HEADER TRANSFERASE/INHIBITOR 05-MAY-16 5JR2
TITLE CRYSTAL STRUCTURE OF THE EPHA4 LBD IN COMPLEX WITH APYD3 PEPTIDE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: EPH-LIKE KINASE 8,HEK8,TYROSINE-PROTEIN KINASE TYRO1,
COMPND 5 TYROSINE-PROTEIN KINASE RECEPTOR SEK;
COMPND 6 EC: 2.7.10.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: APYD3 PEPTIDE;
COMPND 11 CHAIN: E, F, G, H;
COMPND 12 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 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630
KEYWDS RECEPTOR TYROSINE KINASE, PEPTIDE INHIBITOR, EPHRIN, ALS,
KEYWDS 2 TRANSFERASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.C.LECHTENBERG,E.J.OLSON,E.B.PASQUALE,P.E.DAWSON,S.J.RIEDL
REVDAT 5 27-SEP-23 5JR2 1 REMARK
REVDAT 4 27-NOV-19 5JR2 1 REMARK
REVDAT 3 20-SEP-17 5JR2 1 REMARK
REVDAT 2 05-OCT-16 5JR2 1 JRNL
REVDAT 1 06-JUL-16 5JR2 0
JRNL AUTH E.J.OLSON,B.C.LECHTENBERG,C.ZHAO,E.RUBIO DE LA TORRE,
JRNL AUTH 2 I.LAMBERTO,S.J.RIEDL,P.E.DAWSON,E.B.PASQUALE
JRNL TITL MODIFICATIONS OF A NANOMOLAR CYCLIC PEPTIDE ANTAGONIST FOR
JRNL TITL 2 THE EPHA4 RECEPTOR TO ACHIEVE HIGH PLASMA STABILITY.
JRNL REF ACS MED.CHEM.LETT. V. 7 841 2016
JRNL REFN ISSN 1948-5875
JRNL PMID 27660688
JRNL DOI 10.1021/ACSMEDCHEMLETT.6B00132
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 74698
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 4103
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5345
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 332
REMARK 3 BIN FREE R VALUE : 0.2340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6077
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 685
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.13000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : 0.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.07000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.113
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.697
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6683 ; 0.012 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 6210 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9058 ; 1.591 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14311 ; 1.322 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 812 ; 6.630 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 328 ;32.310 ;24.146
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1133 ;12.030 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;14.852 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 952 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7702 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1581 ; 0.006 ; 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): 3225 ; 1.320 ; 1.447
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3223 ; 1.321 ; 1.446
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4082 ; 2.210 ; 2.155
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4082 ; 2.210 ; 2.155
