HEADER SIGNALING PROTEIN 25-AUG-08 3EAE
TITLE PWWP DOMAIN OF HUMAN HEPATOMA-DERIVED GROWTH FACTOR 2 (HDGF2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOMA-DERIVED GROWTH FACTOR-RELATED PROTEIN 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-93;
COMPND 5 SYNONYM: HRP-2, HEPATOMA-DERIVED GROWTH FACTOR 2;
COMPND 6 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: HDGFRP2, HDGF2, UNQ785/PRO1604;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HUMAN HEPATOMA-DERIVED GROWTH FACTOR 2, HEPATOMA-DERIVED GROWTH
KEYWDS 2 FACTOR-RELATED PROTEIN 2, HDGF2, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 3 GENOMICS CONSORTIUM, SGC, PHOSPHOPROTEIN, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.AMAYA,H.ZENG,F.MACKENZIE,C.BOUNTRA,J.WEIGELT,C.H.ARROWSMITH,
AUTHOR 2 A.M.EDWARDS,A.BOCHKAREV,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (SGC)
REVDAT 8 30-AUG-23 3EAE 1 REMARK
REVDAT 7 25-OCT-17 3EAE 1 REMARK
REVDAT 6 20-JUL-11 3EAE 1 JRNL
REVDAT 5 13-JUL-11 3EAE 1 VERSN
REVDAT 4 28-APR-10 3EAE 1 AUTHOR
REVDAT 3 25-AUG-09 3EAE 1 REMARK
REVDAT 2 24-FEB-09 3EAE 1 VERSN
REVDAT 1 16-SEP-08 3EAE 0
JRNL AUTH H.WU,H.ZENG,R.LAM,W.TEMPEL,M.F.AMAYA,C.XU,L.DOMBROVSKI,
JRNL AUTH 2 W.QIU,Y.WANG,J.MIN
JRNL TITL STRUCTURAL AND HISTONE BINDING ABILITY CHARACTERIZATIONS OF
JRNL TITL 2 HUMAN PWWP DOMAINS.
JRNL REF PLOS ONE V. 6 18919 2011
JRNL REFN ESSN 1932-6203
JRNL PMID 21720545
JRNL DOI 10.1371/JOURNAL.PONE.0018919
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 12780
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 632
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) : 2.24
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.29
REMARK 3 REFLECTION IN BIN (WORKING SET) : 724
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 37
REMARK 3 BIN FREE R VALUE : 0.3630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1322
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 45
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.26000
REMARK 3 B22 (A**2) : 3.56000
REMARK 3 B33 (A**2) : -2.30000
REMARK 3 B12 (A**2) : 0.00000
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): 0.233
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.201
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.145
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.564
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1379 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1878 ; 1.261 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 164 ; 7.081 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 69 ;27.567 ;23.623
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 177 ;14.386 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;20.709 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 173 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1134 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 486 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 893 ; 0.318 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 37 ; 0.183 ; 0.200
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): 16 ; 0.148 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.188 ; 0.200
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): 850 ; 0.605 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1329 ; 1.009 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 615 ; 1.680 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 549 ; 2.379 ; 4.500
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 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
