HEADER CYTOKINE, SIGNALING PROTEIN 20-NOV-12 4I18
TITLE CRYSTAL STRUCTURE OF HUMAN PROLACTIN RECEPTOR COMPLEXED WITH FAB
TITLE 2 FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIBODY LIGHT CHAIN;
COMPND 3 CHAIN: L, B;
COMPND 4 FRAGMENT: FAB;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ANTIBODY HEAVY CHAIN;
COMPND 8 CHAIN: H, A;
COMPND 9 FRAGMENT: FAB;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: PROLACTIN RECEPTOR;
COMPND 13 CHAIN: R, C;
COMPND 14 FRAGMENT: EXTRACELLULAR DOMAIN (UNP RESIDUES 25-235);
COMPND 15 SYNONYM: PRL-R;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: 55244;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PHAGEMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: 55244;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PHAGEMID;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 GENE: PRLR;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS IMMUNOGLOBULIN FOLD, PROLACTIN BINDING, RECEPTOR SIGNALING, CYTOKINE,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.DUGUID,S.MUKHERJEE,J.L.KOUADIO
REVDAT 4 20-SEP-23 4I18 1 REMARK LINK
REVDAT 3 15-NOV-17 4I18 1 REMARK
REVDAT 2 28-JAN-15 4I18 1 JRNL
REVDAT 1 20-NOV-13 4I18 0
JRNL AUTH S.S.RIZK,J.L.KOUADIO,A.SZYMBORSKA,E.M.DUGUID,S.MUKHERJEE,
JRNL AUTH 2 J.ZHENG,C.V.CLEVENGER,A.A.KOSSIAKOFF
JRNL TITL ENGINEERING SYNTHETIC ANTIBODY BINDERS FOR ALLOSTERIC
JRNL TITL 2 INHIBITION OF PROLACTIN RECEPTOR SIGNALING.
JRNL REF CELL COMMUN SIGNAL V. 13 1 2015
JRNL REFN
JRNL PMID 25589173
JRNL DOI 10.1186/S12964-014-0080-8
REMARK 2
REMARK 2 RESOLUTION. 3.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 46730
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2365
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.24
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.32
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3031
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9873
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.69000
REMARK 3 B22 (A**2) : 1.69000
REMARK 3 B33 (A**2) : -2.54000
REMARK 3 B12 (A**2) : 0.85000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.912
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.384
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.262
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.491
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10191 ; 0.016 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13885 ; 2.138 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1259 ; 9.484 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 418 ;34.222 ;23.923
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1562 ;22.205 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;22.118 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1502 ; 0.134 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7764 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : L B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 L (A): 750 ; 0.090 ; 0.500
REMARK 3 TIGHT THERMAL 1 L (A**2): 804 ; 8.840 ; 0.500
REMARK 3 MEDIUM THERMAL 1 L (A**2): 750 ; 8.940 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : H A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 H (A): 689 ; 0.130 ; 0.500
REMARK 3 TIGHT THERMAL 2 H (A**2): 801 ; 6.070 ; 0.500
REMARK 3 MEDIUM THERMAL 2 H (A**2): 689 ; 6.590 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 216
REMARK 3 ORIGIN FOR THE GROUP (A):-157.3303 -16.0977 -17.7393
REMARK 3 T TENSOR
REMARK 3 T11: 0.1602 T22: 0.0899
REMARK 3 T33: 0.1801 T12: -0.0342
REMARK 3 T13: -0.0851 T23: 0.0629
REMARK 3 L TENSOR
REMARK 3 L11: 0.1416 L22: 2.8450
REMARK 3 L33: 0.7302 L12: -0.0618
REMARK 3 L13: -0.1372 L23: -0.2759
REMARK 3 S TENSOR
REMARK 3 S11: -0.0739 S12: 0.0430 S13: 0.0603
REMARK 3 S21: -0.0785 S22: 0.2289 S23: 0.3964
REMARK 3 S31: -0.0275 S32: -0.2175 S33: -0.1550
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 4 H 230
REMARK 3 ORIGIN FOR THE GROUP (A):-144.8502 -24.7234 -8.2044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1378 T22: 0.0403
