HEADER TRANSFERASE/TRANSFERASE INHIBITOR 16-AUG-14 4W50
TITLE STRUCTURE OF THE EPHA4 LBD IN COMPLEX WITH PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN, UNP RESIDUES 29-204;
COMPND 5 SYNONYM: EPH-LIKE KINASE 8,HEK8,TYROSINE-PROTEIN KINASE TYRO1,
COMPND 6 TYROSINE-PROTEIN KINASE RECEPTOR SEK;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: APY PEPTIDE;
COMPND 12 CHAIN: E, F, G, H;
COMPND 13 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: EPHA4, HEK8, SEK, TYRO1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI 2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: NKI HIS-3C-LIC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630
KEYWDS PROTEIN-INHIBITOR COMPLEX, LIGAND BINDING DOMAIN, SIGNAL
KEYWDS 2 TRANSDUCTION, RECEPTOR-TYROSINE KINASE, CYCLIC PEPTIDE, EPHA4, PHAGE
KEYWDS 3 DISPLAY, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.C.LECHTENBERG,P.D.MACE,S.J.RIEDL
REVDAT 7 27-SEP-23 4W50 1 REMARK
REVDAT 6 04-DEC-19 4W50 1 REMARK
REVDAT 5 22-NOV-17 4W50 1 REMARK
REVDAT 4 06-SEP-17 4W50 1 SOURCE REMARK
REVDAT 3 14-JAN-15 4W50 1 REMARK
REVDAT 2 07-JAN-15 4W50 1 JRNL
REVDAT 1 08-OCT-14 4W50 0
JRNL AUTH I.LAMBERTO,B.C.LECHTENBERG,E.J.OLSON,P.D.MACE,P.E.DAWSON,
JRNL AUTH 2 S.J.RIEDL,E.B.PASQUALE
JRNL TITL DEVELOPMENT AND STRUCTURAL ANALYSIS OF A NANOMOLAR CYCLIC
JRNL TITL 2 PEPTIDE ANTAGONIST FOR THE EPHA4 RECEPTOR.
JRNL REF ACS CHEM.BIOL. V. 9 2787 2014
JRNL REFN ESSN 1554-8937
JRNL PMID 25268696
JRNL DOI 10.1021/CB500677X
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
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) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 3 NUMBER OF REFLECTIONS : 27253
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1346
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) : 2.42
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.48
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1765
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 95
REMARK 3 BIN FREE R VALUE : 0.4230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6090
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 176
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.62000
REMARK 3 B22 (A**2) : 27.25000
REMARK 3 B33 (A**2) : -22.63000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 16.89000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.295
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.061
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.791
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6276 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 5856 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8484 ; 1.468 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13456 ; 0.734 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 746 ; 7.796 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 312 ;39.641 ;24.103