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3458 ; 1.779 ; 1.667
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3458 ; 1.779 ; 1.667
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4977 ; 2.805 ; 2.402
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7560 ; 6.151 ;12.571
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7561 ; 6.151 ;12.574
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 26 204 B 26 204 10822 0.08 0.05
REMARK 3 2 A 26 204 C 26 204 10302 0.10 0.05
REMARK 3 3 A 26 204 D 26 204 10248 0.11 0.05
REMARK 3 4 B 26 204 C 26 204 10162 0.11 0.05
REMARK 3 5 B 26 204 D 26 204 10187 0.11 0.05
REMARK 3 6 C 26 204 D 26 204 10353 0.07 0.05
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 26 A 204
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3621 -5.8483 137.2390
REMARK 3 T TENSOR
REMARK 3 T11: 0.0234 T22: 0.0149
REMARK 3 T33: 0.0238 T12: -0.0100
REMARK 3 T13: -0.0032 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.5350 L22: 1.2850
REMARK 3 L33: 0.9418 L12: -0.2620
REMARK 3 L13: 0.2743 L23: -0.3252
REMARK 3 S TENSOR
REMARK 3 S11: -0.0122 S12: -0.0624 S13: 0.0351
REMARK 3 S21: 0.1182 S22: -0.0281 S23: -0.0482
REMARK 3 S31: -0.0444 S32: 0.0064 S33: 0.0403
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 26 B 204
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8375 -37.9877 181.9642
REMARK 3 T TENSOR
REMARK 3 T11: 0.0313 T22: 0.0066
REMARK 3 T33: 0.0365 T12: 0.0082
REMARK 3 T13: 0.0026 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.4402 L22: 1.2135
REMARK 3 L33: 0.7170 L12: 0.0870
REMARK 3 L13: -0.2609 L23: -0.0965
REMARK 3 S TENSOR
REMARK 3 S11: -0.0003 S12: 0.0297 S13: -0.0532
REMARK 3 S21: -0.1020 S22: -0.0516 S23: -0.0723
REMARK 3 S31: 0.0236 S32: 0.0136 S33: 0.0519
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 26 C 204
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1435 -45.7752 146.0569
REMARK 3 T TENSOR
REMARK 3 T11: 0.0227 T22: 0.0179
REMARK 3 T33: 0.0149 T12: 0.0026
REMARK 3 T13: -0.0024 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.5135 L22: 1.9511
REMARK 3 L33: 1.2670 L12: -0.1351
REMARK 3 L13: 0.1582 L23: -0.2372
REMARK 3 S TENSOR
REMARK 3 S11: 0.0307 S12: -0.0359 S13: 0.0056
REMARK 3 S21: 0.1526 S22: -0.0167 S23: -0.0075
REMARK 3 S31: 0.0619 S32: 0.0751 S33: -0.0140
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 26 D 204
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3596 1.6479 172.6550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0263 T22: 0.0316
REMARK 3 T33: 0.0307 T12: 0.0049
REMARK 3 T13: 0.0061 T23: 0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.5267 L22: 1.4839
REMARK 3 L33: 1.1182 L12: -0.1627
REMARK 3 L13: -0.0468 L23: -0.2928
REMARK 3 S TENSOR
REMARK 3 S11: 0.0536 S12: 0.0987 S13: 0.0266
REMARK 3 S21: -0.1101 S22: -0.0757 S23: -0.0683
REMARK 3 S31: -0.0832 S32: 0.0722 S33: 0.0221