REMARK 3 T33: 0.1116 T12: -0.0242
REMARK 3 T13: 0.0065 T23: 0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.2340 L22: 1.5711
REMARK 3 L33: 1.2706 L12: 0.2609
REMARK 3 L13: 0.1128 L23: -0.1097
REMARK 3 S TENSOR
REMARK 3 S11: -0.0850 S12: 0.0127 S13: 0.0431
REMARK 3 S21: -0.2314 S22: 0.1475 S23: 0.1699
REMARK 3 S31: -0.0452 S32: -0.1300 S33: -0.0625
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 215
REMARK 3 ORIGIN FOR THE GROUP (A):-101.7038 -19.9678 6.7179
REMARK 3 T TENSOR
REMARK 3 T11: 0.0859 T22: 0.2372
REMARK 3 T33: 0.4226 T12: -0.0875
REMARK 3 T13: -0.0985 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.2046 L22: 2.2002
REMARK 3 L33: 2.5486 L12: -0.0257
REMARK 3 L13: 0.2116 L23: -1.2434
REMARK 3 S TENSOR
REMARK 3 S11: -0.1654 S12: -0.0370 S13: 0.3790
REMARK 3 S21: 0.2429 S22: -0.1530 S23: -0.7311
REMARK 3 S31: -0.3744 S32: 0.7111 S33: 0.3184
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 228
REMARK 3 ORIGIN FOR THE GROUP (A):-117.6431 -27.6810 1.1387
REMARK 3 T TENSOR
REMARK 3 T11: 0.1491 T22: 0.0611
REMARK 3 T33: 0.0713 T12: 0.0019
REMARK 3 T13: 0.0553 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 0.5371 L22: 0.9683
REMARK 3 L33: 1.0856 L12: -0.0087
REMARK 3 L13: 0.1674 L23: -0.6685
REMARK 3 S TENSOR
REMARK 3 S11: -0.0590 S12: 0.1144 S13: 0.0624
REMARK 3 S21: 0.0289 S22: -0.0174 S23: -0.1012
REMARK 3 S31: 0.0531 S32: 0.1774 S33: 0.0764
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : R 3 R 211
REMARK 3 ORIGIN FOR THE GROUP (A):-115.7048 -59.8864 23.5513
REMARK 3 T TENSOR
REMARK 3 T11: 0.2878 T22: 0.0887
REMARK 3 T33: 0.1164 T12: 0.1367
REMARK 3 T13: -0.0075 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 1.1676 L22: 1.1604
REMARK 3 L33: 6.6959 L12: -0.3751
REMARK 3 L13: -2.4678 L23: 0.6288
REMARK 3 S TENSOR
REMARK 3 S11: 0.0341 S12: -0.0514 S13: -0.0590
REMARK 3 S21: -0.0393 S22: -0.1073 S23: -0.1616
REMARK 3 S31: 0.4737 S32: 0.3427 S33: 0.0731
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3 C 201
REMARK 3 ORIGIN FOR THE GROUP (A):-157.0219 -60.1505 -17.1508
REMARK 3 T TENSOR
REMARK 3 T11: 0.2851 T22: 0.1235
REMARK 3 T33: 0.1437 T12: -0.1370
REMARK 3 T13: -0.0241 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 2.8439 L22: 1.4690
REMARK 3 L33: 5.5143 L12: 0.8674
REMARK 3 L13: -1.1158 L23: 0.3908
REMARK 3 S TENSOR
REMARK 3 S11: -0.1673 S12: 0.1286 S13: -0.1406
REMARK 3 S21: 0.0616 S22: 0.2257 S23: -0.1069
REMARK 3 S31: 0.4605 S32: 0.0632 S33: -0.0584
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT, ANISOU RECORDS REMOVED BY AUTHOR REQUEST
REMARK 4
REMARK 4 4I18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000076176.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1271
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47509
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.238
REMARK 200 RESOLUTION RANGE LOW (A) : 250.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.20700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.75000
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: PDB ENTRIES 2R8S AND 3D48
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 160 MM CALCIUM ACETATE, 80 MM SODIUM
REMARK 280 CACODYLATE, PH 6.2, 11% PEG8000, 20% GLYCEROL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 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 20.74933
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 41.49867
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 31.12400
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 51.87333
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 10.37467
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, C
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, R
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 L 217
REMARK 465 GLU H 1
REMARK 465 ILE H 2
REMARK 465 SER H 3
REMARK 465 CYS H 231
REMARK 465 ASP H 232
REMARK 465 LYS H 233
REMARK 465 THR H 234
REMARK 465 HIS H 235
REMARK 465 THR H 236
REMARK 465 GLU B 216
