HEADER IMMUNE SYSTEM 09-DEC-15 5F89
TITLE STRUCTURE OF THE UNLIGANDED FAB FROM HIV-1 NEUTRALISING ANTIBODY
TITLE 2 CAP248-2B THAT BINDS TO THE GP120 C-TERMINUS - GP41 INTERFACE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAP248-2B HEAVY CHAIN;
COMPND 3 CHAIN: H, A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CAP248-2B LIGHT CHAIN;
COMPND 7 CHAIN: L, B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 CELL_LINE: B-CELL;
SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 CELL_LINE: B-CELL;
SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS HIV, NEUTRALIZING ANTIBODY, GP120 C-TERMINUS, CAP248, GP120-GP41
KEYWDS 2 INTERFACE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR C.K.WIBMER,J.GORMAN,P.D.KWONG
REVDAT 2 29-MAR-17 5F89 1 JRNL
REVDAT 1 21-DEC-16 5F89 0
JRNL AUTH C.K.WIBMER,J.GORMAN,G.OZOROWSKI,J.N.BHIMAN,D.J.SHEWARD,
JRNL AUTH 2 D.H.ELLIOTT,J.ROUELLE,A.SMIRA,M.G.JOYCE,N.NDABAMBI,A.DRUZ,
JRNL AUTH 3 M.ASOKAN,D.R.BURTON,M.CONNORS,S.S.ABDOOL KARIM,J.R.MASCOLA,
JRNL AUTH 4 J.E.ROBINSON,A.B.WARD,C.WILLIAMSON,P.D.KWONG,L.MORRIS,
JRNL AUTH 5 P.L.MOORE
JRNL TITL STRUCTURE AND RECOGNITION OF A NOVEL HIV-1 GP120-GP41
JRNL TITL 2 INTERFACE ANTIBODY THAT CAUSED MPER EXPOSURE THROUGH VIRAL
JRNL TITL 3 ESCAPE.
JRNL REF PLOS PATHOG. V. 13 06074 2017
JRNL REFN ESSN 1553-7374
JRNL PMID 28076415
JRNL DOI 10.1371/JOURNAL.PPAT.1006074
REMARK 2
REMARK 2 RESOLUTION. 2.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.1
REMARK 3 NUMBER OF REFLECTIONS : 20492
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1023
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 41.8271 - 5.3229 0.98 3092 163 0.1937 0.2620
REMARK 3 2 5.3229 - 4.2263 0.99 3097 163 0.1793 0.2096
REMARK 3 3 4.2263 - 3.6924 0.99 3134 165 0.2200 0.2920
REMARK 3 4 3.6924 - 3.3550 0.97 3046 160 0.2691 0.2936
REMARK 3 5 3.3550 - 3.1146 0.91 2867 151 0.2913 0.3354
REMARK 3 6 3.1146 - 2.9310 0.77 2429 127 0.3060 0.3980
REMARK 3 7 2.9310 - 2.7842 0.57 1804 94 0.3531 0.3736
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) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.77
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 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 : 0.004 6914
REMARK 3 ANGLE : 0.812 9431
REMARK 3 CHIRALITY : 0.029 1081
REMARK 3 PLANARITY : 0.004 1196
REMARK 3 DIHEDRAL : 10.527 2437
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 2 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5060 -89.6169 68.9236
REMARK 3 T TENSOR
REMARK 3 T11: 0.7421 T22: 0.3275
REMARK 3 T33: 0.6233 T12: 0.0485
REMARK 3 T13: 0.0909 T23: 0.1016
REMARK 3 L TENSOR
REMARK 3 L11: 0.6888 L22: 0.5711
REMARK 3 L33: 0.8978 L12: 0.1297
REMARK 3 L13: 0.0574 L23: -0.2112
REMARK 3 S TENSOR
REMARK 3 S11: -0.1714 S12: 0.0151 S13: 0.2085
REMARK 3 S21: -0.0896 S22: 0.0908 S23: -0.0879
REMARK 3 S31: -0.0452 S32: -0.0117 S33: 0.0359
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 127 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7629-100.9452 96.5778
REMARK 3 T TENSOR