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 13
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3372 -22.3666 142.5893
REMARK 3 T TENSOR
REMARK 3 T11: 0.0587 T22: 0.0121
REMARK 3 T33: 0.0754 T12: -0.0117
REMARK 3 T13: -0.0334 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 4.5793 L22: 1.7976
REMARK 3 L33: 10.0571 L12: -1.1987
REMARK 3 L13: -4.0925 L23: 0.7808
REMARK 3 S TENSOR
REMARK 3 S11: 0.1518 S12: -0.1837 S13: -0.3501
REMARK 3 S21: -0.0033 S22: 0.0123 S23: 0.0416
REMARK 3 S31: 0.3082 S32: 0.0388 S33: -0.1642
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 13
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8196 -21.4717 176.6258
REMARK 3 T TENSOR
REMARK 3 T11: 0.0638 T22: 0.0110
REMARK 3 T33: 0.0765 T12: 0.0098
REMARK 3 T13: 0.0199 T23: 0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 4.8957 L22: 3.8073
REMARK 3 L33: 8.1934 L12: 2.4983
REMARK 3 L13: 4.4951 L23: 0.9087
REMARK 3 S TENSOR
REMARK 3 S11: -0.0131 S12: 0.1999 S13: 0.2506
REMARK 3 S21: -0.0988 S22: 0.1293 S23: 0.0705
REMARK 3 S31: -0.3102 S32: 0.0803 S33: -0.1161
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 13
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2790 -62.5628 152.6395
REMARK 3 T TENSOR
REMARK 3 T11: 0.0924 T22: 0.0138
REMARK 3 T33: 0.0386 T12: 0.0141
REMARK 3 T13: -0.0263 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 5.7917 L22: 3.1089
REMARK 3 L33: 10.3164 L12: -0.8146
REMARK 3 L13: -3.8168 L23: -2.0479
REMARK 3 S TENSOR
REMARK 3 S11: 0.1132 S12: -0.1198 S13: -0.2661
REMARK 3 S21: 0.0396 S22: 0.1601 S23: 0.1587
REMARK 3 S31: 0.3114 S32: 0.1126 S33: -0.2733
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 13
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6709 17.9149 165.8087
REMARK 3 T TENSOR
REMARK 3 T11: 0.0826 T22: 0.0202
REMARK 3 T33: 0.0852 T12: -0.0019
REMARK 3 T13: 0.0137 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 4.0284 L22: 1.8801
REMARK 3 L33: 9.5248 L12: 1.2916
REMARK 3 L13: 3.0663 L23: 0.0317
REMARK 3 S TENSOR
REMARK 3 S11: -0.0778 S12: 0.0599 S13: 0.3346
REMARK 3 S21: -0.0299 S22: -0.0335 S23: -0.0932
REMARK 3 S31: -0.3403 S32: 0.1488 S33: 0.1113
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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
REMARK 4
REMARK 4 5JR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221061.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : XDS MARCH 1, 2015, AIMLESS
REMARK 200 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78825
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 28.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.31600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.7
REMARK 200 STARTING MODEL: 4W4Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MGCL2, 0.1 M BIS-TRIS PH 6.5,
REMARK 280 25% PEG 3,350, 3% 1,6-HEXANEDIOL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 42.23350