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1080 ;16.947 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;12.899 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 916 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7070 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1474 ; 0.001 ; 0.020
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): 3010 ; 0.921 ; 2.605
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3009 ; 0.921 ; 2.605
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3750 ; 1.645 ; 3.900
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 : NULL
REMARK 3
REMARK 3 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.664
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H,-K,L
REMARK 3 TWIN FRACTION : 0.336
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
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 : A 28 A 204
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8670 -18.3155 -5.7050
REMARK 3 T TENSOR
REMARK 3 T11: 0.2514 T22: 0.0082
REMARK 3 T33: 0.1558 T12: 0.0128
REMARK 3 T13: -0.1969 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 1.1030 L22: 0.9989
REMARK 3 L33: 2.7876 L12: -0.2431
REMARK 3 L13: -0.8147 L23: 0.3904
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: -0.0520 S13: -0.0266
REMARK 3 S21: 0.0464 S22: 0.0535 S23: -0.0254
REMARK 3 S31: 0.1489 S32: 0.1092 S33: -0.0538
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 : B 28 B 204
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6244 1.4111 36.7358
REMARK 3 T TENSOR
REMARK 3 T11: 0.2104 T22: 0.0092
REMARK 3 T33: 0.1414 T12: 0.0298
REMARK 3 T13: -0.1592 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.1236 L22: 0.8728
REMARK 3 L33: 2.9532 L12: -0.1613
REMARK 3 L13: -0.0540 L23: -0.5686
REMARK 3 S TENSOR
REMARK 3 S11: 0.0555 S12: -0.0380 S13: -0.0589
REMARK 3 S21: -0.0052 S22: 0.0238 S23: 0.0025
REMARK 3 S31: -0.1868 S32: -0.1191 S33: -0.0793
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 : C 28 C 204
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5702 -27.0246 38.5232
REMARK 3 T TENSOR
REMARK 3 T11: 0.2287 T22: 0.0171
REMARK 3 T33: 0.1529 T12: 0.0229
REMARK 3 T13: -0.1605 T23: -0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 1.4261 L22: 1.6907
REMARK 3 L33: 2.7725 L12: -0.4658
REMARK 3 L13: 0.2723 L23: -0.3160
REMARK 3 S TENSOR
REMARK 3 S11: 0.1238 S12: 0.0532 S13: -0.0160
REMARK 3 S21: -0.1939 S22: -0.1580 S23: -0.0326
REMARK 3 S31: 0.2854 S32: -0.0361 S33: 0.0342
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 : D 28 D 204
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7228 10.3400 -3.5005
REMARK 3 T TENSOR
REMARK 3 T11: 0.2223 T22: 0.0156
REMARK 3 T33: 0.1491 T12: 0.0211
REMARK 3 T13: -0.1418 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 1.8098 L22: 1.4904
REMARK 3 L33: 3.2834 L12: -0.5838
REMARK 3 L13: -0.9804 L23: 0.1193
REMARK 3 S TENSOR
REMARK 3 S11: 0.1501 S12: -0.0682 S13: 0.0730
REMARK 3 S21: -0.1452 S22: -0.0479 S23: 0.0036
REMARK 3 S31: -0.3987 S32: -0.1111 S33: -0.1022
