REMARK 465 LYS A 9
REMARK 465 LYS A 10
REMARK 465 ASN A 11
REMARK 465 ASP A 12
REMARK 465 GLU A 13
REMARK 465 LYS A 299
REMARK 465 LEU A 300
REMARK 465 SER A 301
REMARK 465 SER A 302
REMARK 465 ARG A 303
REMARK 465 LEU A 304
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 HIS B 3
REMARK 465 TYR B 4
REMARK 465 HIS B 5
REMARK 465 ASN B 6
REMARK 465 ASP B 7
REMARK 465 TYR B 8
REMARK 465 LYS B 9
REMARK 465 LYS B 10
REMARK 465 ASN B 11
REMARK 465 ASP B 12
REMARK 465 GLU B 13
REMARK 465 LEU B 300
REMARK 465 SER B 301
REMARK 465 SER B 302
REMARK 465 ARG B 303
REMARK 465 LEU B 304
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 HIS C 3
REMARK 465 TYR C 4
REMARK 465 HIS C 5
REMARK 465 ASN C 6
REMARK 465 ASP C 7
REMARK 465 TYR C 8
REMARK 465 LYS C 9
REMARK 465 LYS C 10
REMARK 465 ASN C 11
REMARK 465 ASP C 12
REMARK 465 GLU C 13
REMARK 465 ARG C 203
REMARK 465 ASP C 204
REMARK 465 SER C 301
REMARK 465 SER C 302
REMARK 465 ARG C 303
REMARK 465 LEU C 304
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 HIS D 3
REMARK 465 TYR D 4
REMARK 465 HIS D 5
REMARK 465 ASN D 6
REMARK 465 ASP D 7
REMARK 465 TYR D 8
REMARK 465 LYS D 9
REMARK 465 LYS D 10
REMARK 465 ASN D 11
REMARK 465 ASP D 12
REMARK 465 GLU D 13
REMARK 465 LEU D 304
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 C 456 O HOH C 461 2.05
REMARK 500 NZ LYS D 122 O HOH D 526 2.12
REMARK 500 O HOH A 447 O HOH A 449 2.15
REMARK 500 O LEU C 247 NH2 ARG C 298 2.18
REMARK 500 O LYS C 36 O HOH C 429 2.18
REMARK 500 O LEU D 247 NH2 ARG D 298 2.18
REMARK 500 O ASP B 216 O HOH D 526 2.19
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 GLU A 15 140.67 67.58
REMARK 500 ILE A 84 -67.45 -121.60
REMARK 500 LYS A 85 -62.88 69.67
REMARK 500 HIS A 129 23.79 -153.09
REMARK 500 THR A 166 -167.38 -176.57
REMARK 500 HIS A 200 -73.81 -66.09
REMARK 500 GLN A 201 -171.83 158.98
REMARK 500 ARG A 203 -133.19 13.65
REMARK 500 ASP A 204 42.01 82.19
REMARK 500 PHE A 207 -55.49 63.34
REMARK 500 LYS A 272 -9.91 -56.13
REMARK 500 ASN A 277 -78.70 -97.60
REMARK 500 LYS A 278 98.00 1.30
REMARK 500 GLU A 279 81.93 -152.58
REMARK 500 ILE B 84 -99.36 -111.39
REMARK 500 LYS B 85 -103.61 68.52
REMARK 500 HIS B 129 24.11 -152.25
REMARK 500 THR B 166 -169.27 -175.12
REMARK 500 HIS B 200 -71.25 -64.02