REMARK 3 T11: 0.8261 T22: 0.3189
REMARK 3 T33: 0.7794 T12: 0.0848
REMARK 3 T13: 0.1326 T23: 0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 0.5691 L22: 0.4180
REMARK 3 L33: 0.6378 L12: 0.3713
REMARK 3 L13: 0.0582 L23: -0.1150
REMARK 3 S TENSOR
REMARK 3 S11: 0.0497 S12: -0.0268 S13: -0.1618
REMARK 3 S21: -0.0364 S22: -0.1035 S23: 0.0746
REMARK 3 S31: 0.4349 S32: 0.1131 S33: 0.0154
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 2 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5469-109.0843 63.6127
REMARK 3 T TENSOR
REMARK 3 T11: 0.9834 T22: 0.3447
REMARK 3 T33: 0.7926 T12: 0.0787
REMARK 3 T13: 0.2078 T23: 0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 0.8208 L22: 0.6395
REMARK 3 L33: 0.7125 L12: 0.5942
REMARK 3 L13: -0.0854 L23: 0.3471
REMARK 3 S TENSOR
REMARK 3 S11: -0.1974 S12: 0.1308 S13: -0.1964
REMARK 3 S21: -0.3242 S22: -0.0561 S23: -0.1588
REMARK 3 S31: 0.2635 S32: 0.0965 S33: -0.0381
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 123 THROUGH 222 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.5090-113.4385 93.3076
REMARK 3 T TENSOR
REMARK 3 T11: 0.9255 T22: 0.2471
REMARK 3 T33: 0.6339 T12: 0.0861
REMARK 3 T13: 0.1346 T23: 0.1114
REMARK 3 L TENSOR
REMARK 3 L11: 0.2845 L22: 0.4079
REMARK 3 L33: 1.1566 L12: -0.0087
REMARK 3 L13: -0.0664 L23: 0.5357
REMARK 3 S TENSOR
REMARK 3 S11: -0.2128 S12: 0.1454 S13: -0.1379
REMARK 3 S21: -0.1829 S22: -0.0954 S23: 0.2799
REMARK 3 S31: 0.5083 S32: -0.4852 S33: -0.1071
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4650 -83.1585 132.1914
REMARK 3 T TENSOR
REMARK 3 T11: 0.8810 T22: 0.3914
REMARK 3 T33: 0.6798 T12: -0.0556
REMARK 3 T13: 0.1415 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 0.5297 L22: 0.5604
REMARK 3 L33: 0.6224 L12: 0.4164
REMARK 3 L13: 0.2330 L23: -0.1587
REMARK 3 S TENSOR
REMARK 3 S11: 0.1044 S12: -0.0554 S13: -0.0520
REMARK 3 S21: -0.3225 S22: -0.0672 S23: -0.2945
REMARK 3 S31: -0.1640 S32: -0.0570 S33: 0.0422
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 228 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6258 -78.4428 99.1862
REMARK 3 T TENSOR
REMARK 3 T11: 1.0705 T22: -0.1030
REMARK 3 T33: 0.8747 T12: 0.2164
REMARK 3 T13: 0.2334 T23: 0.2265
REMARK 3 L TENSOR
REMARK 3 L11: 0.8440 L22: 0.5344
REMARK 3 L33: 0.3461 L12: 0.2651
REMARK 3 L13: 0.0265 L23: 0.3456
REMARK 3 S TENSOR
REMARK 3 S11: -0.0282 S12: 0.8876 S13: 0.5001
REMARK 3 S21: 0.1667 S22: 0.1370 S23: 0.0870
REMARK 3 S31: -0.2622 S32: -0.0801 S33: 0.1902
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9206 -64.4843 126.6260
REMARK 3 T TENSOR
REMARK 3 T11: 0.9660 T22: 0.4449
REMARK 3 T33: 0.8271 T12: 0.0715
REMARK 3 T13: 0.1094 T23: 0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 0.5211 L22: 0.5007
REMARK 3 L33: 0.7846 L12: 0.0629
REMARK 3 L13: 0.0930 L23: -0.2144
REMARK 3 S TENSOR
REMARK 3 S11: 0.0966 S12: 0.0884 S13: -0.0530
REMARK 3 S21: -0.2983 S22: -0.1327 S23: 0.3060
REMARK 3 S31: -0.1797 S32: -0.2420 S33: 0.0956
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 123 THROUGH 223 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6674 -71.4851 97.9364