REMARK 465 CYS B 217
REMARK 465 GLU A 1
REMARK 465 ILE A 2
REMARK 465 SER A 3
REMARK 465 LYS A 144
REMARK 465 SER A 145
REMARK 465 THR A 146
REMARK 465 SER A 147
REMARK 465 GLY A 148
REMARK 465 LYS A 229
REMARK 465 SER A 230
REMARK 465 CYS A 231
REMARK 465 ASP A 232
REMARK 465 LYS A 233
REMARK 465 THR A 234
REMARK 465 HIS A 235
REMARK 465 THR A 236
REMARK 465 GLN R 1
REMARK 465 LEU R 2
REMARK 465 LEU R 32
REMARK 465 PRO R 33
REMARK 465 ASP R 134
REMARK 465 LEU R 135
REMARK 465 GLN C 1
REMARK 465 LEU C 2
REMARK 465 GLN C 115
REMARK 465 PRO C 116
REMARK 465 GLU C 117
REMARK 465 ASP C 118
REMARK 465 ARG C 119
REMARK 465 LYS C 120
REMARK 465 LEU C 172
REMARK 465 HIS C 173
REMARK 465 PRO C 174
REMARK 465 GLY C 175
REMARK 465 GLN C 176
REMARK 465 ILE C 202
REMARK 465 PRO C 203
REMARK 465 SER C 204
REMARK 465 ASP C 205
REMARK 465 PHE C 206
REMARK 465 THR C 207
REMARK 465 MET C 208
REMARK 465 ASN C 209
REMARK 465 ASP C 210
REMARK 465 THR C 211
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 LYS H 144 CG CD CE NZ
REMARK 470 SER H 145 OG
REMARK 470 THR H 146 OG1 CG2
REMARK 470 SER A 143 CA C O CB OG
REMARK 470 LYS R 11 NZ
REMARK 470 LYS R 136 CG CD CE NZ
REMARK 470 LYS C 11 NZ
REMARK 470 MET C 85 CG SD CE
REMARK 470 LYS C 136 CG CD CE NZ
REMARK 470 LYS C 177 CG CD CE NZ
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 TRP R 191 CE2 TRP R 191 CD2 0.072
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 LEU H 156 N - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 VAL H 157 C - N - CA ANGL. DEV. = 17.8 DEGREES
REMARK 500 LEU A 21 CB - CG - CD1 ANGL. DEV. = -12.3 DEGREES
REMARK 500 VAL A 157 C - N - CA ANGL. DEV. = 17.7 DEGREES
REMARK 500 PRO R 4 C - N - CD ANGL. DEV. = -13.6 DEGREES
REMARK 500 ASP R 104 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP R 104 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 LEU R 132 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 LEU R 143 CA - CB - CG ANGL. DEV. = -14.2 DEGREES
REMARK 500 VAL R 182 CB - CA - C ANGL. DEV. = -11.7 DEGREES
REMARK 500 ASP R 210 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 LEU C 38 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
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 VAL L 30 16.25 -148.52
REMARK 500 SER L 31 -109.88 33.70
REMARK 500 ALA L 52 -32.81 76.23
REMARK 500 SER L 53 3.20 -157.93
REMARK 500 ALA L 85 -173.58 -173.09
REMARK 500 ASN L 155 -12.72 90.49
REMARK 500 ASN L 161 14.12 -143.68
REMARK 500 LYS L 193 -60.83 -98.95
REMARK 500 SER H 66 -3.05 -55.77
REMARK 500 VAL H 106 123.23 -39.13
REMARK 500 TYR H 107 8.72 81.81
REMARK 500 TRP H 108 58.19 -150.36
REMARK 500 SER H 142 -154.77 -167.18
REMARK 500 LYS H 144 71.27 55.83
REMARK 500 SER H 145 74.57 -46.82
REMARK 500 THR H 146 110.23 178.80
REMARK 500 VAL H 157 66.69 77.47
REMARK 500 ASP H 159 73.83 61.46
REMARK 500 ASN H 170 74.18 36.71
REMARK 500 SER H 171 39.22 32.96
REMARK 500 THR H 175 -32.40 -139.00
REMARK 500 PRO B 9 173.66 -55.00
REMARK 500 VAL B 30 23.64 -143.43
REMARK 500 SER B 31 -112.24 23.89
REMARK 500 ALA B 52 -35.92 81.57
REMARK 500 SER B 53 5.06 -154.87
REMARK 500 ALA B 85 -179.98 -177.48
REMARK 500 ASN B 155 -12.42 87.28
REMARK 500 ASN B 161 13.19 -149.31
REMARK 500 LYS B 193 -60.86 -97.50
REMARK 500 ARG B 214 173.82 -41.93
REMARK 500 SER A 66 5.48 -62.41
REMARK 500 VAL A 67 -17.48 -143.21
REMARK 500 TYR A 107 9.01 83.79
REMARK 500 TRP A 108 56.89 -141.98
REMARK 500 SER A 113 65.32 -100.15
REMARK 500 SER A 142 -160.09 -170.35
REMARK 500 VAL A 157 63.58 76.94
REMARK 500 ASP A 159 78.17 62.60
REMARK 500 ASN A 170 76.41 39.09
REMARK 500 SER A 171 44.01 27.97
REMARK 500 THR A 175 -30.57 -134.05
REMARK 500 HIS A 215 77.23 -116.44
REMARK 500 GLU R 8 120.98 -174.62
REMARK 500 ASN R 16 25.33 -150.80
REMARK 500 LYS R 17 -4.60 76.50
REMARK 500 THR R 28 137.64 82.71
REMARK 500 ASP R 29 -86.97 -179.29
REMARK 500 GLU R 43 97.88 -28.24
REMARK 500 GLU R 45 113.50 138.27
REMARK 500
REMARK 500 THIS ENTRY HAS 97 RAMACHANDRAN OUTLIERS.