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 2 A 10
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0601 48.8531 -5.0603
REMARK 3 T TENSOR
REMARK 3 T11: 0.0517 T22: 0.1942
REMARK 3 T33: 0.1874 T12: -0.0684
REMARK 3 T13: 0.0233 T23: 0.0606
REMARK 3 L TENSOR
REMARK 3 L11: 16.4280 L22: 8.0876
REMARK 3 L33: 12.8956 L12: -5.6157
REMARK 3 L13: 7.1118 L23: -4.9561
REMARK 3 S TENSOR
REMARK 3 S11: -0.2616 S12: 0.8433 S13: 0.9443
REMARK 3 S21: 0.1628 S22: 0.0291 S23: -0.4283
REMARK 3 S31: -0.6381 S32: 0.1133 S33: 0.2326
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 : A 11 A 25
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0981 36.0774 2.4575
REMARK 3 T TENSOR
REMARK 3 T11: 0.1202 T22: 0.1959
REMARK 3 T33: 0.1869 T12: -0.1112
REMARK 3 T13: -0.0041 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 6.1298 L22: 4.9149
REMARK 3 L33: 6.1488 L12: -0.8441
REMARK 3 L13: -2.1573 L23: -2.2751
REMARK 3 S TENSOR
REMARK 3 S11: -0.0290 S12: 0.2625 S13: -0.7442
REMARK 3 S21: 0.1125 S22: 0.0555 S23: 0.3212
REMARK 3 S31: 0.7963 S32: -0.3814 S33: -0.0264
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 : A 26 A 36
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3795 37.3522 -14.6102
REMARK 3 T TENSOR
REMARK 3 T11: 0.3776 T22: 0.6340
REMARK 3 T33: 0.2771 T12: 0.0646
REMARK 3 T13: 0.1391 T23: -0.2338
REMARK 3 L TENSOR
REMARK 3 L11: 12.6104 L22: 2.4123
REMARK 3 L33: 14.1055 L12: 4.6747
REMARK 3 L13: 3.8020 L23: -1.5577
REMARK 3 S TENSOR
REMARK 3 S11: 0.1076 S12: 2.1868 S13: -1.3004
REMARK 3 S21: -0.4893 S22: 0.2422 S23: -0.8771
REMARK 3 S31: -0.2167 S32: 1.1787 S33: -0.3498
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 37 A 47
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8636 36.8654 -5.2275
REMARK 3 T TENSOR
REMARK 3 T11: 0.0604 T22: 0.1361
REMARK 3 T33: 0.1395 T12: -0.0517
REMARK 3 T13: 0.0002 T23: -0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 4.9573 L22: 5.3115
REMARK 3 L33: 22.0441 L12: -1.1832
REMARK 3 L13: 4.9798 L23: -3.6940
REMARK 3 S TENSOR
REMARK 3 S11: 0.0855 S12: 0.4758 S13: -0.1974
REMARK 3 S21: -0.1805 S22: -0.1021 S23: 0.0791
REMARK 3 S31: 0.2607 S32: -0.4642 S33: 0.0166
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 : A 48 A 62
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3375 39.1224 -1.6845
REMARK 3 T TENSOR
REMARK 3 T11: 0.0446 T22: 0.1919
REMARK 3 T33: 0.1017 T12: -0.0727
REMARK 3 T13: 0.0376 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 8.2173 L22: 5.5034
REMARK 3 L33: 4.8835 L12: -4.2233
REMARK 3 L13: 0.6276 L23: 0.7077
REMARK 3 S TENSOR
REMARK 3 S11: -0.1443 S12: 0.3407 S13: -0.4028
REMARK 3 S21: -0.1715 S22: 0.1736 S23: 0.1934
REMARK 3 S31: 0.3721 S32: -0.2485 S33: -0.0293
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 : A 63 A 72
REMARK 3 ORIGIN FOR THE GROUP (A): 22.0366 41.6557 11.7228
REMARK 3 T TENSOR
REMARK 3 T11: 0.0133 T22: 0.2777
REMARK 3 T33: 0.1316 T12: 0.0820
REMARK 3 T13: 0.0454 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 7.8081 L22: 13.9963
REMARK 3 L33: 16.6427 L12: -4.1345
REMARK 3 L13: 5.3805 L23: -6.6826
REMARK 3 S TENSOR
REMARK 3 S11: -0.3860 S12: -0.9478 S13: 0.0176
REMARK 3 S21: 0.7793 S22: 0.1417 S23: 0.4107
REMARK 3 S31: -0.2294 S32: -0.9472 S33: 0.2442
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 : A 73 A 79
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7631 30.1890 9.8295
REMARK 3 T TENSOR
REMARK 3 T11: 0.2994 T22: 0.1529
REMARK 3 T33: 0.2605 T12: -0.0930
REMARK 3 T13: 0.0323 T23: 0.0627
REMARK 3 L TENSOR
REMARK 3 L11: 9.9495 L22: 4.5720