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 : E 1 E 12
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6074 -23.4177 -22.2079
REMARK 3 T TENSOR
REMARK 3 T11: 0.0951 T22: 0.0801
REMARK 3 T33: 0.0672 T12: -0.0142
REMARK 3 T13: -0.0702 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 0.0234 L22: 7.5830
REMARK 3 L33: 8.0005 L12: -0.0894
REMARK 3 L13: -0.0100 L23: -3.8654
REMARK 3 S TENSOR
REMARK 3 S11: 0.0378 S12: -0.0252 S13: -0.0377
REMARK 3 S21: -0.5107 S22: -0.0458 S23: 0.1470
REMARK 3 S31: 0.0937 S32: -0.1010 S33: 0.0080
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 : F 1 F 12
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5234 17.1385 -19.6639
REMARK 3 T TENSOR
REMARK 3 T11: 0.1920 T22: 0.1151
REMARK 3 T33: 0.0466 T12: 0.0457
REMARK 3 T13: -0.0220 T23: 0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 0.4290 L22: 7.3632
REMARK 3 L33: 3.0231 L12: -1.2534
REMARK 3 L13: -0.7263 L23: -0.3862
REMARK 3 S TENSOR
REMARK 3 S11: 0.1354 S12: -0.0427 S13: 0.0125
REMARK 3 S21: -0.1475 S22: -0.0655 S23: -0.0597
REMARK 3 S31: -0.3403 S32: 0.1661 S33: -0.0700
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 1 G 12
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0521 -33.4688 22.4825
REMARK 3 T TENSOR
REMARK 3 T11: 0.1759 T22: 0.1191
REMARK 3 T33: 0.0368 T12: 0.0645
REMARK 3 T13: -0.0094 T23: -0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 3.4038 L22: 12.6611
REMARK 3 L33: 0.6497 L12: 0.9207
REMARK 3 L13: 0.0985 L23: -2.8024
REMARK 3 S TENSOR
REMARK 3 S11: 0.1574 S12: 0.2433 S13: -0.1180
REMARK 3 S21: -0.3656 S22: -0.1524 S23: 0.0092
REMARK 3 S31: 0.1025 S32: 0.0495 S33: -0.0050
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 12
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8320 6.7100 20.2406
REMARK 3 T TENSOR
REMARK 3 T11: 0.1719 T22: 0.1267
REMARK 3 T33: 0.0756 T12: -0.0004
REMARK 3 T13: -0.0819 T23: 0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 6.7291 L22: 7.8709
REMARK 3 L33: 4.3418 L12: 1.9302
REMARK 3 L13: -2.4127 L23: 4.3227
REMARK 3 S TENSOR
REMARK 3 S11: -0.0152 S12: 0.3199 S13: -0.0001
REMARK 3 S21: -0.2203 S22: 0.1236 S23: -0.2063
REMARK 3 S31: -0.1502 S32: -0.0258 S33: -0.1084
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4W50 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000203216.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.1
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27280
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.420
REMARK 200 RESOLUTION RANGE LOW (A) : 50.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.42
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.24600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.4
REMARK 200 STARTING MODEL: 2WO1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MGCL2, 0.1M TRIS PH8.5, 25%
REMARK 280 PEG3350, 4% 1,3-BUTANEDIOL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 63.84500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 300 REMARK: CHAINS A+E
