REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.B.EDMUNDSON,K.R.ELY,J.N.HERRON,B.D.CHESON REMARK 1 TITL THE BINDING OF OPIOID PEPTIDES TO THE MCG LIGHT REMARK 1 TITL 2 CHAIN DIMER. FLEXIBLE KEYS AND ADJUSTABLE LOCKS REMARK 1 REF MOL.IMMUNOL. V. 24 915 1987 REMARK 1 REFN ISSN 0161-5890 REMARK 1 REFERENCE 2 REMARK 1 AUTH K.R.ELY,J.N.HERRON,A.B.EDMUNDSON REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE ORTHORHOMBIC REMARK 1 TITL 2 FORM OF THE MCG BENCE-JONES DIMER REMARK 1 EDIT Y.YAMAMURA, T.TADA REMARK 1 REF PROGRESS IN IMMUNOLOGY V 61 1983 REMARK 1 PUBL ACADEMIC PRESS, NEW YORK REMARK 1 REFN REMARK 1 REFERENCE 3 REMARK 1 AUTH M.SCHIFFER,F.J.STEVENS,F.A.WESTHOLM,S.S.KIM, REMARK 1 AUTH 2 R.D.CARLSON REMARK 1 TITL SMALL-ANGLE NEUTRON SCATTERING STUDY OF REMARK 1 TITL 2 BENCE-JONES PROTEIN MCG. COMPARISON OF STRUCTURES REMARK 1 TITL 3 IN SOLUTION AND IN CRYSTAL REMARK 1 REF BIOCHEMISTRY V. 21 2874 1982 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 4 REMARK 1 AUTH E.E.ABOLA,K.R.ELY,A.B.EDMUNDSON REMARK 1 TITL MARKED STRUCTURAL DIFFERENCES OF THE MCG REMARK 1 TITL 2 BENCE-JONES DIMER IN TWO CRYSTAL SYSTEMS REMARK 1 REF BIOCHEMISTRY V. 19 432 1980 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 5 REMARK 1 AUTH K.R.ELY,J.R.FIRCA,K.J.WILLIAMS,E.E.ABOLA, REMARK 1 AUTH 2 J.M.FENTON,M.SCHIFFER,N.C.PANAGIOTOPOULOS, REMARK 1 AUTH 3 A.B.EDMUNDSON REMARK 1 TITL CRYSTAL PROPERTIES AS INDICATORS OF CONFORMATIONAL REMARK 1 TITL 2 CHANGES DURING LIGAND BINDING OR INTERCONVERSION REMARK 1 TITL 3 OF MCG LIGHT CHAIN ISOMERS REMARK 1 REF BIOCHEMISTRY V. 17 158 1978 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 6 REMARK 1 AUTH J.R.FIRCA,K.R.ELY,P.KREMSER,F.A.WESTHOLM, REMARK 1 AUTH 2 K.J.DORRINGTON,A.B.EDMUNDSON REMARK 1 TITL INTERCONVERSION OF CONFORMATIONAL ISOMERS OF LIGHT REMARK 1 TITL 2 CHAINS IN THE MCG IMMUNOGLOBULINS REMARK 1 REF BIOCHEMISTRY V. 17 148 1978 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 7 REMARK 1 AUTH J.D.CAPRA,A.B.EDMUNDSON REMARK 1 TITL THE ANTIBODY COMBINING SITE REMARK 1 REF SCI.AM. V. 236 50 1977 REMARK 1 REFN ISSN 0036-8733 REMARK 1 REFERENCE 8 REMARK 1 AUTH A.B.EDMUNDSON,E.E.ABOLA,K.R.ELY,J.R.FIRCA, REMARK 1 AUTH 2 N.C.PANAGIOTOPOULOS,M.SCHIFFER,F.A.WESTHOLM REMARK 1 TITL IMPLICATIONS OF CONFORMATIONAL ISOMERISM AND REMARK 1 TITL 2 ROTATIONAL ALLOMERISM TO THE BINDING OF SMALL REMARK 1 TITL 3 MOLECULES BY THE MCG BENCE-JONES DIMER REMARK 1 EDIT E.HABER, R.M.KRAUSE REMARK 1 REF ANTIBODIES IN HUMAN 135 1977 REMARK 1 REF 2 DIAGNOSIS AND THERAPY REMARK 1 PUBL RAVEN PRESS,NEW YORK REMARK 1 REFN REMARK 1 REFERENCE 9 REMARK 1 AUTH A.B.EDMUNDSON,K.R.ELY,E.E.ABOLA,M.SCHIFFER, REMARK 1 AUTH 2 N.PANAGIOTOPOULOS,H.F.DEUTSCH REMARK 1 TITL CONFORMATIONAL ISOMERISM,ROTATIONAL ALLOMERISM, REMARK 1 TITL 2 AND DIVERGENT EVOLUTION IN IMMUNOGLOBULIN LIGHT REMARK 1 TITL 3 CHAINS REMARK 1 REF FED.PROC. V. 35 2119 1976 REMARK 1 REFN ISSN 0014-9446 REMARK 1 REFERENCE 10 REMARK 1 AUTH A.B.EDMUNDSON,K.R.ELY,E.E.ABOLA,M.SCHIFFER, REMARK 1 AUTH 2 N.PANAGIOTOPOULOS REMARK 1 TITL ROTATIONAL ALLOMERISM AND DIVERGENT EVOLUTION OF REMARK 1 TITL 2 DOMAINS IN IMMUNOGLOBULIN LIGHT