REMARK 500 GLN B 201 147.94 139.98
REMARK 500 LYS B 228 -64.43 -120.70
REMARK 500 GLU B 230 122.15 7.33
REMARK 500 LYS B 278 94.13 -162.53
REMARK 500 HIS C 129 23.00 -151.82
REMARK 500 THR C 166 -169.88 -174.35
REMARK 500 HIS C 200 -73.93 -70.51
REMARK 500 GLN C 201 -16.76 165.62
REMARK 500 SER C 234 130.91 -170.13
REMARK 500 LYS C 272 -9.79 -57.31
REMARK 500 ASN C 277 -81.16 -97.62
REMARK 500 LYS C 278 97.96 13.74
REMARK 500 HIS D 129 23.19 -153.13
REMARK 500 THR D 166 -167.99 -175.78
REMARK 500 HIS D 200 -75.80 -68.66
REMARK 500 GLN D 201 -159.07 159.76
REMARK 500 ARG D 203 -143.99 66.35
REMARK 500 ASP D 204 34.58 71.21
REMARK 500 PHE D 207 -51.25 -28.17
REMARK 500 ASP D 227 -35.16 69.54
REMARK 500 SER D 234 141.29 -171.26
REMARK 500 ASN D 277 -82.62 -96.03
REMARK 500 LYS D 278 98.93 6.13
REMARK 500 LYS D 299 -51.21 -161.07
REMARK 500 SER D 301 156.19 75.13
REMARK 500 SER D 302 -142.94 -168.23
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 ARG B 298 LYS B 299 149.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 402
DBREF 4MB8 A 1 304 PDB 4MB8 4MB8 1 304
DBREF 4MB8 B 1 304 PDB 4MB8 4MB8 1 304
DBREF 4MB8 C 1 304 PDB 4MB8 4MB8 1 304
DBREF 4MB8 D 1 304 PDB 4MB8 4MB8 1 304
SEQRES 1 A 304 MET ALA HIS TYR HIS ASN ASP TYR LYS LYS ASN ASP GLU
SEQRES 2 A 304 VAL GLU PHE VAL ARG THR GLY TYR GLY LYS ASP MET VAL
SEQRES 3 A 304 LYS VAL LEU HIS ILE GLN ARG ASP GLY LYS TYR HIS SER
SEQRES 4 A 304 ILE LYS GLU VAL ALA THR SER VAL GLN LEU THR LEU SER
SEQRES 5 A 304 SER LYS LYS ASP TYR LEU HIS GLY ASP ASN SER ASP ILE
SEQRES 6 A 304 ILE PRO THR ASP THR ILE LYS ASN THR VAL HIS VAL LEU
SEQRES 7 A 304 ALA LYS PHE LYS GLY ILE LYS SER ILE GLU ALA PHE ALA
SEQRES 8 A 304 MET ASN ILE CYS GLU HIS PHE LEU SER SER PHE ASN HIS
SEQRES 9 A 304 VAL ILE ARG ALA GLN VAL TYR VAL GLU GLU VAL PRO TRP
SEQRES 10 A 304 LYS ARG PHE GLU LYS ASN GLY VAL LYS HIS VAL HIS ALA
SEQRES 11 A 304 PHE ILE HIS THR PRO THR GLY THR HIS PHE CYS GLU VAL
SEQRES 12 A 304 GLU GLN MET LYS SER GLY PRO PRO VAL ILE HIS SER GLY
SEQRES 13 A 304 ILE LYS ASP LEU LYS VAL LEU LYS THR THR GLN SER GLY
SEQRES 14 A 304 PHE GLU GLY PHE ILE LYS ASP GLN PHE THR THR LEU PRO
SEQRES 15 A 304 GLU VAL LYS ASP ARG CYS PHE ALA THR GLN VAL TYR CYS