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 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: 2160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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: 2160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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: 1910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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: 1650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 GLU C 62
REMARK 465 LYS C 63
REMARK 465 VAL C 114
REMARK 465 MET C 115
REMARK 465 ASP D 61
REMARK 465 GLU D 62
REMARK 465 LYS D 63
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 O HOH D 500 O HOH D 552 2.11
REMARK 500 OG SER A 48 O HOH A 401 2.13
REMARK 500 O HOH B 411 O HOH B 493 2.13
REMARK 500 O HOH D 451 O HOH D 483 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 554 O HOH C 491 1455 2.12
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 B 43 CB - CG - CD2 ANGL. DEV. = -10.2 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 CYS A 73 58.88 -159.37
REMARK 500 ASN A 74 49.61 -91.72
REMARK 500 ASN A 81 68.73 -152.65
REMARK 500 GLU A 92 -131.47 57.31
REMARK 500 PHE A 136 71.21 37.33
REMARK 500 ASP A 151 -139.43 -132.53
REMARK 500 GLN B 40 86.14 -68.54
REMARK 500 CYS B 73 59.26 -158.95
REMARK 500 ASN B 74 51.25 -94.46
REMARK 500 ASN B 81 71.16 -152.34
REMARK 500 GLU B 92 -131.01 57.63
REMARK 500 ASP B 151 -139.27 -132.13
REMARK 500 CYS C 73 60.48 -160.96
REMARK 500 ASN C 74 50.09 -94.03
REMARK 500 ASN C 81 71.77 -153.97
REMARK 500 GLU C 92 -132.97 58.20
REMARK 500 PHE C 136 67.54 37.84
REMARK 500 ASP C 151 -138.46 -131.89
REMARK 500 SER C 177 -0.48 -143.73
REMARK 500 CYS D 73 60.35 -158.76
REMARK 500 ASN D 74 49.79 -94.16
REMARK 500 ASN D 81 72.53 -154.53
REMARK 500 GLU D 92 -129.47 48.12
REMARK 500 PHE D 136 74.03 41.09
REMARK 500 ASP D 151 -135.70 -134.22
REMARK 500 SER D 177 -1.61 -142.29
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 ARG E 7 BAL E 8 -140.18
REMARK 500 ARG F 7 BAL F 8 -143.81
REMARK 500 ARG G 7 BAL G 8 -140.70
REMARK 500 ARG H 7 BAL H 8 -147.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 553 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH B 554 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH C 559 DISTANCE = 6.84 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ 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 GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEZ C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BAL E 1 and PRO E 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG E 7 and BAL E 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BAL E 8 and SER E 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide CYS E 12 and NH2 E