CHAINS REMARK 1 REF BIOCHEMISTRY V. 14 3953 1975 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 11 REMARK 1 AUTH A.B.EDMUNDSON,K.R.ELY,R.L.GIRLING,E.E.ABOLA, REMARK 1 AUTH 2 M.SCHIFFER,F.A.WESTHOLM,M.D.FAUSCH,H.F.DEUTSCH REMARK 1 TITL BINDING OF 2,4-DINITROPHENYL COMPOUNDS AND OTHER REMARK 1 TITL 2 SMALL MOLECULES TO A CRYSTALLINE LAMBDA-TYPE REMARK 1 TITL 3 BENCE-JONES DIMER REMARK 1 REF BIOCHEMISTRY V. 13 3816 1974 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 12 REMARK 1 AUTH A.B.EDMUNDSON,K.R.ELY,R.L.GIRLING,E.E.ABOLA, REMARK 1 AUTH 2 M.SCHIFFER,F.A.WESTHOLM REMARK 1 TITL STRUCTURE AND BINDING PROPERTIES OF A LAMBDA-TYPE REMARK 1 TITL 2 BENCE-JONES DIMER REMARK 1 EDIT L.BRENT, J.HOLBOROW REMARK 1 REF PROGRESS IN IMMUNOLOGY II V. 1 103 1974 REMARK 1 PUBL NORTH-HOLLAND PUBL.CO.,AMSTERDAM REMARK 1 REFN REMARK 1 REFERENCE 13 REMARK 1 AUTH J.W.FETT,H.F.DEUTSCH REMARK 1 TITL PRIMARY STRUCTURE OF THE MCG LAMBDA CHAIN REMARK 1 REF BIOCHEMISTRY V. 13 4102 1974 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 14 REMARK 1 AUTH K.R.ELY,R.L.GIRLING,M.SCHIFFER,D.E.CUNNINGHAM, REMARK 1 AUTH 2 A.B.EDMUNDSON REMARK 1 TITL PREPARATION AND PROPERTIES OF A BENCE-JONES DIMER REMARK 1 TITL 2 WITH MERCURY INSERTED INTO THE INTERCHAIN REMARK 1 TITL 3 DISULFIDE BOND REMARK 1 REF BIOCHEMISTRY V. 12 4233 1973 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 15 REMARK 1 AUTH M.SCHIFFER,R.L.GIRLING,K.R.ELY,A.B.EDMUNDSON REMARK 1 TITL STRUCTURE OF A LAMBDA-TYPE BENCE-JONES PROTEIN AT REMARK 1 TITL 2 3.5-ANGSTROMS RESOLUTION REMARK 1 REF BIOCHEMISTRY V. 12 4620 1973 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 16 REMARK 1 AUTH A.B.EDMUNDSON,M.SCHIFFER,K.R.ELY,M.K.WOOD REMARK 1 TITL STRUCTURAL FEATURES OF IMMUNOGLOBULIN LIGHT CHAINS REMARK 1 REF PROG.MOL.SUBCELL.BIOL. V. 3 159 1973 REMARK 1 REFN ISSN 0079-6484 REMARK 1 REFERENCE 17 REMARK 1 AUTH A.B.EDMUNDSON,M.SCHIFFER,K.R.ELY,M.K.WOOD REMARK 1 TITL STRUCTURE OF A LAMBDA-TYPE BENCE-JONES PROTEIN AT REMARK 1 TITL 2 6-ANGSTROMS RESOLUTION REMARK 1 REF BIOCHEMISTRY V. 11 1822 1972 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 18 REMARK 1 AUTH A.B.EDMUNDSON,M.SCHIFFER,M.K.WOOD,K.D.HARDMAN, REMARK 1 AUTH 2 K.R.ELY,C.F.AINSWORTH REMARK 1 TITL CRYSTALLOGRAPHIC STUDIES OF AN IGG IMMUNOGLOBULIN REMARK 1 TITL 2 AND THE BENCE-JONES PROTEIN FROM ONE PATIENT REMARK 1 REF COLD SPRING HARBOR V. 36 427 1972 REMARK 1 REF 2 SYMP.QUANT.BIOL. REMARK 1 REFN ISSN 0091-7451 REMARK 2 REMARK 2 RESOLUTION. 2.00 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) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 12906 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) : 0.187 REMARK 3 R VALUE (WORKING SET) : NULL 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) : NULL 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 : 3212 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 318 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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) : 0.026 ; 0.030 REMARK 3 ANGLE DISTANCE (A) : 0.052 ; 0.040 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.030 ; 0.030 