SEQRES 16 A 304 LYS TRP ARG TYR HIS GLN GLY ARG ASP VAL ASP PHE GLU
SEQRES 17 A 304 ALA THR TRP ASP THR VAL ARG ASP ILE VAL LEU LYS LYS
SEQRES 18 A 304 PHE ALA GLY PRO TYR ASP LYS GLY GLU TYR SER PRO SER
SEQRES 19 A 304 VAL GLN LYS THR LEU TYR ASP ILE GLN VAL LEU SER LEU
SEQRES 20 A 304 SER ARG VAL PRO GLU ILE GLU ASP MET GLU ILE SER LEU
SEQRES 21 A 304 PRO ASN ILE HIS TYR PHE ASN ILE ASP MET SER LYS MET
SEQRES 22 A 304 GLY LEU ILE ASN LYS GLU GLU VAL LEU LEU PRO LEU ASP
SEQRES 23 A 304 ASN PRO TYR GLY LYS ILE THR GLY THR VAL LYS ARG LYS
SEQRES 24 A 304 LEU SER SER ARG LEU
SEQRES 1 B 304 MET ALA HIS TYR HIS ASN ASP TYR LYS LYS ASN ASP GLU
SEQRES 2 B 304 VAL GLU PHE VAL ARG THR GLY TYR GLY LYS ASP MET VAL
SEQRES 3 B 304 LYS VAL LEU HIS ILE GLN ARG ASP GLY LYS TYR HIS SER
SEQRES 4 B 304 ILE LYS GLU VAL ALA THR SER VAL GLN LEU THR LEU SER
SEQRES 5 B 304 SER LYS LYS ASP TYR LEU HIS GLY ASP ASN SER ASP ILE
SEQRES 6 B 304 ILE PRO THR ASP THR ILE LYS ASN THR VAL HIS VAL LEU
SEQRES 7 B 304 ALA LYS PHE LYS GLY ILE LYS SER ILE GLU ALA PHE ALA
SEQRES 8 B 304 MET ASN ILE CYS GLU HIS PHE LEU SER SER PHE ASN HIS
SEQRES 9 B 304 VAL ILE ARG ALA GLN VAL TYR VAL GLU GLU VAL PRO TRP
SEQRES 10 B 304 LYS ARG PHE GLU LYS ASN GLY VAL LYS HIS VAL HIS ALA
SEQRES 11 B 304 PHE ILE HIS THR PRO THR GLY THR HIS PHE CYS GLU VAL
SEQRES 12 B 304 GLU GLN MET LYS SER GLY PRO PRO VAL ILE HIS SER GLY
SEQRES 13 B 304 ILE LYS ASP LEU LYS VAL LEU LYS THR THR GLN SER GLY
SEQRES 14 B 304 PHE GLU GLY PHE ILE LYS ASP GLN PHE THR THR LEU PRO
SEQRES 15 B 304 GLU VAL LYS ASP ARG CYS PHE ALA THR GLN VAL TYR CYS
SEQRES 16 B 304 LYS TRP ARG TYR HIS GLN GLY ARG ASP VAL ASP PHE GLU
SEQRES 17 B 304 ALA THR TRP ASP THR VAL ARG ASP ILE VAL LEU LYS LYS
SEQRES 18 B 304 PHE ALA GLY PRO TYR ASP LYS GLY GLU TYR SER PRO SER
SEQRES 19 B 304 VAL GLN LYS THR LEU TYR ASP ILE GLN VAL LEU SER LEU
SEQRES 20 B 304 SER ARG VAL PRO GLU ILE GLU ASP MET GLU ILE SER LEU
SEQRES 21 B 304 PRO ASN ILE HIS TYR PHE ASN ILE ASP MET SER LYS MET
SEQRES 22 B 304 GLY LEU ILE ASN LYS GLU GLU VAL LEU LEU PRO LEU ASP
SEQRES 23 B 304 ASN PRO TYR GLY LYS ILE THR GLY THR VAL LYS ARG LYS
SEQRES 24 B 304 LEU SER SER ARG LEU
SEQRES 1 C 304 MET ALA HIS TYR HIS ASN ASP TYR LYS LYS ASN ASP GLU
SEQRES 2 C 304 VAL GLU PHE VAL ARG THR GLY TYR GLY LYS ASP MET VAL