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: 1770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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: 1890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F
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: 3
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: 1480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
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: 4
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: 1680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
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 GLY A 26
REMARK 465 PRO A 27
REMARK 465 GLY B 26
REMARK 465 PRO B 27
REMARK 465 GLY C 26
REMARK 465 PRO C 27
REMARK 465 GLY D 26
REMARK 465 PRO D 27
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 ALA C 204 CA C O CB
REMARK 470 ALA D 204 CA C O CB
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 OG SER C 196 O HOH C 417 2.13
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 ASN A 29 10.60 -140.20
REMARK 500 CYS A 73 52.42 -151.85
REMARK 500 SER A 79 68.44 33.29
REMARK 500 ASN A 81 74.82 -156.00
REMARK 500 GLU A 92 -124.84 37.48
REMARK 500 MET A 115 61.93 -160.87
REMARK 500 LYS A 133 36.37 -154.98
REMARK 500 ASP A 151 -141.83 -103.86
REMARK 500 CYS B 73 43.59 -153.39
REMARK 500 ASN B 74 44.11 -77.86
REMARK 500 GLU B 92 -132.35 55.74
REMARK 500 ARG B 135 -71.72 -93.81
REMARK 500 ASP B 151 -151.98 -108.76
REMARK 500 CYS C 73 55.66 -160.96
REMARK 500 ASN C 81 86.71 -157.55
REMARK 500 GLU C 92 -130.26 54.24
REMARK 500 MET C 115 -119.65 -125.12
REMARK 500 LYS C 133 58.69 -118.60
REMARK 500 ILE C 145 -63.92 -92.25
REMARK 500 ASP C 151 -162.09 -123.75
REMARK 500 ASP D 61 -154.44 -93.61
REMARK 500 ASN D 64 11.04 82.31
REMARK 500 VAL D 72 126.74 -173.27
REMARK 500 CYS D 73 61.97 -151.35
REMARK 500 ASN D 74 57.02 -93.23
REMARK 500 SER D 79 75.87 47.88
REMARK 500 ASN D 81 60.57 -158.99
REMARK 500 GLU D 92 -133.09 54.70
REMARK 500 PRO D 112 -171.39 -67.37
REMARK 500 ASP D 151 -143.61 -108.80
REMARK 500 SER E 11 89.94 -170.60
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 LYS A 203 ALA A 204 -147.97
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 BU2 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BU2 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BU2 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BU2 D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4W4Z RELATED DB: PDB
DBREF 4W50 A 29 204 UNP P54764 EPHA4_HUMAN 29 204
DBREF 4W50 B 29 204 UNP P54764 EPHA4_HUMAN 29 204
DBREF 4W50 C 29 204 UNP P54764 EPHA4_HUMAN 29 204
DBREF 4W50 D 29 204 UNP P54764 EPHA4_HUMAN 29 204
DBREF 4W50 E 1 12 PDB 4W50 4W50 1 12
DBREF 4W50 F 1 12 PDB 4W50 4W50 1 12
DBREF 4W50 G 1 12 PDB 4W50 4W50 1 12
DBREF 4W50 H 1 12 PDB 4W50 4W50 1 12
SEQADV 4W50 GLY A 26 UNP P54764 EXPRESSION TAG
SEQADV 4W50 PRO A 27 UNP P54764 EXPRESSION TAG
