HEADER RNA BINDING PROTEIN/RNA 25-AUG-15 5DET
TITLE X-RAY STRUCTURE OF HUMAN RBPMS IN COMPLEX WITH THE RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA-BINDING PROTEIN WITH MULTIPLE SPLICING;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 14-111;
COMPND 5 SYNONYM: RBP-MS,HEART AND RRM EXPRESSED SEQUENCE,HERMES;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RNA (5'-R(P*UP*CP*AP*CP*U)-3');
COMPND 9 CHAIN: Q;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: RNA (5'-R(*UP*CP*AP*C)-3');
COMPND 13 CHAIN: P;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: RBPMS, HERMES;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606
KEYWDS RRM DOMAIN, RNA BINDING PROTEIN, RNA BINDING PROTEIN-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TEPLOVA,T.A.FARAZI,T.TUSCHL,D.J.PATEL
REVDAT 4 27-SEP-23 5DET 1 REMARK
REVDAT 3 27-SEP-17 5DET 1 JRNL REMARK
REVDAT 2 05-OCT-16 5DET 1 JRNL
REVDAT 1 23-SEP-15 5DET 0
JRNL AUTH M.TEPLOVA,T.A.FARAZI,T.TUSCHL,D.J.PATEL
JRNL TITL STRUCTURAL BASIS UNDERLYING CAC RNA RECOGNITION BY THE RRM
JRNL TITL 2 DOMAIN OF DIMERIC RNA-BINDING PROTEIN RBPMS.
JRNL REF Q. REV. BIOPHYS. V. 49 E1 2016
JRNL REFN ESSN 1469-8994
JRNL PMID 26347403
JRNL DOI 10.1017/S0033583515000207
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 13266
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 656
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 19.8678 - 3.3303 0.96 2515 132 0.1701 0.2047
REMARK 3 2 3.3303 - 2.6454 0.97 2500 139 0.1916 0.2486
REMARK 3 3 2.6454 - 2.3116 0.98 2566 117 0.1987 0.2662
REMARK 3 4 2.3116 - 2.1005 0.97 2508 126 0.2057 0.2706
REMARK 3 5 2.1005 - 1.9501 0.99 2521 142 0.2584 0.3130
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) : 27.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.93
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 : 0.008 1728
REMARK 3 ANGLE : 1.184 2364
REMARK 3 CHIRALITY : 0.048 273
REMARK 3 PLANARITY : 0.006 273
REMARK 3 DIHEDRAL : 15.654 699
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 8 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.6533 24.6777 57.8058
REMARK 3 T TENSOR
REMARK 3 T11: 0.1267 T22: 0.1313
REMARK 3 T33: 0.0871 T12: -0.0038
REMARK 3 T13: -0.0053 T23: -0.0272
REMARK 3 L TENSOR
REMARK 3 L11: 4.5713 L22: 3.2716
REMARK 3 L33: 1.4004 L12: -0.3303
REMARK 3 L13: -0.4421 L23: -0.8945
REMARK 3 S TENSOR
REMARK 3 S11: -0.0150 S12: 0.0002 S13: -0.0418
REMARK 3 S21: -0.0196 S22: -0.0671 S23: 0.1629
REMARK 3 S31: 0.1017 S32: -0.0425 S33: 0.0981
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 9 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.5469 2.6221 63.3333
REMARK 3 T TENSOR
REMARK 3 T11: 0.1551 T22: 0.1117
REMARK 3 T33: 0.1315 T12: -0.0149
REMARK 3 T13: -0.0152 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 5.2737 L22: 4.3313
REMARK 3 L33: 2.2046 L12: -0.7542
REMARK 3 L13: -0.6747 L23: -1.1486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0570 S12: 0.0927 S13: 0.0225
REMARK 3 S21: -0.2252 S22: -0.0579 S23: -0.0461
REMARK 3 S31: 0.0274 S32: 0.0158 S33: -0.0076
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'P' AND (RESID 1 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.3402 -7.6170 64.5206
REMARK 3 T TENSOR
REMARK 3 T11: 0.3700 T22: 0.2352
REMARK 3 T33: 0.3110 T12: -0.0104
REMARK 3 T13: -0.0256 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 5.3211 L22: 0.6842
REMARK 3 L33: 2.3729 L12: -1.1801
REMARK 3 L13: 1.8815 L23: -1.2224
REMARK 3 S TENSOR
REMARK 3 S11: 0.3677 S12: 0.0792 S13: -0.8043
REMARK 3 S21: -0.1950 S22: 0.1807 S23: 0.1401
REMARK 3 S31: 0.1132 S32: -0.2811 S33: -0.5452