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 GLY H 154 CYS H 155 147.50
REMARK 500 GLY A 154 CYS A 155 95.03
REMARK 500 CYS A 155 LEU A 156 146.89
REMARK 500 PRO R 103 ASP R 104 124.96
REMARK 500 ASN C 35 TYR C 36 31.45
REMARK 500 PRO C 103 ASP C 104 136.85
REMARK 500 LYS C 136 THR C 137 -132.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER H 78 OG
REMARK 620 2 SER A 78 OG 133.8
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT R 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301
DBREF 4I18 R 1 211 UNP P16471 PRLR_HUMAN 25 235
DBREF 4I18 C 1 211 UNP P16471 PRLR_HUMAN 25 235
DBREF 4I18 L 1 217 PDB 4I18 4I18 1 217
DBREF 4I18 B 1 217 PDB 4I18 4I18 1 217
DBREF 4I18 H 1 236 PDB 4I18 4I18 1 236
DBREF 4I18 A 1 236 PDB 4I18 4I18 1 236
SEQRES 1 L 217 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER
SEQRES 2 L 217 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA
SEQRES 3 L 217 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN
SEQRES 4 L 217 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA
SEQRES 5 L 217 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY
SEQRES 6 L 217 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER
SEQRES 7 L 217 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN
SEQRES 8 L 217 TYR TYR SER TYR TYR TYR PRO PHE THR PHE GLY GLN GLY
SEQRES 9 L 217 THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER
SEQRES 10 L 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER
SEQRES 11 L 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR
SEQRES 12 L 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA
SEQRES 13 L 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN
SEQRES 14 L 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU
SEQRES 15 L 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR
SEQRES 16 L 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL
SEQRES 17 L 217 THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 H 236 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY
SEQRES 2 H 236 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA
SEQRES 3 H 236 ALA SER GLY PHE ASN PHE SER SER SER SER MET HIS TRP
SEQRES 4 H 236 VAL ARG GLN ALA PRO GLY GLN GLY LEU GLU TRP VAL ALA
SEQRES 5 H 236 TYR ILE SER PRO TYR TYR GLY SER THR SER TYR ALA ASP
SEQRES 6 H 236 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER
SEQRES 7 H 236 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA
SEQRES 8 H 236 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG SER TYR GLY
SEQRES 9 H 236 TYR VAL TYR TRP ASN ALA TYR SER SER GLY MET ASP TYR
SEQRES 10 H 236 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER
SEQRES 11 H 236 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER
SEQRES 12 H 236 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU
SEQRES 13 H 236 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP
SEQRES 14 H 236 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO
SEQRES 15 H 236 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER
SEQRES 16 H 236 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR
SEQRES 17 H 236 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS
SEQRES 18 H 236 VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR
SEQRES 19 H 236 HIS THR
SEQRES 1 B 217 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER
SEQRES 2 B 217 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA
SEQRES 3 B 217 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN
SEQRES 4 B 217 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA
SEQRES 5 B 217 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY
SEQRES 6 B 217 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER
SEQRES 7 B 217 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN
SEQRES 8 B 217 TYR TYR SER TYR TYR TYR PRO PHE THR PHE GLY GLN GLY
SEQRES 9 B 217 THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER
SEQRES 10 B 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER
SEQRES 11 B 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR
SEQRES 12 B 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA
SEQRES 13 B 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN
SEQRES 14 B 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU
SEQRES 15 B 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR
SEQRES 16 B 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL
SEQRES 17 B 217 THR LYS SER PHE ASN ARG GLY GLU CYS
SEQRES 1 A 236 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY
SEQRES 2 A 236 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA
SEQRES 3 A 236 ALA SER GLY PHE ASN PHE SER SER SER SER MET HIS TRP
SEQRES 4 A 236 VAL ARG GLN ALA PRO GLY GLN GLY LEU GLU TRP VAL ALA
SEQRES 5 A 236 TYR ILE SER PRO TYR TYR GLY SER THR SER TYR ALA ASP
SEQRES 6 A 236 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER
SEQRES 7 A 236 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA
SEQRES 8 A 236 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG SER TYR GLY
SEQRES 9 A 236 TYR VAL TYR TRP ASN ALA TYR SER SER GLY MET ASP TYR
SEQRES 10 A 236 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER
SEQRES 11 A 236 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER
SEQRES 12 A 236 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU
SEQRES 13 A 236 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP
SEQRES 14 A 236 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO
SEQRES 15 A 236 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER
SEQRES 16 A 236 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR
SEQRES 17 A 236 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS
SEQRES 18 A 236 VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP LYS THR
SEQRES 19 A 236 HIS THR
SEQRES 1 R 211 GLN LEU PRO PRO GLY LYS PRO GLU ILE PHE LYS CYS ARG
SEQRES 2 R 211 SER PRO ASN LYS GLU THR PHE THR CYS TRP TRP ARG PRO
SEQRES 3 R 211 GLY THR ASP GLY GLY LEU PRO THR ASN TYR SER LEU THR
SEQRES 4 R 211 TYR HIS ARG GLU GLY GLU THR LEU MET HIS GLU CYS PRO
SEQRES 5 R 211 ASP TYR ILE THR GLY GLY PRO ASN SER CYS HIS PHE GLY
SEQRES 6 R 211 LYS GLN TYR THR SER MET TRP ARG THR TYR ILE MET MET
SEQRES 7 R 211 VAL ASN ALA THR ASN GLN MET GLY SER SER PHE SER ASP
SEQRES 8 R 211 GLU LEU TYR VAL ASP VAL THR TYR ILE VAL GLN PRO ASP
SEQRES 9 R 211 PRO PRO LEU GLU LEU ALA VAL GLU VAL LYS GLN PRO GLU
SEQRES 10 R 211 ASP ARG LYS PRO TYR LEU TRP ILE LYS TRP SER PRO PRO
SEQRES 11 R 211 THR LEU ILE ASP LEU LYS THR GLY TRP PHE THR LEU LEU
SEQRES 12 R 211 TYR GLU ILE ARG LEU LYS PRO GLU LYS ALA ALA GLU TRP
SEQRES 13 R 211 GLU ILE HIS PHE ALA GLY GLN GLN THR GLU PHE LYS ILE
SEQRES 14 R 211 LEU SER LEU HIS PRO GLY GLN LYS TYR LEU VAL GLN VAL
SEQRES 15 R 211 ARG CYS LYS PRO ASP HIS GLY TYR TRP SER ALA TRP SER
SEQRES 16 R 211 PRO ALA THR PHE ILE GLN ILE PRO SER ASP PHE THR MET
SEQRES 17 R 211 ASN ASP THR
SEQRES 1 C 211 GLN LEU PRO PRO GLY LYS PRO GLU ILE PHE LYS CYS ARG
SEQRES 2 C 211 SER PRO ASN LYS GLU THR PHE THR CYS TRP TRP ARG PRO