SEQADV 4W50 GLY A 28 UNP P54764 EXPRESSION TAG
SEQADV 4W50 ALA A 204 UNP P54764 CYS 204 ENGINEERED MUTATION
SEQADV 4W50 GLY B 26 UNP P54764 EXPRESSION TAG
SEQADV 4W50 PRO B 27 UNP P54764 EXPRESSION TAG
SEQADV 4W50 GLY B 28 UNP P54764 EXPRESSION TAG
SEQADV 4W50 ALA B 204 UNP P54764 CYS 204 ENGINEERED MUTATION
SEQADV 4W50 GLY C 26 UNP P54764 EXPRESSION TAG
SEQADV 4W50 PRO C 27 UNP P54764 EXPRESSION TAG
SEQADV 4W50 GLY C 28 UNP P54764 EXPRESSION TAG
SEQADV 4W50 ALA C 204 UNP P54764 CYS 204 ENGINEERED MUTATION
SEQADV 4W50 GLY D 26 UNP P54764 EXPRESSION TAG
SEQADV 4W50 PRO D 27 UNP P54764 EXPRESSION TAG
SEQADV 4W50 GLY D 28 UNP P54764 EXPRESSION TAG
SEQADV 4W50 ALA D 204 UNP P54764 CYS 204 ENGINEERED MUTATION
SEQRES 1 A 179 GLY PRO GLY ASN GLU VAL THR LEU LEU ASP SER ARG SER
SEQRES 2 A 179 VAL GLN GLY GLU LEU GLY TRP ILE ALA SER PRO LEU GLU
SEQRES 3 A 179 GLY GLY TRP GLU GLU VAL SER ILE MET ASP GLU LYS ASN
SEQRES 4 A 179 THR PRO ILE ARG THR TYR GLN VAL CYS ASN VAL MET GLU
SEQRES 5 A 179 PRO SER GLN ASN ASN TRP LEU ARG THR ASP TRP ILE THR
SEQRES 6 A 179 ARG GLU GLY ALA GLN ARG VAL TYR ILE GLU ILE LYS PHE
SEQRES 7 A 179 THR LEU ARG ASP CYS ASN SER LEU PRO GLY VAL MET GLY
SEQRES 8 A 179 THR CYS LYS GLU THR PHE ASN LEU TYR TYR TYR GLU SER
SEQRES 9 A 179 ASP ASN ASP LYS GLU ARG PHE ILE ARG GLU ASN GLN PHE
SEQRES 10 A 179 VAL LYS ILE ASP THR ILE ALA ALA ASP GLU SER PHE THR
SEQRES 11 A 179 GLN VAL ASP ILE GLY ASP ARG ILE MET LYS LEU ASN THR
SEQRES 12 A 179 GLU ILE ARG ASP VAL GLY PRO LEU SER LYS LYS GLY PHE
SEQRES 13 A 179 TYR LEU ALA PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU
SEQRES 14 A 179 VAL SER VAL ARG VAL PHE TYR LYS LYS ALA
SEQRES 1 B 179 GLY PRO GLY ASN GLU VAL THR LEU LEU ASP SER ARG SER
SEQRES 2 B 179 VAL GLN GLY GLU LEU GLY TRP ILE ALA SER PRO LEU GLU
SEQRES 3 B 179 GLY GLY TRP GLU GLU VAL SER ILE MET ASP GLU LYS ASN
SEQRES 4 B 179 THR PRO ILE ARG THR TYR GLN VAL CYS ASN VAL MET GLU
SEQRES 5 B 179 PRO SER GLN ASN ASN TRP LEU ARG THR ASP TRP ILE THR
SEQRES 6 B 179 ARG GLU GLY ALA GLN ARG VAL TYR ILE GLU ILE LYS PHE
SEQRES 7 B 179 THR LEU ARG ASP CYS ASN SER LEU PRO GLY VAL MET GLY
SEQRES 8 B 179 THR CYS LYS GLU THR PHE ASN LEU TYR TYR TYR GLU SER
SEQRES 9 B 179 ASP ASN ASP LYS GLU ARG PHE ILE ARG GLU ASN GLN PHE
SEQRES 10 B 179 VAL LYS ILE ASP THR ILE ALA ALA ASP GLU SER PHE THR
SEQRES 11 B 179 GLN VAL ASP ILE GLY ASP ARG ILE MET LYS LEU ASN THR
SEQRES 12 B 179 GLU ILE ARG ASP VAL GLY PRO LEU SER LYS LYS GLY PHE
SEQRES 13 B 179 TYR LEU ALA PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU
SEQRES 14 B 179 VAL SER VAL ARG VAL PHE TYR LYS LYS ALA
SEQRES 1 C 179 GLY PRO GLY ASN GLU VAL THR LEU LEU ASP SER ARG SER
SEQRES 2 C 179 VAL GLN GLY GLU LEU GLY TRP ILE ALA SER PRO LEU GLU
SEQRES 3 C 179 GLY GLY TRP GLU GLU VAL SER ILE MET ASP GLU LYS ASN
SEQRES 4 C 179 THR PRO ILE ARG THR TYR GLN VAL CYS ASN VAL MET GLU
SEQRES 5 C 179 PRO SER GLN ASN ASN TRP LEU ARG THR ASP TRP ILE THR