SEQRES 3 C 304 LYS VAL LEU HIS ILE GLN ARG ASP GLY LYS TYR HIS SER
SEQRES 4 C 304 ILE LYS GLU VAL ALA THR SER VAL GLN LEU THR LEU SER
SEQRES 5 C 304 SER LYS LYS ASP TYR LEU HIS GLY ASP ASN SER ASP ILE
SEQRES 6 C 304 ILE PRO THR ASP THR ILE LYS ASN THR VAL HIS VAL LEU
SEQRES 7 C 304 ALA LYS PHE LYS GLY ILE LYS SER ILE GLU ALA PHE ALA
SEQRES 8 C 304 MET ASN ILE CYS GLU HIS PHE LEU SER SER PHE ASN HIS
SEQRES 9 C 304 VAL ILE ARG ALA GLN VAL TYR VAL GLU GLU VAL PRO TRP
SEQRES 10 C 304 LYS ARG PHE GLU LYS ASN GLY VAL LYS HIS VAL HIS ALA
SEQRES 11 C 304 PHE ILE HIS THR PRO THR GLY THR HIS PHE CYS GLU VAL
SEQRES 12 C 304 GLU GLN MET LYS SER GLY PRO PRO VAL ILE HIS SER GLY
SEQRES 13 C 304 ILE LYS ASP LEU LYS VAL LEU LYS THR THR GLN SER GLY
SEQRES 14 C 304 PHE GLU GLY PHE ILE LYS ASP GLN PHE THR THR LEU PRO
SEQRES 15 C 304 GLU VAL LYS ASP ARG CYS PHE ALA THR GLN VAL TYR CYS
SEQRES 16 C 304 LYS TRP ARG TYR HIS GLN GLY ARG ASP VAL ASP PHE GLU
SEQRES 17 C 304 ALA THR TRP ASP THR VAL ARG ASP ILE VAL LEU LYS LYS
SEQRES 18 C 304 PHE ALA GLY PRO TYR ASP LYS GLY GLU TYR SER PRO SER
SEQRES 19 C 304 VAL GLN LYS THR LEU TYR ASP ILE GLN VAL LEU SER LEU
SEQRES 20 C 304 SER ARG VAL PRO GLU ILE GLU ASP MET GLU ILE SER LEU
SEQRES 21 C 304 PRO ASN ILE HIS TYR PHE ASN ILE ASP MET SER LYS MET
SEQRES 22 C 304 GLY LEU ILE ASN LYS GLU GLU VAL LEU LEU PRO LEU ASP
SEQRES 23 C 304 ASN PRO TYR GLY LYS ILE THR GLY THR VAL LYS ARG LYS
SEQRES 24 C 304 LEU SER SER ARG LEU
SEQRES 1 D 304 MET ALA HIS TYR HIS ASN ASP TYR LYS LYS ASN ASP GLU
SEQRES 2 D 304 VAL GLU PHE VAL ARG THR GLY TYR GLY LYS ASP MET VAL
SEQRES 3 D 304 LYS VAL LEU HIS ILE GLN ARG ASP GLY LYS TYR HIS SER
SEQRES 4 D 304 ILE LYS GLU VAL ALA THR SER VAL GLN LEU THR LEU SER
SEQRES 5 D 304 SER LYS LYS ASP TYR LEU HIS GLY ASP ASN SER ASP ILE
SEQRES 6 D 304 ILE PRO THR ASP THR ILE LYS ASN THR VAL HIS VAL LEU
SEQRES 7 D 304 ALA LYS PHE LYS GLY ILE LYS SER ILE GLU ALA PHE ALA
SEQRES 8 D 304 MET ASN ILE CYS GLU HIS PHE LEU SER SER PHE ASN HIS
SEQRES 9 D 304 VAL ILE ARG ALA GLN VAL TYR VAL GLU GLU VAL PRO TRP
SEQRES 10 D 304 LYS ARG PHE GLU LYS ASN GLY VAL LYS HIS VAL HIS ALA
SEQRES 11 D 304 PHE ILE HIS THR PRO THR GLY THR HIS PHE CYS GLU VAL
SEQRES 12 D 304 GLU GLN MET LYS SER GLY PRO PRO VAL ILE HIS SER GLY