REMARK 3 T TENSOR
REMARK 3 T11: 0.8899 T22: 0.2400
REMARK 3 T33: 0.6958 T12: 0.0821
REMARK 3 T13: 0.1134 T23: 0.1275
REMARK 3 L TENSOR
REMARK 3 L11: 0.7095 L22: 0.8646
REMARK 3 L33: 0.3848 L12: 0.0389
REMARK 3 L13: -0.2716 L23: -0.2374
REMARK 3 S TENSOR
REMARK 3 S11: -0.0318 S12: -0.0003 S13: -0.0883
REMARK 3 S21: 0.0748 S22: 0.0506 S23: 0.1733
REMARK 3 S31: -0.0950 S32: -0.1023 S33: 0.0795
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 5F89 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216189.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20522
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.780
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 57.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.5% PEG4000 12.5% ISOPROPANOL 0.1M
REMARK 280 SODIUM CITRATE PH5.6 CRYOPROTECTANT: 30% ETHYLENE GLYCOL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 CYS H 216
REMARK 465 GLN L 1
REMARK 465 GLU L 211
REMARK 465 CYS L 212
REMARK 465 SER L 213
REMARK 465 CYS A 216
REMARK 465 GLN B 1
REMARK 465 CYS B 212
REMARK 465 SER B 213
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 PHE L 95C CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE L 95D CG CD1 CD2 CE1 CE2 CZ
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 ALA H 88 175.83 177.83
REMARK 500 SER H 130 50.47 -90.32
REMARK 500 ASP H 144 82.93 50.59
REMARK 500 SER H 187 32.31 -84.51
REMARK 500 THR H 191 -70.02 -93.43
REMARK 500 THR L 26 -153.32 -143.24
REMARK 500 ILE L 27C -58.53 65.08
REMARK 500 TYR L 32 56.64 -94.43
REMARK 500 ARG L 42 -167.28 -77.81
REMARK 500 VAL L 51 -58.93 68.30
REMARK 500 ALA L 68 -122.03 52.67
REMARK 500 ASP L 82 33.92 -90.55
REMARK 500 SER L 95B -159.55 -83.55
REMARK 500 PRO L 142 -176.47 -69.44
REMARK 500 ASP L 152 -100.70 54.64
REMARK 500 ASN L 171 -2.34 66.62
REMARK 500 LEU L 181 -166.28 -128.40
REMARK 500 SER A 7 -164.58 -78.55
REMARK 500 SER A 127 -162.35 -169.96
REMARK 500 SER A 132 92.81 -165.01
REMARK 500 THR A 160 -57.42 -132.98
REMARK 500 SER A 177 135.78 -175.93
REMARK 500 SER A 188 53.56 -116.84
REMARK 500 THR A 191 -67.95 -101.21
REMARK 500 THR B 26 -156.89 -151.40
REMARK 500 ILE B 27C -65.89 59.21
REMARK 500 VAL B 51 -56.53 67.05
REMARK 500 ALA B 68 -119.00 53.64
REMARK 500 GLN B 79 -169.74 -128.45
REMARK 500 ASP B 139 77.64 60.34
REMARK 500 ASP B 152 -107.02 55.04
REMARK 500 PRO B 165 107.49 -58.15
REMARK 500 HIS B 198 107.06 -161.15
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5F89 H 1 216 PDB 5F89 5F89 1 216
DBREF 5F89 L 1 213 PDB 5F89 5F89 1 213
DBREF 5F89 A 1 216 PDB 5F89 5F89 1 216
DBREF 5F89 B 1 213 PDB 5F89 5F89 1 213
SEQRES 1 H 229 PCA VAL GLN LEU GLN GLN SER GLY PRO GLY LEU VAL LYS
SEQRES 2 H 229 PRO SER GLN THR LEU SER LEU THR CYS ASN VAL TYR GLY
SEQRES 3 H 229 VAL ALA ILE SER ASN GLU ASP TYR TYR TRP THR TRP ILE
SEQRES 4 H 229 ARG GLN HIS PRO GLY LYS GLY LEU GLU TRP ILE GLY ASP
SEQRES 5 H 229 ILE TYR TYR ASN SER GLY THR THR HIS TYR ASN PRO SER