REMARK 800 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BAL F 1 and PRO F 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG F 7 and BAL F 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BAL F 8 and SER F 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide CYS F 12 and NH2 F
REMARK 800 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BAL G 1 and PRO G 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG G 7 and BAL G 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BAL G 8 and SER G 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide CYS G 12 and NH2 G
REMARK 800 13
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BAL H 1 and PRO H 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ARG H 7 and BAL H 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide BAL H 8 and SER H 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide CYS H 12 and NH2 H
REMARK 800 13
DBREF 5JR2 A 29 204 UNP P54764 EPHA4_HUMAN 29 204
DBREF 5JR2 B 29 204 UNP P54764 EPHA4_HUMAN 29 204
DBREF 5JR2 C 29 204 UNP P54764 EPHA4_HUMAN 29 204
DBREF 5JR2 D 29 204 UNP P54764 EPHA4_HUMAN 29 204
DBREF 5JR2 E 1 13 PDB 5JR2 5JR2 1 13
DBREF 5JR2 F 1 13 PDB 5JR2 5JR2 1 13
DBREF 5JR2 G 1 13 PDB 5JR2 5JR2 1 13
DBREF 5JR2 H 1 13 PDB 5JR2 5JR2 1 13
SEQADV 5JR2 GLY A 26 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 PRO A 27 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 GLY A 28 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 ALA A 204 UNP P54764 CYS 204 ENGINEERED MUTATION
SEQADV 5JR2 GLY B 26 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 PRO B 27 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 GLY B 28 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 ALA B 204 UNP P54764 CYS 204 ENGINEERED MUTATION
SEQADV 5JR2 GLY C 26 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 PRO C 27 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 GLY C 28 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 ALA C 204 UNP P54764 CYS 204 ENGINEERED MUTATION
SEQADV 5JR2 GLY D 26 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 PRO D 27 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 GLY D 28 UNP P54764 EXPRESSION TAG
SEQADV 5JR2 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 13 BAL PRO TYR CYS VAL TYR ARG BAL SER TRP SER CYS NH2
SEQRES 1 F 13 BAL PRO TYR CYS VAL TYR ARG BAL SER TRP SER CYS NH2
SEQRES 1 G 13 BAL PRO TYR CYS VAL TYR ARG BAL SER TRP SER CYS NH2
SEQRES 1 H 13 BAL PRO TYR CYS VAL TYR ARG BAL SER TRP SER CYS NH2
HET BAL E 1 5
HET BAL E 8 5
HET NH2 E 13 1
HET BAL F 1 5
HET BAL F 8 5
HET NH2 F 13 1
HET BAL G 1 5
HET BAL G 8 5
HET NH2 G 13 1
HET BAL H 1 5
HET BAL H 8 5
HET NH2 H 13 1
HET HEZ A 301 8
HET HEZ A 302 8
HET GOL A 303 6
HET GOL A 304 6
HET GOL A 305 6
HET HEZ B 301 8
HET HEZ B 302 8
HET HEZ B 303 8
HET GOL B 304 6
HET GOL B 305 6
HET GOL B 306 6
HET HEZ C 301 8
HET GOL C 302 6
HET GOL D 301 6
HETNAM BAL BETA-ALANINE
HETNAM NH2 AMINO GROUP
HETNAM HEZ HEXANE-1,6-DIOL
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 BAL 8(C3 H7 N O2)