SEQRES 13 D 304 ILE LYS ASP LEU LYS VAL LEU LYS THR THR GLN SER GLY
SEQRES 14 D 304 PHE GLU GLY PHE ILE LYS ASP GLN PHE THR THR LEU PRO
SEQRES 15 D 304 GLU VAL LYS ASP ARG CYS PHE ALA THR GLN VAL TYR CYS
SEQRES 16 D 304 LYS TRP ARG TYR HIS GLN GLY ARG ASP VAL ASP PHE GLU
SEQRES 17 D 304 ALA THR TRP ASP THR VAL ARG ASP ILE VAL LEU LYS LYS
SEQRES 18 D 304 PHE ALA GLY PRO TYR ASP LYS GLY GLU TYR SER PRO SER
SEQRES 19 D 304 VAL GLN LYS THR LEU TYR ASP ILE GLN VAL LEU SER LEU
SEQRES 20 D 304 SER ARG VAL PRO GLU ILE GLU ASP MET GLU ILE SER LEU
SEQRES 21 D 304 PRO ASN ILE HIS TYR PHE ASN ILE ASP MET SER LYS MET
SEQRES 22 D 304 GLY LEU ILE ASN LYS GLU GLU VAL LEU LEU PRO LEU ASP
SEQRES 23 D 304 ASN PRO TYR GLY LYS ILE THR GLY THR VAL LYS ARG LYS
SEQRES 24 D 304 LEU SER SER ARG LEU
HET ACT B 401 7
HET ACT D 401 4
HET ACT D 402 7
HETNAM ACT ACETATE ION
FORMUL 5 ACT 3(C2 H3 O2 1-)
FORMUL 8 HOH *248(H2 O)
HELIX 1 1 LYS A 54 HIS A 59 1 6
HELIX 2 2 PRO A 67 LYS A 82 1 16
HELIX 3 3 SER A 86 PHE A 102 1 17
HELIX 4 4 PHE A 207 GLY A 224 1 18
HELIX 5 5 SER A 234 VAL A 250 1 17
HELIX 6 6 MET A 270 GLY A 274 5 5
HELIX 7 7 LYS B 54 HIS B 59 1 6
HELIX 8 8 PRO B 67 LYS B 82 1 16
HELIX 9 9 SER B 86 PHE B 102 1 17
HELIX 10 10 ASP B 206 GLY B 224 1 19
HELIX 11 11 SER B 234 VAL B 250 1 17
HELIX 12 12 MET B 270 GLY B 274 5 5
HELIX 13 13 LYS C 54 HIS C 59 1 6
HELIX 14 14 PRO C 67 LYS C 82 1 16
HELIX 15 15 SER C 86 PHE C 102 1 17
HELIX 16 16 ASP C 206 GLY C 224 1 19
HELIX 17 17 SER C 234 VAL C 250 1 17
HELIX 18 18 MET C 270 GLY C 274 5 5
HELIX 19 19 LYS D 54 HIS D 59 1 6
HELIX 20 20 PRO D 67 LYS D 82 1 16
HELIX 21 21 SER D 86 PHE D 102 1 17
HELIX 22 22 ASP D 206 GLY D 224 1 19
HELIX 23 23 SER D 234 VAL D 250 1 17
HELIX 24 24 MET D 270 GLY D 274 5 5
SHEET 1 AA111 PHE A 16 ASP A 34 0
SHEET 2 AA111 TYR A 37 LEU A 51 -1 O LYS A 41 N HIS A 30
SHEET 3 AA111 VAL A 105 GLU A 114 -1 O TYR A 111 N SER A 46
SHEET 4 AA111 THR A 138 MET A 146 -1 O HIS A 139 N GLU A 114
SHEET 5 AA111 PRO A 151 LYS A 164 -1 O HIS A 154 N GLU A 142
SHEET 6 AA111 PHE A 189 TYR A 199 -1 O PHE A 189 N LYS A 164
SHEET 7 AA111 ILE A 253 ASN A 262 -1 O GLU A 257 N LYS A 196
SHEET 8 AA111 TYR A 289 LYS A 297 -1 O ILE A 292 N LEU A 260