SEQRES 6 H 229 LEU LYS SER ARG ALA SER VAL SER VAL ASP LEU SER ARG
SEQRES 7 H 229 ASN GLN PHE THR LEU LYS VAL THR SER VAL THR THR ALA
SEQRES 8 H 229 ASP ALA ALA VAL TYR TYR CYS ALA ARG GLU ALA SER THR
SEQRES 9 H 229 LYS ILE THR ASP ASP GLY GLY ALA PHE ASP PHE TRP GLY
SEQRES 10 H 229 ARG GLY THR MET VAL THR VAL SER SER ALA SER THR LYS
SEQRES 11 H 229 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER
SEQRES 12 H 229 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS
SEQRES 13 H 229 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER
SEQRES 14 H 229 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL
SEQRES 15 H 229 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL
SEQRES 16 H 229 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE
SEQRES 17 H 229 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP
SEQRES 18 H 229 LYS LYS VAL GLU PRO LYS SER CYS
SEQRES 1 L 225 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER
SEQRES 2 L 225 PRO GLY GLN SER ILE SER ILE SER CYS THR GLY THR SER
SEQRES 3 L 225 SER ASP ILE GLY GLY TYR LYS TYR VAL SER TRP TYR GLN
SEQRES 4 L 225 GLN HIS PRO GLY ARG ALA PRO LYS LEU ILE ILE TYR ASP
SEQRES 5 L 225 VAL ILE LYS ARG PRO SER GLY ILE SER ASP ARG PHE SER
SEQRES 6 L 225 GLY SER LYS SER ALA ASN THR ALA SER LEU THR ILE SER
SEQRES 7 L 225 GLY LEU GLN ALA GLY ASP GLU ALA SER TYR TYR CYS SER
SEQRES 8 L 225 SER TYR THR THR LYS LYS THR SER PHE PHE GLY PRO ALA
SEQRES 9 L 225 THR ARG ALA TYR VAL PHE GLY SER GLY THR GLN VAL THR
SEQRES 10 L 225 VAL LEU GLY GLN PRO LYS ALA ASN PRO THR VAL THR LEU
SEQRES 11 L 225 PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA
SEQRES 12 L 225 THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA
SEQRES 13 L 225 VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS
SEQRES 14 L 225 ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN
SEQRES 15 L 225 ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO
SEQRES 16 L 225 GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN VAL
SEQRES 17 L 225 THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO
SEQRES 18 L 225 THR GLU CYS SER
SEQRES 1 A 229 PCA VAL GLN LEU GLN GLN SER GLY PRO GLY LEU VAL LYS
SEQRES 2 A 229 PRO SER GLN THR LEU SER LEU THR CYS ASN VAL TYR GLY
SEQRES 3 A 229 VAL ALA ILE SER ASN GLU ASP TYR TYR TRP THR TRP ILE
SEQRES 4 A 229 ARG GLN HIS PRO GLY LYS GLY LEU GLU TRP ILE GLY ASP
SEQRES 5 A 229 ILE TYR TYR ASN SER GLY THR THR HIS TYR ASN PRO SER
SEQRES 6 A 229 LEU LYS SER ARG ALA SER VAL SER VAL ASP LEU SER ARG
SEQRES 7 A 229 ASN GLN PHE THR LEU LYS VAL THR SER VAL THR THR ALA
SEQRES 8 A 229 ASP ALA ALA VAL TYR TYR CYS ALA ARG GLU ALA SER THR
SEQRES 9 A 229 LYS ILE THR ASP ASP GLY GLY ALA PHE ASP PHE TRP GLY
SEQRES 10 A 229 ARG GLY THR MET VAL THR VAL SER SER ALA SER THR LYS
SEQRES 11 A 229 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER
SEQRES 12 A 229 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS
SEQRES 13 A 229 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER
SEQRES 14 A 229 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL
SEQRES 15 A 229 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL
SEQRES 16 A 229 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE
SEQRES 17 A 229 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP
SEQRES 18 A 229 LYS LYS VAL GLU PRO LYS SER CYS
SEQRES 1 B 225 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER
SEQRES 2 B 225 PRO GLY GLN SER ILE SER ILE SER CYS THR GLY THR SER
SEQRES 3 B 225 SER ASP ILE GLY GLY TYR LYS TYR VAL SER TRP TYR GLN
SEQRES 4 B 225 GLN HIS PRO GLY ARG ALA PRO LYS LEU ILE ILE TYR ASP
SEQRES 5 B 225 VAL ILE LYS ARG PRO SER GLY ILE SER ASP ARG PHE SER
SEQRES 6 B 225 GLY SER LYS SER ALA ASN THR ALA SER LEU THR ILE SER
SEQRES 7 B 225 GLY LEU GLN ALA GLY ASP GLU ALA SER TYR TYR CYS SER
SEQRES 8 B 225 SER TYR THR THR LYS LYS THR SER PHE PHE GLY PRO ALA
SEQRES 9 B 225 THR ARG ALA TYR VAL PHE GLY SER GLY THR GLN VAL THR
SEQRES 10 B 225 VAL LEU GLY GLN PRO LYS ALA ASN PRO THR VAL THR LEU
SEQRES 11 B 225 PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA
SEQRES 12 B 225 THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA
SEQRES 13 B 225 VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS
SEQRES 14 B 225 ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN
SEQRES 15 B 225 ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO
SEQRES 16 B 225 GLU GLN TRP LYS SER HIS LYS SER TYR SER CYS GLN VAL
SEQRES 17 B 225 THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO
SEQRES 18 B 225 THR GLU CYS SER
HET PCA H 1 14
HET PCA A 1 14
HETNAM PCA PYROGLUTAMIC ACID
FORMUL 1 PCA 2(C5 H7 N O3)
FORMUL 5 HOH *23(H2 O)
HELIX 1 AA1 PRO H 61 LYS H 64 5 4
HELIX 2 AA2 THR H 83 ALA H 87 5 5
HELIX 3 AA3 SER H 187 LEU H 189 5 3
HELIX 4 AA4 GLN L 79 GLU L 83 5 5
HELIX 5 AA5 SER L 122 ALA L 128 1 7
HELIX 6 AA6 THR L 182 SER L 188 1 7
HELIX 7 AA7 PRO A 61 LYS A 64 5 4
HELIX 8 AA8 THR A 83 ALA A 87 5 5
HELIX 9 AA9 SER A 156 ALA A 158 5 3
HELIX 10 AB1 GLN B 79 GLU B 83 5 5
HELIX 11 AB2 SER B 122 ALA B 128 1 7
HELIX 12 AB3 THR B 182 LYS B 187 1 6
SHEET 1 AA1 4 GLN H 3 GLN H 6 0
SHEET 2 AA1 4 LEU H 18 TYR H 25 -1 O ASN H 23 N GLN H 5
SHEET 3 AA1 4 GLN H 77 VAL H 82 -1 O VAL H 82 N LEU H 18
SHEET 4 AA1 4 ALA H 67 ASP H 72 -1 N ASP H 72 O GLN H 77
SHEET 1 AA2 6 GLY H 10 VAL H 12 0
SHEET 2 AA2 6 THR H 107 VAL H 111 1 O MET H 108 N GLY H 10
SHEET 3 AA2 6 ALA H 88 ALA H 96 -1 N TYR H 90 O THR H 107
SHEET 4 AA2 6 TYR H 34 GLN H 39 -1 N ILE H 37 O TYR H 91
SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O ILE H 51 N TRP H 35A
SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O HIS H 58 N ASP H 50
SHEET 1 AA3 4 GLY H 10 VAL H 12 0
SHEET 2 AA3 4 THR H 107 VAL H 111 1 O MET H 108 N GLY H 10
SHEET 3 AA3 4 ALA H 88 ALA H 96 -1 N TYR H 90 O THR H 107
SHEET 4 AA3 4 ALA H 100F TRP H 103 -1 O PHE H 102 N ARG H 94
SHEET 1 AA4 4 SER H 120 LEU H 124 0
SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122
SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145
SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 AA5 4 THR H 131 SER H 132 0
SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132
SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145
SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 AA6 3 THR H 151 TRP H 154 0
SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 199 N THR H 151
SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200
SHEET 1 AA7 5 SER L 9 GLY L 13 0
SHEET 2 AA7 5 THR L 102 VAL L 106 1 O GLN L 103 N VAL L 11
SHEET 3 AA7 5 SER L 85 LYS L 95 -1 N TYR L 86 O THR L 102
SHEET 4 AA7 5 VAL L 33 GLN L 38 -1 N SER L 34 O SER L 89
SHEET 5 AA7 5 LYS L 45 ILE L 48 -1 O ILE L 48 N TRP L 35
SHEET 1 AA8 4 SER L 9 GLY L 13 0
SHEET 2 AA8 4 THR L 102 VAL L 106 1 O GLN L 103 N VAL L 11
SHEET 3 AA8 4 SER L 85 LYS L 95 -1 N TYR L 86 O THR L 102
SHEET 4 AA8 4 ALA L 95G PHE L 98 -1 O ALA L 95J N THR L 92
SHEET 1 AA9 3 ILE L 19 THR L 24 0
SHEET 2 AA9 3 THR L 70 ILE L 75 -1 O ALA L 71 N CYS L 23
SHEET 3 AA9 3 PHE L 62 SER L 67 -1 N SER L 67 O THR L 70
SHEET 1 AB1 4 THR L 115 PHE L 119 0
SHEET 2 AB1 4 ALA L 131 PHE L 140 -1 O SER L 138 N THR L 115
SHEET 3 AB1 4 TYR L 173 LEU L 181 -1 O TYR L 173 N PHE L 140
SHEET 4 AB1 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178
SHEET 1 AB2 4 THR L 115 PHE L 119 0
SHEET 2 AB2 4 ALA L 131 PHE L 140 -1 O SER L 138 N THR L 115
SHEET 3 AB2 4 TYR L 173 LEU L 181 -1 O TYR L 173 N PHE L 140
SHEET 4 AB2 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174
SHEET 1 AB3 4 SER L 154 VAL L 156 0
SHEET 2 AB3 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154
SHEET 3 AB3 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148
SHEET 4 AB3 4 SER L 201 VAL L 207 -1 O SER L 201 N HIS L 198
SHEET 1 AB4 4 GLN A 3 SER A 7 0
SHEET 2 AB4 4 LEU A 18 TYR A 25 -1 O ASN A 23 N GLN A 5
SHEET 3 AB4 4 GLN A 77 VAL A 82 -1 O LEU A 80 N LEU A 20
SHEET 4 AB4 4 ALA A 67 ASP A 72 -1 N ASP A 72 O GLN A 77
SHEET 1 AB5 6 LEU A 11 VAL A 12 0
SHEET 2 AB5 6 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12
SHEET 3 AB5 6 ALA A 88 ALA A 96 -1 N TYR A 90 O THR A 107
SHEET 4 AB5 6 TYR A 35 GLN A 39 -1 N ILE A 37 O TYR A 91
SHEET 5 AB5 6 LEU A 45 TYR A 52 -1 O GLY A 49 N TRP A 36
SHEET 6 AB5 6 THR A 56 TYR A 59 -1 O THR A 56 N TYR A 52
SHEET 1 AB6 4 LEU A 11 VAL A 12 0
SHEET 2 AB6 4 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12
SHEET 3 AB6 4 ALA A 88 ALA A 96 -1 N TYR A 90 O THR A 107
SHEET 4 AB6 4 ALA A 100F TRP A 103 -1 O PHE A 102 N ARG A 94
SHEET 1 AB7 4 SER A 120 LEU A 124 0
SHEET 2 AB7 4 THR A 135 TYR A 145 -1 O LYS A 143 N SER A 120
SHEET 3 AB7 4 TYR A 176 PRO A 185 -1 O VAL A 182 N LEU A 138
SHEET 4 AB7 4 HIS A 164 THR A 165 -1 N HIS A 164 O VAL A 181
SHEET 1 AB8 4 THR A 131 SER A 132 0
SHEET 2 AB8 4 THR A 135 TYR A 145 -1 O THR A 135 N SER A 132
SHEET 3 AB8 4 TYR A 176 PRO A 185 -1 O VAL A 182 N LEU A 138
SHEET 4 AB8 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177
SHEET 1 AB9 3 THR A 151 TRP A 154 0
SHEET 2 AB9 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153
SHEET 3 AB9 3 THR A 205 LYS A 210 -1 O THR A 205 N HIS A 200
SHEET 1 AC1 5 SER B 9 GLY B 13 0