FORMUL 5 NH2 4(H2 N)
FORMUL 9 HEZ 6(C6 H14 O2)
FORMUL 11 GOL 8(C3 H8 O3)
FORMUL 23 HOH *685(H2 O)
HELIX 1 AA1 GLY A 26 GLY A 28 5 3
HELIX 2 AA2 ARG A 37 VAL A 39 5 3
HELIX 3 AA3 ASP A 107 LEU A 111 5 5
HELIX 4 AA4 ARG A 138 PHE A 142 5 5
HELIX 5 AA5 GLY B 26 GLY B 28 5 3
HELIX 6 AA6 ARG B 37 VAL B 39 5 3
HELIX 7 AA7 ASP B 107 LEU B 111 5 5
HELIX 8 AA8 ARG B 138 PHE B 142 5 5
HELIX 9 AA9 GLY C 26 GLY C 28 5 3
HELIX 10 AB1 ARG C 37 VAL C 39 5 3
HELIX 11 AB2 ASP C 107 LEU C 111 5 5
HELIX 12 AB3 ARG C 138 PHE C 142 5 5
HELIX 13 AB4 GLY D 26 GLY D 28 5 3
HELIX 14 AB5 ARG D 37 VAL D 39 5 3
HELIX 15 AB6 ASP D 107 LEU D 111 5 5
HELIX 16 AB7 ARG D 138 PHE D 142 5 5
SHEET 1 AA1 4 GLU A 30 ASP A 35 0
SHEET 2 AA1 4 CYS A 191 LYS A 202 -1 O VAL A 199 N LEU A 33
SHEET 3 AA1 4 PRO A 66 CYS A 73 -1 N TYR A 70 O LEU A 194
SHEET 4 AA1 4 GLU A 55 MET A 60 -1 N ILE A 59 O ILE A 67
SHEET 1 AA2 5 GLU A 30 ASP A 35 0
SHEET 2 AA2 5 CYS A 191 LYS A 202 -1 O VAL A 199 N LEU A 33
SHEET 3 AA2 5 VAL A 97 LEU A 105 -1 N GLU A 100 O ARG A 198
SHEET 4 AA2 5 ILE A 163 VAL A 173 -1 O ARG A 171 N ILE A 99
SHEET 5 AA2 5 PHE A 154 ASP A 158 -1 N VAL A 157 O MET A 164
SHEET 1 AA3 4 ILE A 46 SER A 48 0
SHEET 2 AA3 4 ASN A 82 ARG A 85 -1 O TRP A 83 N SER A 48
SHEET 3 AA3 4 GLY A 180 ASP A 187 -1 O ASP A 187 N ASN A 82
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 TRP A 83 N SER A 48
SHEET 3 AA4 5 GLY A 180 ASP A 187 -1 O ASP A 187 N ASN A 82
SHEET 4 AA4 5 THR A 121 SER A 129 -1 N TYR A 125 O ALA A 184
SHEET 5 AA4 5 VAL A 143 ALA A 149 -1 O ILE A 148 N PHE A 122
SHEET 1 AA5 4 GLU B 30 ASP B 35 0
SHEET 2 AA5 4 CYS B 191 LYS B 202 -1 O VAL B 199 N LEU B 33
SHEET 3 AA5 4 PRO B 66 CYS B 73 -1 N TYR B 70 O LEU B 194
SHEET 4 AA5 4 GLU B 55 MET B 60 -1 N ILE B 59 O ILE B 67
SHEET 1 AA6 5 GLU B 30 ASP B 35 0
SHEET 2 AA6 5 CYS B 191 LYS B 202 -1 O VAL B 199 N LEU B 33
SHEET 3 AA6 5 VAL B 97 LEU B 105 -1 N GLU B 100 O ARG B 198
SHEET 4 AA6 5 ILE B 163 VAL B 173 -1 O ARG B 171 N ILE B 99
SHEET 5 AA6 5 PHE B 154 ASP B 158 -1 N VAL B 157 O MET B 164
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 ILE B 148 N PHE B 122
SHEET 1 AA9 4 GLU C 30 ASP C 35 0
SHEET 2 AA9 4 ILE C 192 LYS C 202 -1 O VAL C 199 N LEU C 33
SHEET 3 AA9 4 PRO C 66 VAL C 72 -1 N TYR C 70 O LEU C 194
SHEET 4 AA9 4 GLU C 55 MET C 60 -1 N ILE C 59 O ILE C 67
SHEET 1 AB1 5 GLU C 30 ASP C 35 0
SHEET 2 AB1 5 ILE C 192 LYS C 202 -1 O VAL C 199 N LEU C 33
SHEET 3 AB1 5 VAL C 97 LEU C 105 -1 N GLU C 100 O ARG C 198
SHEET 4 AB1 5 ILE C 163 VAL C 173 -1 O ARG C 171 N ILE C 99
SHEET 5 AB1 5 PHE C 154 ASP C 158 -1 N VAL C 157 O MET C 164
SHEET 1 AB2 4 ILE C 46 SER C 48 0
SHEET 2 AB2 4 ASN C 82 ARG C 85 -1 O TRP C 83 N SER C 48
SHEET 3 AB2 4 GLY C 180 ASP C 187 -1 O ASP C 187 N ASN C 82
SHEET 4 AB2 4 ILE C 89 THR C 90 -1 N ILE C 89 O PHE C 181
SHEET 1 AB3 5 ILE C 46 SER C 48 0