SHEET 9 AA111 GLU B 15 ASP B 34 -1 O VAL B 17 N THR A 295
SHEET 10 AA111 VAL D 281 PRO D 284 -1 O LEU D 282 N LEU B 29
SHEET 11 AA111 TYR D 265 ASN D 267 -1 N PHE D 266 O LEU D 283
SHEET 1 AA2 9 TYR C 265 ASN C 267 0
SHEET 2 AA2 9 VAL C 281 PRO C 284 -1 O LEU C 283 N PHE C 266
SHEET 3 AA2 9 TYR A 37 LEU A 51 0
SHEET 4 AA2 9 TYR B 289 LYS B 297 0
SHEET 5 AA2 9 ILE B 253 ASN B 262 -1 N LEU B 260 O ILE B 292
SHEET 6 AA2 9 PHE B 189 TYR B 199 -1 N LYS B 196 O GLU B 257
SHEET 7 AA2 9 PRO B 151 LYS B 164 -1 N ILE B 157 O CYS B 195
SHEET 8 AA2 9 VAL D 125 HIS D 133 -1 O HIS D 133 N LYS B 161
SHEET 9 AA2 9 TRP D 117 LYS D 122 -1 N LYS D 118 O ILE D 132
SHEET 1 AA3 9 TRP D 117 LYS D 122 0
SHEET 2 AA3 9 VAL D 125 HIS D 133 -1 O ILE D 132 N LYS D 118
SHEET 3 AA3 9 PRO B 151 LYS B 164 -1 N LYS B 161 O HIS D 133
SHEET 4 AA3 9 THR B 138 MET B 146 -1 N GLU B 144 O VAL B 152
SHEET 5 AA3 9 VAL B 105 GLU B 114 -1 N VAL B 110 O VAL B 143
SHEET 6 AA3 9 TYR B 37 LEU B 51 -1 N GLN B 48 O GLN B 109
SHEET 7 AA3 9 GLU B 15 ASP B 34 -1 N GLN B 32 O SER B 39
SHEET 8 AA3 9 VAL D 281 PRO D 284 -1 O LEU D 282 N LEU B 29
SHEET 9 AA3 9 TYR D 265 ASN D 267 -1 N PHE D 266 O LEU D 283
SHEET 1 AA4 9 TRP C 117 LYS C 122 0
SHEET 2 AA4 9 VAL C 125 HIS C 133 -1 O ILE C 132 N LYS C 118
SHEET 3 AA4 9 PRO A 151 LYS A 164 -1 N LYS A 161 O HIS C 133
SHEET 4 AA4 9 PHE A 189 TYR A 199 -1 O PHE A 189 N LYS A 164
SHEET 5 AA4 9 ILE A 253 ASN A 262 -1 O GLU A 257 N LYS A 196
SHEET 6 AA4 9 TYR A 289 LYS A 297 -1 O ILE A 292 N LEU A 260
SHEET 7 AA4 9 GLU B 15 ASP B 34 -1 O VAL B 17 N THR A 295
SHEET 8 AA4 9 VAL D 281 PRO D 284 -1 O LEU D 282 N LEU B 29
SHEET 9 AA4 9 TYR D 265 ASN D 267 -1 N PHE D 266 O LEU D 283
SHEET 1 AA5 9 TRP A 117 LYS A 122 0
SHEET 2 AA5 9 VAL A 125 HIS A 133 -1 O ILE A 132 N LYS A 118
SHEET 3 AA5 9 PRO C 151 LYS C 164 -1 O LYS C 161 N HIS A 133
SHEET 4 AA5 9 THR C 138 MET C 146 -1 N GLU C 144 O VAL C 152
SHEET 5 AA5 9 VAL C 105 GLU C 114 -1 N VAL C 110 O VAL C 143
SHEET 6 AA5 9 TYR C 37 LEU C 51 -1 N GLN C 48 O GLN C 109
SHEET 7 AA5 9 PHE C 16 ASP C 34 -1 N TYR C 21 O LEU C 49
SHEET 8 AA5 9 VAL A 281 PRO A 284 -1 N LEU A 282 O LEU C 29
SHEET 9 AA5 9 TYR A 265 ASN A 267 -1 N PHE A 266 O LEU A 283
SHEET 1 AA6 9 TRP A 117 LYS A 122 0
SHEET 2 AA6 9 VAL A 125 HIS A 133 -1 O ILE A 132 N LYS A 118