SEQRES 6 C 179 ARG GLU GLY ALA GLN ARG VAL TYR ILE GLU ILE LYS PHE
SEQRES 7 C 179 THR LEU ARG ASP CYS ASN SER LEU PRO GLY VAL MET GLY
SEQRES 8 C 179 THR CYS LYS GLU THR PHE ASN LEU TYR TYR TYR GLU SER
SEQRES 9 C 179 ASP ASN ASP LYS GLU ARG PHE ILE ARG GLU ASN GLN PHE
SEQRES 10 C 179 VAL LYS ILE ASP THR ILE ALA ALA ASP GLU SER PHE THR
SEQRES 11 C 179 GLN VAL ASP ILE GLY ASP ARG ILE MET LYS LEU ASN THR
SEQRES 12 C 179 GLU ILE ARG ASP VAL GLY PRO LEU SER LYS LYS GLY PHE
SEQRES 13 C 179 TYR LEU ALA PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU
SEQRES 14 C 179 VAL SER VAL ARG VAL PHE TYR LYS LYS ALA
SEQRES 1 D 179 GLY PRO GLY ASN GLU VAL THR LEU LEU ASP SER ARG SER
SEQRES 2 D 179 VAL GLN GLY GLU LEU GLY TRP ILE ALA SER PRO LEU GLU
SEQRES 3 D 179 GLY GLY TRP GLU GLU VAL SER ILE MET ASP GLU LYS ASN
SEQRES 4 D 179 THR PRO ILE ARG THR TYR GLN VAL CYS ASN VAL MET GLU
SEQRES 5 D 179 PRO SER GLN ASN ASN TRP LEU ARG THR ASP TRP ILE THR
SEQRES 6 D 179 ARG GLU GLY ALA GLN ARG VAL TYR ILE GLU ILE LYS PHE
SEQRES 7 D 179 THR LEU ARG ASP CYS ASN SER LEU PRO GLY VAL MET GLY
SEQRES 8 D 179 THR CYS LYS GLU THR PHE ASN LEU TYR TYR TYR GLU SER
SEQRES 9 D 179 ASP ASN ASP LYS GLU ARG PHE ILE ARG GLU ASN GLN PHE
SEQRES 10 D 179 VAL LYS ILE ASP THR ILE ALA ALA ASP GLU SER PHE THR
SEQRES 11 D 179 GLN VAL ASP ILE GLY ASP ARG ILE MET LYS LEU ASN THR
SEQRES 12 D 179 GLU ILE ARG ASP VAL GLY PRO LEU SER LYS LYS GLY PHE
SEQRES 13 D 179 TYR LEU ALA PHE GLN ASP VAL GLY ALA CYS ILE ALA LEU
SEQRES 14 D 179 VAL SER VAL ARG VAL PHE TYR LYS LYS ALA
SEQRES 1 E 12 ALA PRO TYR CYS VAL TYR ARG GLY SER TRP SER CYS
SEQRES 1 F 12 ALA PRO TYR CYS VAL TYR ARG GLY SER TRP SER CYS
SEQRES 1 G 12 ALA PRO TYR CYS VAL TYR ARG GLY SER TRP SER CYS
SEQRES 1 H 12 ALA PRO TYR CYS VAL TYR ARG GLY SER TRP SER CYS
HET BU2 A 301 6
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HET BU2 B 301 6
HET GOL B 302 6
HET BU2 C 301 6
HET GOL C 302 6
HET BU2 D 301 6
HET GOL D 302 6
HETNAM BU2 1,3-BUTANEDIOL
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 BU2 4(C4 H10 O2)
FORMUL 10 GOL 6(C3 H8 O3)
FORMUL 19 HOH *176(H2 O)
HELIX 1 AA1 ARG A 37 VAL A 39 5 3
HELIX 2 AA2 ARG A 138 PHE A 142 5 5
HELIX 3 AA3 ARG B 37 VAL B 39 5 3
HELIX 4 AA4 ASP B 107 LEU B 111 5 5
HELIX 5 AA5 ARG C 37 VAL C 39 5 3
HELIX 6 AA6 ARG C 138 PHE C 142 5 5
HELIX 7 AA7 ARG D 37 VAL D 39 5 3
HELIX 8 AA8 ASP D 107 LEU D 111 5 5
HELIX 9 AA9 ARG D 138 PHE D 142 5 5
SHEET 1 AA110 GLU A 30 ASP A 35 0
SHEET 2 AA110 ILE A 192 LYS A 202 -1 O VAL A 199 N LEU A 34
SHEET 3 AA110 VAL A 97 LEU A 105 -1 N TYR A 98 O PHE A 200
SHEET 4 AA110 ILE A 163 VAL A 173 -1 O ARG A 171 N ILE A 99
SHEET 5 AA110 PHE A 154 ASP A 158 -1 N THR A 155 O LEU A 166
SHEET 6 AA110 SER D 153 ASP D 158 -1 O PHE D 154 N PHE A 154
SHEET 7 AA110 ILE D 163 VAL D 173 -1 O LEU D 166 N THR D 155
SHEET 8 AA110 VAL D 97 LEU D 105 -1 N ILE D 99 O ARG D 171
SHEET 9 AA110 ILE D 192 LYS D 202 -1 O ARG D 198 N GLU D 100