SEQRES 3 C 211 GLY THR ASP GLY GLY LEU PRO THR ASN TYR SER LEU THR
SEQRES 4 C 211 TYR HIS ARG GLU GLY GLU THR LEU MET HIS GLU CYS PRO
SEQRES 5 C 211 ASP TYR ILE THR GLY GLY PRO ASN SER CYS HIS PHE GLY
SEQRES 6 C 211 LYS GLN TYR THR SER MET TRP ARG THR TYR ILE MET MET
SEQRES 7 C 211 VAL ASN ALA THR ASN GLN MET GLY SER SER PHE SER ASP
SEQRES 8 C 211 GLU LEU TYR VAL ASP VAL THR TYR ILE VAL GLN PRO ASP
SEQRES 9 C 211 PRO PRO LEU GLU LEU ALA VAL GLU VAL LYS GLN PRO GLU
SEQRES 10 C 211 ASP ARG LYS PRO TYR LEU TRP ILE LYS TRP SER PRO PRO
SEQRES 11 C 211 THR LEU ILE ASP LEU LYS THR GLY TRP PHE THR LEU LEU
SEQRES 12 C 211 TYR GLU ILE ARG LEU LYS PRO GLU LYS ALA ALA GLU TRP
SEQRES 13 C 211 GLU ILE HIS PHE ALA GLY GLN GLN THR GLU PHE LYS ILE
SEQRES 14 C 211 LEU SER LEU HIS PRO GLY GLN LYS TYR LEU VAL GLN VAL
SEQRES 15 C 211 ARG CYS LYS PRO ASP HIS GLY TYR TRP SER ALA TRP SER
SEQRES 16 C 211 PRO ALA THR PHE ILE GLN ILE PRO SER ASP PHE THR MET
SEQRES 17 C 211 ASN ASP THR
HET GOL L 301 6
HET CA H 301 1
HET GOL H 302 6
HET CA B 301 1
HET GOL A 301 6
HET ACT R 301 4
HET GOL C 301 6
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 8 CA 2(CA 2+)
FORMUL 12 ACT C2 H3 O2 1-
HELIX 1 6 GLN L 80 PHE L 84 5 5
HELIX 2 7 SER L 124 GLY L 131 1 8
HELIX 3 8 LYS L 186 LYS L 191 1 6
HELIX 4 12 ASN H 31 SER H 33 5 3
HELIX 5 13 ASP H 65 LYS H 68 5 4
HELIX 6 14 SER H 202 LEU H 204 5 3
HELIX 7 15 LYS H 216 ASN H 219 5 4
HELIX 8 9 GLN B 80 PHE B 84 5 5
HELIX 9 10 SER B 124 SER B 130 1 7
HELIX 10 11 LYS B 186 LYS B 191 1 6
HELIX 11 16 ASN A 31 SER A 33 5 3
HELIX 12 17 ARG A 90 THR A 94 5 5
HELIX 13 18 SER A 202 LEU A 204 5 3
HELIX 14 19 LYS A 216 ASN A 219 5 4
HELIX 15 1 GLY R 65 THR R 69 5 5
HELIX 16 2 VAL R 97 VAL R 101 5 5
HELIX 17 3 ASP R 205 ASN R 209 5 5
HELIX 18 4 GLY C 65 SER C 70 1 6
HELIX 19 5 THR C 98 VAL C 101 5 4
SHEET 1 A 3 GLU R 8 ARG R 13 0
SHEET 2 A 3 PHE R 20 ARG R 25 -1 O THR R 21 N ARG R 13
SHEET 3 A 3 SER R 61 PHE R 64 -1 O PHE R 64 N PHE R 20
SHEET 1 B 4 HIS R 49 GLU R 50 0
SHEET 2 B 4 ASN R 35 ARG R 42 -1 N TYR R 40 O HIS R 49
SHEET 3 B 4 TYR R 75 THR R 82 -1 O ASN R 80 N SER R 37
SHEET 4 B 4 SER R 87 SER R 88 -1 O SER R 88 N ALA R 81
SHEET 1 C 4 HIS R 49 GLU R 50 0
SHEET 2 C 4 ASN R 35 ARG R 42 -1 N TYR R 40 O HIS R 49
SHEET 3 C 4 TYR R 75 THR R 82 -1 O ASN R 80 N SER R 37
SHEET 4 C 4 GLU R 92 VAL R 95 -1 O VAL R 95 N TYR R 75
SHEET 1 D 3 LEU R 107 LYS R 114 0
SHEET 2 D 3 TYR R 122 SER R 128 -1 O TYR R 122 N LYS R 114
SHEET 3 D 3 GLU R 166 ILE R 169 -1 O PHE R 167 N ILE R 125
SHEET 1 E 4 GLU R 157 PHE R 160 0
SHEET 2 E 4 LEU R 142 PRO R 150 -1 N ILE R 146 O HIS R 159
SHEET 3 E 4 LYS R 177 PRO R 186 -1 O LYS R 185 N LEU R 143
SHEET 4 E 4 THR R 198 GLN R 201 -1 O ILE R 200 N TYR R 178
SHEET 1 F 3 GLU C 8 ARG C 13 0
SHEET 2 F 3 PHE C 20 ARG C 25 -1 O TRP C 23 N LYS C 11
SHEET 3 F 3 SER C 61 PHE C 64 -1 O PHE C 64 N PHE C 20
SHEET 1 G 4 HIS C 49 GLU C 50 0
SHEET 2 G 4 LEU C 38 HIS C 41 -1 N TYR C 40 O HIS C 49
SHEET 3 G 4 THR C 74 THR C 82 -1 O ILE C 76 N HIS C 41
SHEET 4 G 4 SER C 87 PHE C 89 -1 O SER C 88 N ALA C 81
SHEET 1 H 4 HIS C 49 GLU C 50 0
SHEET 2 H 4 LEU C 38 HIS C 41 -1 N TYR C 40 O HIS C 49
SHEET 3 H 4 THR C 74 THR C 82 -1 O ILE C 76 N HIS C 41
SHEET 4 H 4 LEU C 93 ASP C 96 -1 O VAL C 95 N TYR C 75
SHEET 1 I 3 LEU C 107 VAL C 113 0
SHEET 2 I 3 LEU C 123 SER C 128 -1 O TRP C 124 N GLU C 112
SHEET 3 I 3 GLU C 166 ILE C 169 -1 O PHE C 167 N ILE C 125