SHEET 2 AC1 5 THR B 102 VAL B 106 1 O THR B 105 N VAL B 11
SHEET 3 AC1 5 ALA B 84 LYS B 95 -1 N ALA B 84 O VAL B 104
SHEET 4 AC1 5 VAL B 33 GLN B 38 -1 N SER B 34 O SER B 89
SHEET 5 AC1 5 LYS B 45 ILE B 48 -1 O ILE B 48 N TRP B 35
SHEET 1 AC2 4 SER B 9 GLY B 13 0
SHEET 2 AC2 4 THR B 102 VAL B 106 1 O THR B 105 N VAL B 11
SHEET 3 AC2 4 ALA B 84 LYS B 95 -1 N ALA B 84 O VAL B 104
SHEET 4 AC2 4 ALA B 95G PHE B 98 -1 O THR B 95H N LYS B 94
SHEET 1 AC3 3 SER B 18 THR B 24 0
SHEET 2 AC3 3 THR B 70 SER B 76 -1 O ALA B 71 N CYS B 23
SHEET 3 AC3 3 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74
SHEET 1 AC4 4 THR B 115 PHE B 119 0
SHEET 2 AC4 4 ALA B 131 PHE B 140 -1 O SER B 138 N THR B 115
SHEET 3 AC4 4 TYR B 173 LEU B 181 -1 O LEU B 179 N LEU B 133
SHEET 4 AC4 4 VAL B 160 THR B 162 -1 N GLU B 161 O TYR B 178
SHEET 1 AC5 4 THR B 115 PHE B 119 0
SHEET 2 AC5 4 ALA B 131 PHE B 140 -1 O SER B 138 N THR B 115
SHEET 3 AC5 4 TYR B 173 LEU B 181 -1 O LEU B 179 N LEU B 133
SHEET 4 AC5 4 SER B 166 LYS B 167 -1 N SER B 166 O ALA B 174
SHEET 1 AC6 4 SER B 154 VAL B 156 0
SHEET 2 AC6 4 THR B 146 ALA B 151 -1 N ALA B 151 O SER B 154
SHEET 3 AC6 4 TYR B 192 HIS B 198 -1 O SER B 193 N LYS B 150
SHEET 4 AC6 4 SER B 201 VAL B 207 -1 O SER B 201 N HIS B 198
SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04
SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.04
SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03
SSBOND 4 CYS L 135 CYS L 194 1555 1555 2.04
SSBOND 5 CYS A 22 CYS A 92 1555 1555 2.04
SSBOND 6 CYS A 140 CYS A 196 1555 1555 2.04
SSBOND 7 CYS B 23 CYS B 88 1555 1555 2.03
SSBOND 8 CYS B 135 CYS B 194 1555 1555 2.04
LINK C PCA H 1 N VAL H 2 1555 1555 1.33
LINK C PCA A 1 N VAL A 2 1555 1555 1.33
CISPEP 1 PHE H 146 PRO H 147 0 -3.88
CISPEP 2 GLU H 148 PRO H 149 0 -3.78
CISPEP 3 PRO L 40 GLY L 41 0 -3.72
CISPEP 4 TYR L 141 PRO L 142 0 -2.24
CISPEP 5 GLY A 8 PRO A 9 0 0.07
CISPEP 6 PHE A 146 PRO A 147 0 -6.68
CISPEP 7 GLU A 148 PRO A 149 0 -4.59
CISPEP 8 TYR B 141 PRO B 142 0 -0.33
CRYST1 43.002 68.280 85.731 95.59 99.82 102.54 P 1 2
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 0.023255 0.005172 0.004795 0.00000
SCALE2 0.000000 0.015003 0.002118 0.00000
SCALE3 0.000000 0.000000 0.011955 0.00000
HETATM 1 N PCA H 1 3.360 -96.960 78.817 1.00 59.59 N
HETATM 2 CA PCA H 1 3.717 -95.526 79.055 1.00 59.66 C
HETATM 3 CB PCA H 1 4.857 -95.087 78.143 1.00 61.07 C
HETATM 4 CG PCA H 1 5.077 -96.216 77.157 1.00 61.94 C
HETATM 5 CD PCA H 1 4.188 -97.319 77.666 1.00 60.93 C
HETATM 6 OE PCA H 1 4.189 -98.435 77.150 1.00 61.29 O
HETATM 7 C PCA H 1 2.525 -94.631 78.789 1.00 59.07 C
HETATM 8 O PCA H 1 2.139 -93.836 79.646 1.00 58.28 O
HETATM 9 H PCA H 1 4.062 -97.476 79.003 1.00 71.50 H
HETATM 10 HA PCA H 1 4.002 -95.420 79.987 1.00 71.59 H
HETATM 11 HB2 PCA H 1 4.622 -94.251 77.688 1.00 73.28 H
HETATM 12 HB3 PCA H 1 5.670 -94.936 78.669 1.00 73.28 H
HETATM 13 HG2 PCA H 1 4.838 -95.938 76.248 1.00 74.33 H
HETATM 14 HG3 PCA H 1 6.014 -96.505 77.170 1.00 74.33 H
(ATOM LINES ARE NOT SHOWN.)
END