SHEET 10 AA110 GLU D 30 ASP D 35 -1 N LEU D 33 O VAL D 199
SHEET 1 AA212 GLU A 55 MET A 60 0
SHEET 2 AA212 PRO A 66 VAL A 72 -1 O THR A 69 N VAL A 57
SHEET 3 AA212 ILE A 192 LYS A 202 -1 O LEU A 194 N TYR A 70
SHEET 4 AA212 VAL A 97 LEU A 105 -1 N TYR A 98 O PHE A 200
SHEET 5 AA212 ILE A 163 VAL A 173 -1 O ARG A 171 N ILE A 99
SHEET 6 AA212 PHE A 154 ASP A 158 -1 N THR A 155 O LEU A 166
SHEET 7 AA212 SER D 153 ASP D 158 -1 O PHE D 154 N PHE A 154
SHEET 8 AA212 ILE D 163 VAL D 173 -1 O LEU D 166 N THR D 155
SHEET 9 AA212 VAL D 97 LEU D 105 -1 N ILE D 99 O ARG D 171
SHEET 10 AA212 ILE D 192 LYS D 202 -1 O ARG D 198 N GLU D 100
SHEET 11 AA212 ILE D 67 VAL D 72 -1 N TYR D 70 O LEU D 194
SHEET 12 AA212 GLU D 55 ILE D 59 -1 N GLU D 55 O GLN D 71
SHEET 1 AA3 4 ILE A 46 SER A 48 0
SHEET 2 AA3 4 ASN A 82 ARG A 85 -1 O ARG A 85 N ILE A 46
SHEET 3 AA3 4 GLY A 180 ASP A 187 -1 O PHE A 185 N LEU A 84
SHEET 4 AA3 4 ILE A 89 THR A 90 -1 N ILE A 89 O PHE A 181
SHEET 1 AA4 5 ILE A 46 SER A 48 0
SHEET 2 AA4 5 ASN A 82 ARG A 85 -1 O ARG A 85 N ILE A 46
SHEET 3 AA4 5 GLY A 180 ASP A 187 -1 O PHE A 185 N LEU A 84
SHEET 4 AA4 5 THR A 121 SER A 129 -1 N ASN A 123 O GLN A 186
SHEET 5 AA4 5 VAL A 143 ALA A 149 -1 O ILE A 148 N PHE A 122
SHEET 1 AA510 GLU B 30 ASP B 35 0
SHEET 2 AA510 CYS B 191 LYS B 202 -1 O VAL B 199 N LEU B 33
SHEET 3 AA510 VAL B 97 ARG B 106 -1 N GLU B 100 O ARG B 198
SHEET 4 AA510 ILE B 163 VAL B 173 -1 O ARG B 171 N ILE B 99
SHEET 5 AA510 PHE B 154 ASP B 158 -1 N VAL B 157 O MET B 164
SHEET 6 AA510 SER C 153 ASP C 158 -1 O PHE C 154 N PHE B 154
SHEET 7 AA510 ILE C 163 VAL C 173 -1 O LEU C 166 N THR C 155
SHEET 8 AA510 VAL C 97 LEU C 105 -1 N ILE C 99 O ARG C 171
SHEET 9 AA510 ILE C 192 LYS C 202 -1 O ARG C 198 N GLU C 100
SHEET 10 AA510 GLU C 30 ASP C 35 -1 N LEU C 33 O VAL C 199
SHEET 1 AA612 GLU B 55 MET B 60 0
SHEET 2 AA612 PRO B 66 VAL B 72 -1 O ILE B 67 N ILE B 59
SHEET 3 AA612 CYS B 191 LYS B 202 -1 O LEU B 194 N TYR B 70
SHEET 4 AA612 VAL B 97 ARG B 106 -1 N GLU B 100 O ARG B 198
SHEET 5 AA612 ILE B 163 VAL B 173 -1 O ARG B 171 N ILE B 99
SHEET 6 AA612 PHE B 154 ASP B 158 -1 N VAL B 157 O MET B 164
SHEET 7 AA612 SER C 153 ASP C 158 -1 O PHE C 154 N PHE B 154
SHEET 8 AA612 ILE C 163 VAL C 173 -1 O LEU C 166 N THR C 155
SHEET 9 AA612 VAL C 97 LEU C 105 -1 N ILE C 99 O ARG C 171
SHEET 10 AA612 ILE C 192 LYS C 202 -1 O ARG C 198 N GLU C 100
SHEET 11 AA612 ILE C 67 VAL C 72 -1 N TYR C 70 O LEU C 194
SHEET 12 AA612 GLU C 55 ILE C 59 -1 N GLU C 55 O GLN C 71
SHEET 1 AA7 4 ILE B 46 SER B 48 0
SHEET 2 AA7 4 ASN B 82 ARG B 85 -1 O TRP B 83 N SER B 48
SHEET 3 AA7 4 GLY B 180 ASP B 187 -1 O ASP B 187 N ASN B 82
SHEET 4 AA7 4 ILE B 89 THR B 90 -1 N ILE B 89 O PHE B 181
SHEET 1 AA8 5 ILE B 46 SER B 48 0
SHEET 2 AA8 5 ASN B 82 ARG B 85 -1 O TRP B 83 N SER B 48
SHEET 3 AA8 5 GLY B 180 ASP B 187 -1 O ASP B 187 N ASN B 82
SHEET 4 AA8 5 THR B 121 SER B 129 -1 N ASN B 123 O GLN B 186
SHEET 5 AA8 5 VAL B 143 ALA B 149 -1 O VAL B 143 N TYR B 126