SHEET 2 AB3 5 ASN C 82 ARG C 85 -1 O TRP C 83 N SER C 48
SHEET 3 AB3 5 GLY C 180 ASP C 187 -1 O ASP C 187 N ASN C 82
SHEET 4 AB3 5 THR C 121 SER C 129 -1 N TYR C 125 O ALA C 184
SHEET 5 AB3 5 VAL C 143 ALA C 149 -1 O ILE C 148 N PHE C 122
SHEET 1 AB4 4 GLU D 30 ASP D 35 0
SHEET 2 AB4 4 ILE D 192 LYS D 202 -1 O VAL D 199 N LEU D 33
SHEET 3 AB4 4 ILE D 67 VAL D 72 -1 N TYR D 70 O LEU D 194
SHEET 4 AB4 4 GLU D 55 ILE D 59 -1 N ILE D 59 O ILE D 67
SHEET 1 AB5 5 GLU D 30 ASP D 35 0
SHEET 2 AB5 5 ILE D 192 LYS D 202 -1 O VAL D 199 N LEU D 33
SHEET 3 AB5 5 VAL D 97 LEU D 105 -1 N GLU D 100 O ARG D 198
SHEET 4 AB5 5 ILE D 163 VAL D 173 -1 O ARG D 171 N ILE D 99
SHEET 5 AB5 5 PHE D 154 ASP D 158 -1 N VAL D 157 O MET D 164
SHEET 1 AB6 4 ILE D 46 SER D 48 0
SHEET 2 AB6 4 ASN D 82 ARG D 85 -1 O TRP D 83 N SER D 48
SHEET 3 AB6 4 GLY D 180 ASP D 187 -1 O ASP D 187 N ASN D 82
SHEET 4 AB6 4 ILE D 89 THR D 90 -1 N ILE D 89 O PHE D 181
SHEET 1 AB7 5 ILE D 46 SER D 48 0
SHEET 2 AB7 5 ASN D 82 ARG D 85 -1 O TRP D 83 N SER D 48
SHEET 3 AB7 5 GLY D 180 ASP D 187 -1 O ASP D 187 N ASN D 82
SHEET 4 AB7 5 THR D 121 SER D 129 -1 N TYR D 125 O ALA D 184
SHEET 5 AB7 5 VAL D 143 ALA D 149 -1 O ILE D 148 N PHE D 122
SHEET 1 AB8 2 VAL E 5 TYR E 6 0
SHEET 2 AB8 2 TRP E 10 SER E 11 -1 O SER E 11 N VAL E 5
SHEET 1 AB9 2 VAL F 5 TYR F 6 0
SHEET 2 AB9 2 TRP F 10 SER F 11 -1 O SER F 11 N VAL F 5
SHEET 1 AC1 2 VAL G 5 TYR G 6 0
SHEET 2 AC1 2 TRP G 10 SER G 11 -1 O SER G 11 N VAL G 5
SHEET 1 AC2 2 VAL H 5 TYR H 6 0
SHEET 2 AC2 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 2.11
SSBOND 2 CYS A 108 CYS A 118 1555 1555 2.07
SSBOND 3 CYS B 73 CYS B 191 1555 1555 2.10
SSBOND 4 CYS B 108 CYS B 118 1555 1555 2.06
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 2.08
SSBOND 8 CYS D 108 CYS D 118 1555 1555 2.06
SSBOND 9 CYS E 4 CYS E 12 1555 1555 2.05
SSBOND 10 CYS F 4 CYS F 12 1555 1555 2.03
SSBOND 11 CYS G 4 CYS G 12 1555 1555 2.06
SSBOND 12 CYS H 4 CYS H 12 1555 1555 2.05
LINK C BAL E 1 N PRO E 2 1555 1555 1.35
LINK C ARG E 7 N BAL E 8 1555 1555 1.31
LINK C BAL E 8 N SER E 9 1555 1555 1.33
LINK C CYS E 12 N NH2 E 13 1555 1555 1.34
LINK C BAL F 1 N PRO F 2 1555 1555 1.32
LINK C ARG F 7 N BAL F 8 1555 1555 1.33
LINK C BAL F 8 N SER F 9 1555 1555 1.32
LINK C CYS F 12 N NH2 F 13 1555 1555 1.32
LINK C BAL G 1 N PRO G 2 1555 1555 1.33
LINK C ARG G 7 N BAL G 8 1555 1555 1.34
LINK C BAL G 8 N SER G 9 1555 1555 1.32
LINK C CYS G 12 N NH2 G 13 1555 1555 1.33
LINK C BAL H 1 N PRO H 2 1555 1555 1.33
LINK C ARG H 7 N BAL H 8 1555 1555 1.34
LINK C BAL H 8 N SER H 9 1555 1555 1.34
LINK C CYS H 12 N NH2 H 13 1555 1555 1.33
CISPEP 1 SER A 48 PRO A 49 0 5.01
CISPEP 2 SER A 48 PRO A 49 0 4.71
CISPEP 3 GLY A 174 PRO A 175 0 2.23
CISPEP 4 SER B 48 PRO B 49 0 2.50
CISPEP 5 SER B 48 PRO B 49 0 2.23
CISPEP 6 GLY B 174 PRO B 175 0 -1.01
CISPEP 7 SER C 48 PRO C 49 0 6.72
CISPEP 8 GLY C 174 PRO C 175 0 12.62