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 5DET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000213099.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97919
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17527
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 90.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.77500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: 5CYJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS-HCL PH 6.5, 28% (W/V)
REMARK 280 PEG 2000 MME, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 45.11600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, Q, P
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 A 14
REMARK 465 GLU A 15
REMARK 465 ALA A 16
REMARK 465 ASN A 17
REMARK 465 LEU A 18
REMARK 465 GLN A 19
REMARK 465 GLU A 20
REMARK 465 SER B 14
REMARK 465 GLU B 15
REMARK 465 ALA B 16
REMARK 465 GLN B 19
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 B 247 O HOH Q 112 1.83
REMARK 500 O HOH B 259 O HOH B 262 2.09
REMARK 500 O HOH A 301 O HOH A 334 2.11
REMARK 500 O HOH B 213 O HOH B 232 2.14
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 LYS B 60 -113.33 -118.76
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 SO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5CYJ RELATED DB: PDB
REMARK 900 5CYJ CONTAINS THE SAME PROTEIN IN THE FREE STATE
DBREF 5DET A 14 111 UNP Q93062 RBPMS_HUMAN 14 111
DBREF 5DET B 14 111 UNP Q93062 RBPMS_HUMAN 14 111
DBREF 5DET Q 1 5 PDB 5DET 5DET 1 5
DBREF 5DET P 1 4 PDB 5DET 5DET 1 4
SEQRES 1 A 98 SER GLU ALA ASN LEU GLN GLU GLU GLU VAL ARG THR LEU
SEQRES 2 A 98 PHE VAL SER GLY LEU PRO LEU ASP ILE LYS PRO ARG GLU
SEQRES 3 A 98 LEU TYR LEU LEU PHE ARG PRO PHE LYS GLY TYR GLU GLY
SEQRES 4 A 98 SER LEU ILE LYS LEU THR SER LYS GLN PRO VAL GLY PHE
SEQRES 5 A 98 VAL SER PHE ASP SER ARG SER GLU ALA GLU ALA ALA LYS
SEQRES 6 A 98 ASN ALA LEU ASN GLY ILE ARG PHE ASP PRO GLU ILE PRO
SEQRES 7 A 98 GLN THR LEU ARG LEU GLU PHE ALA LYS ALA ASN THR LYS
SEQRES 8 A 98 MET ALA LYS ASN LYS LEU VAL
SEQRES 1 B 98 SER GLU ALA ASN LEU GLN GLU GLU GLU VAL ARG THR LEU
SEQRES 2 B 98 PHE VAL SER GLY LEU PRO LEU ASP ILE LYS PRO ARG GLU
SEQRES 3 B 98 LEU TYR LEU LEU PHE ARG PRO PHE LYS GLY TYR GLU GLY
SEQRES 4 B 98 SER LEU ILE LYS LEU THR SER LYS GLN PRO VAL GLY PHE
SEQRES 5 B 98 VAL SER PHE ASP SER ARG SER GLU ALA GLU ALA ALA LYS
SEQRES 6 B 98 ASN ALA LEU ASN GLY ILE ARG PHE ASP PRO GLU ILE PRO
SEQRES 7 B 98 GLN THR LEU ARG LEU GLU PHE ALA LYS ALA ASN THR LYS
SEQRES 8 B 98 MET ALA LYS ASN LYS LEU VAL
SEQRES 1 Q 5 U C A C U
SEQRES 1 P 4 U C A C
HET SO4 A 201 5
HET SO4 A 202 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *135(H2 O)
HELIX 1 AA1 LYS A 36 ARG A 45 1 10
HELIX 2 AA2 SER A 70 ASN A 82 1 13
HELIX 3 AA3 ALA A 106 LEU A 110 5 5
HELIX 4 AA4 LYS B 36 ARG B 45 1 10
HELIX 5 AA5 SER B 70 ASN B 82 1 13
HELIX 6 AA6 ALA B 106 LEU B 110 5 5
SHEET 1 AA1 4 TYR A 50 LYS A 56 0
SHEET 2 AA1 4 VAL A 63 PHE A 68 -1 O SER A 67 N GLU A 51
SHEET 3 AA1 4 THR A 25 SER A 29 -1 N VAL A 28 O GLY A 64
SHEET 4 AA1 4 ARG A 95 PHE A 98 -1 O GLU A 97 N PHE A 27
SHEET 1 AA2 4 TYR B 50 LYS B 56 0
SHEET 2 AA2 4 VAL B 63 PHE B 68 -1 O SER B 67 N GLY B 52
SHEET 3 AA2 4 THR B 25 SER B 29 -1 N VAL B 28 O GLY B 64
SHEET 4 AA2 4 ARG B 95 PHE B 98 -1 O GLU B 97 N PHE B 27
SITE 1 AC1 4 SER A 59 LYS A 60 ARG A 71 HOH A 339
SITE 1 AC2 4 LYS A 60 LYS A 78 PHE A 98 HOH A 316
CRYST1 30.800 90.232 34.160 90.00 93.70 90.00 P 1 21 1 4
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 0.032468 0.000000 0.002101 0.00000
SCALE2 0.000000 0.011083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029335 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