SHEET 1 J 4 GLU C 157 PHE C 160 0
SHEET 2 J 4 LEU C 143 LEU C 148 -1 N LEU C 148 O GLU C 157
SHEET 3 J 4 TYR C 178 LYS C 185 -1 O GLN C 181 N ARG C 147
SHEET 4 J 4 THR C 198 ILE C 200 -1 O ILE C 200 N TYR C 178
SHEET 1 K 4 MET L 5 SER L 8 0
SHEET 2 K 4 VAL L 20 ALA L 26 -1 O ARG L 25 N THR L 6
SHEET 3 K 4 ASP L 71 ILE L 76 -1 O PHE L 72 N CYS L 24
SHEET 4 K 4 PHE L 63 SER L 68 -1 N SER L 68 O ASP L 71
SHEET 1 L 6 SER L 11 SER L 15 0
SHEET 2 L 6 THR L 105 LYS L 110 1 O GLU L 108 N LEU L 12
SHEET 3 L 6 ALA L 85 GLN L 91 -1 N ALA L 85 O VAL L 107
SHEET 4 L 6 VAL L 34 GLN L 39 -1 N TYR L 37 O TYR L 88
SHEET 5 L 6 LYS L 46 TYR L 50 -1 O LEU L 48 N TRP L 36
SHEET 6 L 6 SER L 54 LEU L 55 -1 O SER L 54 N TYR L 50
SHEET 1 M 4 SER L 11 SER L 15 0
SHEET 2 M 4 THR L 105 LYS L 110 1 O GLU L 108 N LEU L 12
SHEET 3 M 4 ALA L 85 GLN L 91 -1 N ALA L 85 O VAL L 107
SHEET 4 M 4 THR L 100 PHE L 101 -1 O THR L 100 N GLN L 91
SHEET 1 N 4 SER L 117 PHE L 121 0
SHEET 2 N 4 THR L 132 PHE L 142 -1 O VAL L 136 N PHE L 121
SHEET 3 N 4 TYR L 176 SER L 185 -1 O TYR L 176 N PHE L 142
SHEET 4 N 4 SER L 162 VAL L 166 -1 N SER L 165 O SER L 179
SHEET 1 O 4 ALA L 156 LEU L 157 0
SHEET 2 O 4 LYS L 148 VAL L 153 -1 N VAL L 153 O ALA L 156
SHEET 3 O 4 VAL L 194 THR L 200 -1 O ALA L 196 N LYS L 152
SHEET 4 O 4 VAL L 208 ASN L 213 -1 O VAL L 208 N VAL L 199
SHEET 1 P 4 MET B 5 SER B 8 0
SHEET 2 P 4 VAL B 20 ALA B 26 -1 O ARG B 25 N THR B 6
SHEET 3 P 4 ASP B 71 ILE B 76 -1 O PHE B 72 N CYS B 24
SHEET 4 P 4 PHE B 63 SER B 68 -1 N SER B 68 O ASP B 71
SHEET 1 Q 6 SER B 11 SER B 15 0
SHEET 2 Q 6 THR B 105 LYS B 110 1 O GLU B 108 N LEU B 12
SHEET 3 Q 6 ALA B 85 GLN B 91 -1 N ALA B 85 O VAL B 107
SHEET 4 Q 6 VAL B 34 GLN B 39 -1 N TYR B 37 O TYR B 88
SHEET 5 Q 6 LYS B 46 TYR B 50 -1 O LEU B 48 N TRP B 36
SHEET 6 Q 6 SER B 54 LEU B 55 -1 O SER B 54 N TYR B 50
SHEET 1 R 4 SER B 117 PHE B 121 0
SHEET 2 R 4 THR B 132 PHE B 142 -1 O VAL B 136 N PHE B 121
SHEET 3 R 4 TYR B 176 SER B 185 -1 O LEU B 184 N ALA B 133
SHEET 4 R 4 SER B 162 VAL B 166 -1 N GLN B 163 O THR B 181
SHEET 1 S 4 ALA B 156 LEU B 157 0
SHEET 2 S 4 LYS B 148 VAL B 153 -1 N VAL B 153 O ALA B 156
SHEET 3 S 4 VAL B 194 THR B 200 -1 O ALA B 196 N LYS B 152
SHEET 4 S 4 VAL B 208 ASN B 213 -1 O VAL B 208 N VAL B 199
SHEET 1 T 4 GLN H 6 SER H 10 0
SHEET 2 T 4 LEU H 21 SER H 28 -1 O SER H 24 N SER H 10
SHEET 3 T 4 THR H 81 MET H 86 -1 O MET H 86 N LEU H 21
SHEET 4 T 4 PHE H 71 ASP H 76 -1 N SER H 74 O TYR H 83
SHEET 1 U 6 GLY H 13 VAL H 15 0
SHEET 2 U 6 THR H 122 VAL H 126 1 O THR H 125 N GLY H 13
SHEET 3 U 6 ALA H 95 TYR H 103 -1 N TYR H 97 O THR H 122
SHEET 4 U 6 SER H 35 GLN H 42 -1 N HIS H 38 O ALA H 100
SHEET 5 U 6 LEU H 48 ILE H 54 -1 O GLU H 49 N ARG H 41
SHEET 6 U 6 THR H 61 TYR H 63 -1 O SER H 62 N TYR H 53
SHEET 1 V 4 GLY H 13 VAL H 15 0
SHEET 2 V 4 THR H 122 VAL H 126 1 O THR H 125 N GLY H 13
SHEET 3 V 4 ALA H 95 TYR H 103 -1 N TYR H 97 O THR H 122
SHEET 4 V 4 TYR H 117 TRP H 118 -1 O TYR H 117 N ARG H 101
SHEET 1 W 4 SER H 135 LEU H 139 0
SHEET 2 W 4 THR H 150 TYR H 160 -1 O GLY H 154 N LEU H 139
SHEET 3 W 4 TYR H 191 PRO H 200 -1 O TYR H 191 N TYR H 160
SHEET 4 W 4 VAL H 178 THR H 180 -1 N HIS H 179 O VAL H 196
SHEET 1 X 4 SER H 135 LEU H 139 0
SHEET 2 X 4 THR H 150 TYR H 160 -1 O GLY H 154 N LEU H 139
SHEET 3 X 4 TYR H 191 PRO H 200 -1 O TYR H 191 N TYR H 160
SHEET 4 X 4 VAL H 184 LEU H 185 -1 N VAL H 184 O SER H 192
SHEET 1 Y 3 THR H 166 TRP H 169 0
SHEET 2 Y 3 ILE H 210 HIS H 215 -1 O ASN H 212 N SER H 168