CISPEP 9 SER D 48 PRO D 49 0 2.98
CISPEP 10 SER D 48 PRO D 49 0 1.13
CISPEP 11 GLY D 174 PRO D 175 0 9.90
CISPEP 12 BAL E 1 PRO E 2 0 1.54
CISPEP 13 BAL F 1 PRO F 2 0 10.27
CISPEP 14 BAL G 1 PRO G 2 0 -8.85
SITE 1 AC1 6 ILE A 170 ARG A 171 LYS A 202 HOH A 463
SITE 2 AC1 6 HOH A 472 HOH A 520
SITE 1 AC2 11 SER A 48 ASN A 81 TRP A 83 ARG A 85
SITE 2 AC2 11 ILE A 137 GLU A 139 PHE A 142 HOH A 439
SITE 3 AC2 11 HOH A 455 LEU D 50 GLU D 51
SITE 1 AC3 3 GLU A 30 GLU A 100 ARG A 198
SITE 1 AC4 7 ARG A 96 ASP A 172 VAL A 173 GLY A 174
SITE 2 AC4 7 HOH A 434 HOH A 438 HOH A 522
SITE 1 AC5 2 ASP A 158 GLY A 160
SITE 1 AC6 4 ILE B 170 ARG B 171 LYS B 202 HOH B 467
SITE 1 AC7 6 THR B 104 LEU B 105 PHE B 154 LYS B 165
SITE 2 AC7 6 ASN B 167 HOH B 476
SITE 1 AC8 9 GLY B 93 ALA B 94 GLN B 95 ARG B 96
SITE 2 AC8 9 TYR B 201 LYS B 202 HOH B 402 HOH B 460
SITE 3 AC8 9 HOH B 525
SITE 1 AC9 4 PRO B 27 GLU B 30 GLU B 100 ARG B 198
SITE 1 AD1 3 ASP B 158 GLY B 160 HOH B 404
SITE 1 AD2 5 ARG B 96 ASP B 172 VAL B 173 GLY B 174
SITE 2 AD2 5 HOH B 457
SITE 1 AD3 9 SER C 48 ARG C 85 ILE C 137 GLU C 139
SITE 2 AD3 9 PHE C 142 HOH C 403 HOH C 478 HOH C 499
SITE 3 AD3 9 HOH C 533
SITE 1 AD4 6 ARG C 96 ASP C 172 VAL C 173 GLY C 174
SITE 2 AD4 6 HOH C 455 HOH C 490
SITE 1 AD5 5 ARG D 96 ASP D 172 VAL D 173 GLY D 174
SITE 2 AD5 5 HOH D 483
SITE 1 AD6 5 CYS A 73 ASN A 74 GLU A 77 TYR E 3
SITE 2 AD6 5 CYS E 4
SITE 1 AD7 7 ARG A 162 HOH A 452 VAL E 5 TYR E 6
SITE 2 AD7 7 SER E 9 HOH E 103 HOH E 105
SITE 1 AD8 6 ARG A 162 TYR E 6 ARG E 7 TRP E 10
SITE 2 AD8 6 SER E 11 HOH E 102
SITE 1 AD9 3 TYR E 3 CYS E 4 SER E 11
SITE 1 AE1 6 CYS B 73 ASN B 74 GLU B 77 TYR F 3
SITE 2 AE1 6 CYS F 4 HOH F 102
SITE 1 AE2 7 ARG B 162 HOH B 420 VAL F 5 TYR F 6
SITE 2 AE2 7 SER F 9 HOH F 106 HOH F 108
SITE 1 AE3 5 ARG B 162 TYR F 6 ARG F 7 TRP F 10
SITE 2 AE3 5 HOH F 104
SITE 1 AE4 3 TYR F 3 CYS F 4 SER F 11
SITE 1 AE5 9 CYS C 73 ASN C 74 GLU C 77 PRO D 112
SITE 2 AE5 9 GLY D 113 HOH D 463 TYR G 3 CYS G 4
SITE 3 AE5 9 HOH G 102
SITE 1 AE6 7 ILE C 59 HOH C 480 VAL G 5 TYR G 6
SITE 2 AE6 7 SER G 9 HOH G 103 HOH G 105
SITE 1 AE7 7 ARG C 162 HOH C 404 TYR G 6 ARG G 7
SITE 2 AE7 7 TRP G 10 SER G 11 HOH G 103
SITE 1 AE8 7 GLY D 113 MET D 115 HOH D 468 TYR G 3
SITE 2 AE8 7 CYS G 4 SER G 11 HOH G 106
SITE 1 AE9 9 GLY D 52 CYS D 73 ASN D 74 GLU D 77
SITE 2 AE9 9 HOH D 456 TYR H 3 CYS H 4 HOH H 102
SITE 3 AE9 9 HOH H 104
SITE 1 AF1 7 ILE D 59 ARG D 162 HOH D 431 VAL H 5
SITE 2 AF1 7 TYR H 6 SER H 9 HOH H 101
SITE 1 AF2 5 TYR H 6 ARG H 7 TRP H 10 SER H 11
SITE 2 AF2 5 HOH H 101
SITE 1 AF3 5 TYR H 3 CYS H 4 SER H 11 HOH H 106
SITE 2 AF3 5 HOH H 107
CRYST1 37.137 84.467 127.894 90.00 93.87 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 0.026927 0.000000 0.001822 0.00000
SCALE2 0.000000 0.011839 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007837 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