SHEET 1 AA9 4 ILE C 46 SER C 48 0
SHEET 2 AA9 4 ASN C 82 ARG C 85 -1 O TRP C 83 N SER C 48
SHEET 3 AA9 4 GLY C 180 ASP C 187 -1 O ASP C 187 N ASN C 82
SHEET 4 AA9 4 ILE C 89 THR C 90 -1 N ILE C 89 O PHE C 181
SHEET 1 AB1 5 ILE C 46 SER C 48 0
SHEET 2 AB1 5 ASN C 82 ARG C 85 -1 O TRP C 83 N SER C 48
SHEET 3 AB1 5 GLY C 180 ASP C 187 -1 O ASP C 187 N ASN C 82
SHEET 4 AB1 5 THR C 121 SER C 129 -1 N TYR C 125 O ALA C 184
SHEET 5 AB1 5 VAL C 143 ALA C 149 -1 O VAL C 143 N TYR C 126
SHEET 1 AB2 4 ILE D 46 SER D 48 0
SHEET 2 AB2 4 ASN D 82 ARG D 85 -1 O TRP D 83 N SER D 48
SHEET 3 AB2 4 GLY D 180 ASP D 187 -1 O PHE D 185 N LEU D 84
SHEET 4 AB2 4 ILE D 89 THR D 90 -1 N ILE D 89 O PHE D 181
SHEET 1 AB3 5 ILE D 46 SER D 48 0
SHEET 2 AB3 5 ASN D 82 ARG D 85 -1 O TRP D 83 N SER D 48
SHEET 3 AB3 5 GLY D 180 ASP D 187 -1 O PHE D 185 N LEU D 84
SHEET 4 AB3 5 THR D 121 SER D 129 -1 N ASN D 123 O GLN D 186
SHEET 5 AB3 5 VAL D 143 ALA D 149 -1 O ILE D 148 N PHE D 122
SHEET 1 AB4 2 VAL F 5 TYR F 6 0
SHEET 2 AB4 2 TRP F 10 SER F 11 -1 O SER F 11 N VAL F 5
SHEET 1 AB5 2 VAL G 5 TYR G 6 0
SHEET 2 AB5 2 TRP G 10 SER G 11 -1 O SER G 11 N VAL G 5
SHEET 1 AB6 2 VAL H 5 TYR H 6 0
SHEET 2 AB6 2 TRP H 10 SER H 11 -1 O SER H 11 N VAL H 5
SSBOND 1 CYS A 73 CYS A 191 1555 1555 2.05
SSBOND 2 CYS A 108 CYS A 118 1555 1555 2.07
SSBOND 3 CYS B 73 CYS B 191 1555 1555 2.09
SSBOND 4 CYS B 108 CYS B 118 1555 1555 2.07
SSBOND 5 CYS C 73 CYS C 191 1555 1555 2.07
SSBOND 6 CYS C 108 CYS C 118 1555 1555 2.07
SSBOND 7 CYS D 73 CYS D 191 1555 1555 2.06
SSBOND 8 CYS D 108 CYS D 118 1555 1555 2.05
SSBOND 9 CYS E 4 CYS E 12 1555 1555 2.07
SSBOND 10 CYS F 4 CYS F 12 1555 1555 2.07
SSBOND 11 CYS G 4 CYS G 12 1555 1555 2.05
SSBOND 12 CYS H 4 CYS H 12 1555 1555 2.05
CISPEP 1 SER A 48 PRO A 49 0 7.85
CISPEP 2 GLY A 174 PRO A 175 0 2.61
CISPEP 3 SER B 48 PRO B 49 0 0.89
CISPEP 4 GLY B 174 PRO B 175 0 3.09
CISPEP 5 SER C 48 PRO C 49 0 -0.85
CISPEP 6 GLY C 174 PRO C 175 0 -3.83
CISPEP 7 SER D 48 PRO D 49 0 4.91
CISPEP 8 GLY D 174 PRO D 175 0 -0.99
SITE 1 AC1 6 GLU A 30 ILE A 170 LYS A 202 ILE D 170
SITE 2 AC1 6 ARG D 171 ASP D 172
SITE 1 AC2 4 ARG A 85 PHE A 136 ILE A 137 HOH A 439
SITE 1 AC3 3 GLU A 62 ASP A 158 GLY A 160
SITE 1 AC4 3 ARG A 96 GLY A 174 GLY B 160
SITE 1 AC5 4 ILE B 170 ASP B 172 ILE C 170 LYS C 202
SITE 1 AC6 4 ARG B 85 ARG B 135 PHE B 136 ILE B 137
SITE 1 AC7 5 GLU B 30 ARG B 198 ASP C 151 SER C 153
SITE 2 AC7 5 GLU C 169
SITE 1 AC8 5 ILE C 46 SER C 48 ILE C 137 GLU C 139
SITE 2 AC8 5 PHE C 142
SITE 1 AC9 5 ASP A 151 SER A 153 GLU D 30 GLU D 100
SITE 2 AC9 5 ARG D 198
SITE 1 AD1 4 TRP D 83 PHE D 136 ILE D 137 GLU D 139
CRYST1 36.270 127.690 84.569 90.00 90.00 90.00 P 1 21 1 8
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 0.027571 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007831 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011825 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