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.014 ; 0.025 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.241 ; 0.150 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.270 ; 0.500 REMARK 3 MULTIPLE TORSION (A) : 0.400 ; 0.500 REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : 0.387 ; 0.500 REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 6.200 ; 3.000 REMARK 3 STAGGERED (DEGREES) : 27.900; 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) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2MCG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 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 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 61.96667 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 123.93333 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 123.93333 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 61.96667 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19600 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 1, 2 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 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 2 222 DISTANCE = 5.71 ANGSTROMS REMARK 525 HOH 2 224 DISTANCE = 9.26 ANGSTROMS REMARK 525 HOH 2 231 DISTANCE = 8.33 ANGSTROMS REMARK 525 HOH 2 233 DISTANCE = 6.50 ANGSTROMS REMARK 525 HOH 2 234 DISTANCE = 8.67 ANGSTROMS REMARK 525 HOH 2 236 DISTANCE = 6.45 ANGSTROMS REMARK 525 HOH 1 240 DISTANCE = 6.63 ANGSTROMS REMARK 525 HOH 1 245 DISTANCE = 5.96 ANGSTROMS REMARK 525 HOH 1 246 DISTANCE = 7.83 ANGSTROMS REMARK 525 HOH 2 251 DISTANCE = 7.47 ANGSTROMS REMARK 525 HOH 2 254 DISTANCE = 8.23 ANGSTROMS REMARK 525 HOH 2 264 DISTANCE = 7.07 ANGSTROMS REMARK 525 HOH 2 270 DISTANCE = 8.40 ANGSTROMS REMARK 525 HOH 2 273 DISTANCE = 5.53 ANGSTROMS REMARK 525 HOH 1 276 DISTANCE = 5.83 ANGSTROMS REMARK 525 HOH 1 277 DISTANCE = 6.11 ANGSTROMS REMARK 525 HOH 1 278 DISTANCE = 6.58 ANGSTROMS REMARK 525 HOH 2 281 DISTANCE = 7.08 ANGSTROMS REMARK 525 HOH 2 286 DISTANCE = 7.84 ANGSTROMS REMARK 525 HOH 2 288 DISTANCE = 5.70 ANGSTROMS REMARK 525 HOH 2 290 DISTANCE = 6.88 ANGSTROMS REMARK 525 HOH 2 292 DISTANCE = 5.31 ANGSTROMS REMARK 525 HOH 1 294 DISTANCE = 5.50 ANGSTROMS REMARK 525 HOH 1 295 DISTANCE = 5.51 ANGSTROMS REMARK 525 HOH 2 297 DISTANCE = 7.12 ANGSTROMS REMARK 525 HOH 2 299 DISTANCE = 9.11 ANGSTROMS REMARK 525 HOH 2 304 DISTANCE = 5.64 ANGSTROMS REMARK 525 HOH 1 306 DISTANCE = 6.84 ANGSTROMS REMARK 525 HOH 1 309 DISTANCE = 6.82 ANGSTROMS REMARK 525 HOH 1 312 DISTANCE = 5.05 ANGSTROMS REMARK 525 HOH 1 319 DISTANCE = 7.50 ANGSTROMS REMARK 525 HOH 1 320 DISTANCE = 7.39 ANGSTROMS REMARK 525 HOH 2 329 DISTANCE = 7.59 ANGSTROMS REMARK 525 HOH 1 331 DISTANCE = 6.11 ANGSTROMS REMARK 525 HOH 2 331 DISTANCE = 5.54 ANGSTROMS REMARK 525 HOH 2 333 DISTANCE = 7.78 ANGSTROMS REMARK 525 HOH 1 334 DISTANCE = 7.69 ANGSTROMS REMARK 525 HOH 2 340 DISTANCE = 6.00 ANGSTROMS REMARK 525 HOH 2 341 DISTANCE = 6.63 ANGSTROMS REMARK 525 HOH 2 355 DISTANCE = 8.16 ANGSTROMS REMARK 525 HOH 2 356 DISTANCE = 7.90 ANGSTROMS REMARK 525 HOH 2 366 DISTANCE = 5.21 ANGSTROMS REMARK 525 HOH 2 380 DISTANCE = 5.18 ANGSTROMS REMARK 525 HOH 2 382 DISTANCE = 6.07 ANGSTROMS