SHEET 3 Y 3 THR H 220 LYS H 225 -1 O VAL H 222 N VAL H 213
SHEET 1 Z 4 GLN A 6 SER A 10 0
SHEET 2 Z 4 LEU A 21 SER A 28 -1 O ALA A 26 N VAL A 8
SHEET 3 Z 4 THR A 81 MET A 86 -1 O MET A 86 N LEU A 21
SHEET 4 Z 4 PHE A 71 ASP A 76 -1 N SER A 74 O TYR A 83
SHEET 1 AA 6 GLY A 13 VAL A 15 0
SHEET 2 AA 6 THR A 122 VAL A 126 1 O THR A 125 N VAL A 15
SHEET 3 AA 6 ALA A 95 TYR A 103 -1 N TYR A 97 O THR A 122
SHEET 4 AA 6 SER A 35 GLN A 42 -1 N HIS A 38 O ALA A 100
SHEET 5 AA 6 LEU A 48 ILE A 54 -1 O ALA A 52 N TRP A 39
SHEET 6 AA 6 THR A 61 TYR A 63 -1 O SER A 62 N TYR A 53
SHEET 1 AB 4 GLY A 13 VAL A 15 0
SHEET 2 AB 4 THR A 122 VAL A 126 1 O THR A 125 N VAL A 15
SHEET 3 AB 4 ALA A 95 TYR A 103 -1 N TYR A 97 O THR A 122
SHEET 4 AB 4 TYR A 117 TRP A 118 -1 O TYR A 117 N ARG A 101
SHEET 1 AC 4 SER A 135 LEU A 139 0
SHEET 2 AC 4 THR A 150 TYR A 160 -1 O LYS A 158 N SER A 135
SHEET 3 AC 4 TYR A 191 PRO A 200 -1 O TYR A 191 N TYR A 160
SHEET 4 AC 4 VAL A 178 THR A 180 -1 N HIS A 179 O VAL A 196
SHEET 1 AD 4 SER A 135 LEU A 139 0
SHEET 2 AD 4 THR A 150 TYR A 160 -1 O LYS A 158 N SER A 135
SHEET 3 AD 4 TYR A 191 PRO A 200 -1 O TYR A 191 N TYR A 160
SHEET 4 AD 4 VAL A 184 LEU A 185 -1 N VAL A 184 O SER A 192
SHEET 1 AE 3 THR A 166 TRP A 169 0
SHEET 2 AE 3 ILE A 210 HIS A 215 -1 O ASN A 212 N SER A 168
SHEET 3 AE 3 THR A 220 LYS A 225 -1 O THR A 220 N HIS A 215
SSBOND 1 CYS L 24 CYS L 89 1555 1555 2.09
SSBOND 2 CYS L 137 CYS L 197 1555 1555 2.06
SSBOND 3 CYS H 25 CYS H 99 1555 1555 2.08
SSBOND 4 CYS H 155 CYS H 211 1555 1555 2.03
SSBOND 5 CYS B 24 CYS B 89 1555 1555 2.09
SSBOND 6 CYS B 137 CYS B 197 1555 1555 2.05
SSBOND 7 CYS A 25 CYS A 99 1555 1555 2.11
SSBOND 8 CYS A 155 CYS A 211 1555 1555 2.01
SSBOND 9 CYS R 12 CYS R 22 1555 1555 2.14
SSBOND 10 CYS R 51 CYS R 62 1555 1555 2.08
SSBOND 11 CYS C 12 CYS C 22 1555 1555 2.12
SSBOND 12 CYS C 51 CYS C 62 1555 1555 2.07
LINK OG SER H 78 CA CA H 301 1555 1555 1.85
LINK CA CA H 301 OG SER A 78 1555 1555 2.50
CISPEP 1 SER L 8 PRO L 9 0 -6.57
CISPEP 2 TYR L 143 PRO L 144 0 5.31
CISPEP 3 LYS H 144 SER H 145 0 20.49
CISPEP 4 LEU H 156 VAL H 157 0 20.39
CISPEP 5 PHE H 161 PRO H 162 0 -5.77
CISPEP 6 GLU H 163 PRO H 164 0 -4.02
CISPEP 7 SER B 8 PRO B 9 0 -13.70
CISPEP 8 TYR B 143 PRO B 144 0 6.29
CISPEP 9 LEU A 156 VAL A 157 0 18.92
CISPEP 10 PHE A 161 PRO A 162 0 -5.70
CISPEP 11 GLU A 163 PRO A 164 0 -7.20
CISPEP 12 GLY R 27 THR R 28 0 -22.02
CISPEP 13 THR R 137 GLY R 138 0 27.90
CISPEP 14 LEU R 172 HIS R 173 0 12.32
CISPEP 15 PRO C 4 GLY C 5 0 7.03
CISPEP 16 PRO C 26 GLY C 27 0 15.90
CISPEP 17 GLY C 30 GLY C 31 0 -4.25
CISPEP 18 THR C 137 GLY C 138 0 15.60
CISPEP 19 ASP C 187 HIS C 188 0 12.20
SITE 1 AC1 3 TYR A 111 LYS R 11 TRP R 23
SITE 1 AC2 4 LYS C 11 TRP C 23 TYR L 50 SER L 51
SITE 1 AC3 5 VAL L 149 GLN L 150 TRP L 151 GLN L 158
SITE 2 AC3 5 SER L 159
SITE 1 AC4 2 ASP B 2 TYR B 95
SITE 1 AC5 4 SER A 78 ASP H 76 SER H 78 MET R 208
SITE 1 AC6 8 GLN C 102 PRO C 103 PRO C 105 ALA C 193
SITE 2 AC6 8 TYR H 107 TRP H 108 ASN H 109 ALA H 110
SITE 1 AC7 9 TYR A 107 TRP A 108 ASN A 109 ALA A 110
SITE 2 AC7 9 GLN R 102 PRO R 103 ASP R 104 PRO R 105
SITE 3 AC7 9 ALA R 193
CRYST1 285.826 285.826 62.248 90.00 90.00 120.00 P 61 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 0.003499 0.002020 0.000000 0.00000
SCALE2 0.000000 0.004040 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016065 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