SHEET 3 AA6 9 PRO C 151 LYS C 164 -1 O LYS C 161 N HIS A 133
SHEET 4 AA6 9 PHE C 189 TYR C 199 -1 O PHE C 189 N LYS C 164
SHEET 5 AA6 9 ILE C 253 ASN C 262 -1 O GLU C 257 N LYS C 196
SHEET 6 AA6 9 TYR C 289 LYS C 297 -1 O ILE C 292 N LEU C 260
SHEET 7 AA6 9 GLU D 15 ASP D 34 -1 O GLY D 20 N THR C 293
SHEET 8 AA6 9 VAL B 281 PRO B 284 -1 N LEU B 282 O LEU D 29
SHEET 9 AA6 9 TYR B 265 ASN B 267 -1 N PHE B 266 O LEU B 283
SHEET 1 AA7 9 TYR B 265 ASN B 267 0
SHEET 2 AA7 9 VAL B 281 PRO B 284 -1 O LEU B 283 N PHE B 266
SHEET 3 AA7 9 GLU D 15 ASP D 34 -1 O LEU D 29 N LEU B 282
SHEET 4 AA7 9 TYR D 37 LEU D 51 -1 O LYS D 41 N HIS D 30
SHEET 5 AA7 9 VAL D 105 GLU D 114 -1 O GLN D 109 N GLN D 48
SHEET 6 AA7 9 THR D 138 MET D 146 -1 O HIS D 139 N GLU D 114
SHEET 7 AA7 9 PRO D 151 LYS D 164 -1 O HIS D 154 N GLU D 142
SHEET 8 AA7 9 VAL B 125 HIS B 133 -1 N HIS B 133 O LYS D 161
SHEET 9 AA7 9 TRP B 117 LYS B 122 -1 N LYS B 118 O ILE B 132
SHEET 1 AA8 9 TRP B 117 LYS B 122 0
SHEET 2 AA8 9 VAL B 125 HIS B 133 -1 O ILE B 132 N LYS B 118
SHEET 3 AA8 9 PRO D 151 LYS D 164 -1 O LYS D 161 N HIS B 133
SHEET 4 AA8 9 PHE D 189 TYR D 199 -1 O PHE D 189 N LYS D 164
SHEET 5 AA8 9 ILE D 253 ASN D 262 -1 O GLU D 257 N LYS D 196
SHEET 6 AA8 9 TYR D 289 LYS D 297 -1 O GLY D 290 N ASN D 262
SHEET 7 AA8 9 PHE C 16 ASP C 34 -1 N GLY C 20 O THR D 293
SHEET 8 AA8 9 VAL A 281 PRO A 284 -1 N LEU A 282 O LEU C 29
SHEET 9 AA8 9 TYR A 265 ASN A 267 -1 N PHE A 266 O LEU A 283
CISPEP 1 LYS A 278 GLU A 279 0 -1.04
CISPEP 2 ASN A 287 PRO A 288 0 -4.85
CISPEP 3 LYS B 278 GLU B 279 0 -1.45
CISPEP 4 ASN B 287 PRO B 288 0 -2.39
CISPEP 5 LYS C 278 GLU C 279 0 1.26
CISPEP 6 ASN C 287 PRO C 288 0 -2.99
CISPEP 7 ARG C 298 LYS C 299 0 20.92
CISPEP 8 LYS C 299 LEU C 300 0 -1.58
CISPEP 9 LYS D 278 GLU D 279 0 2.49
CISPEP 10 ASN D 287 PRO D 288 0 -4.16
SITE 1 AC1 3 SER A 46 GLN A 109 LYS B 291
SITE 1 AC2 4 THR C 68 PHE D 170 ARG D 187 HOH D 555
SITE 1 AC3 1 LYS D 291
CRYST1 143.778 143.778 138.870 90.00 90.00 120.00 P 61 24
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 0.006955 0.004016 0.000000 0.00000
SCALE2 0.000000 0.008031 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007201 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