REMARK 3 L33: 11.3583 L12: -4.3402
REMARK 3 L13: 9.9848 L23: -2.4624
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: 0.5934 S13: -1.1328
REMARK 3 S21: -0.2669 S22: 0.5606 S23: -0.0515
REMARK 3 S31: 1.2946 S32: -0.5565 S33: -0.5801
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 : A 80 A 93
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5677 38.3975 4.5513
REMARK 3 T TENSOR
REMARK 3 T11: 0.0858 T22: 0.2057
REMARK 3 T33: 0.1817 T12: 0.0213
REMARK 3 T13: 0.0129 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 10.5581 L22: 1.8267
REMARK 3 L33: 16.1106 L12: 3.0010
REMARK 3 L13: -5.6948 L23: -2.6427
REMARK 3 S TENSOR
REMARK 3 S11: -0.1621 S12: -0.2947 S13: -0.5481
REMARK 3 S21: -0.0752 S22: -0.1218 S23: -0.2997
REMARK 3 S31: 0.2668 S32: 0.8832 S33: 0.2840
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 5 B 10
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3637 42.6148 30.4898
REMARK 3 T TENSOR
REMARK 3 T11: 0.6460 T22: 0.5593
REMARK 3 T33: 0.1607 T12: -0.2187
REMARK 3 T13: -0.1473 T23: 0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 24.9467 L22: 18.0888
REMARK 3 L33: 14.9676 L12: -4.1764
REMARK 3 L13: 3.1747 L23: -10.5505
REMARK 3 S TENSOR
REMARK 3 S11: 0.2494 S12: -1.9110 S13: 1.1378
REMARK 3 S21: 2.3230 S22: -0.6121 S23: -1.4048
REMARK 3 S31: -2.4148 S32: 1.4887 S33: 0.3627
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 11 B 20
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0359 29.0829 23.0252
REMARK 3 T TENSOR
REMARK 3 T11: 0.2127 T22: 0.3320
REMARK 3 T33: 0.3991 T12: 0.0726
REMARK 3 T13: -0.0567 T23: 0.2431
REMARK 3 L TENSOR
REMARK 3 L11: 9.8076 L22: 12.1116
REMARK 3 L33: 15.4641 L12: -6.2237
REMARK 3 L13: 4.9084 L23: 3.3085
REMARK 3 S TENSOR
REMARK 3 S11: 0.6355 S12: -1.0611 S13: -1.5858
REMARK 3 S21: -0.0906 S22: -0.2916 S23: 0.2451
REMARK 3 S31: 1.3742 S32: 0.9112 S33: -0.3439
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 21 B 26
REMARK 3 ORIGIN FOR THE GROUP (A): 38.0790 35.5639 26.9757
REMARK 3 T TENSOR
REMARK 3 T11: 0.1868 T22: 0.1512
REMARK 3 T33: -0.0312 T12: 0.0108
REMARK 3 T13: -0.1231 T23: 0.1637
REMARK 3 L TENSOR
REMARK 3 L11: 6.3231 L22: 11.5535
REMARK 3 L33: 24.0216 L12: 8.0843
REMARK 3 L13: 3.8921 L23: -0.1551
REMARK 3 S TENSOR
REMARK 3 S11: -0.2294 S12: -1.0918 S13: -0.8569
REMARK 3 S21: 0.3923 S22: -0.2724 S23: 0.3940
REMARK 3 S31: 0.0846 S32: 0.0172 S33: 0.5017
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 27 B 48
REMARK 3 ORIGIN FOR THE GROUP (A): 37.5517 33.9404 30.3959
REMARK 3 T TENSOR
REMARK 3 T11: 0.2196 T22: 0.2665
REMARK 3 T33: 0.1096 T12: -0.0469
REMARK 3 T13: -0.0484 T23: 0.2041
REMARK 3 L TENSOR
REMARK 3 L11: 15.5654 L22: 4.5238
REMARK 3 L33: 22.2879 L12: 2.7396
REMARK 3 L13: 9.4699 L23: -0.6061
REMARK 3 S TENSOR
REMARK 3 S11: 0.5823 S12: -1.0634 S13: 0.2433
REMARK 3 S21: 0.6815 S22: -0.6480 S23: -0.3770
REMARK 3 S31: -0.0129 S32: -0.2531 S33: 0.0657
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 49 B 61
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3378 33.7639 28.7247
REMARK 3 T TENSOR
REMARK 3 T11: 0.1525 T22: 0.2926
REMARK 3 T33: 0.0392 T12: 0.0003
REMARK 3 T13: -0.0799 T23: 0.0889
REMARK 3 L TENSOR
REMARK 3 L11: 28.0052 L22: 7.5452
REMARK 3 L33: 15.6982 L12: 5.6948
REMARK 3 L13: -2.2335 L23: -7.9716
REMARK 3 S TENSOR
REMARK 3 S11: 0.8896 S12: -1.8175 S13: -1.2009
REMARK 3 S21: 1.0767 S22: -1.1633 S23: -0.4973
REMARK 3 S31: -0.0507 S32: 2.5198 S33: 0.2737
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 62 B 68
REMARK 3 ORIGIN FOR THE GROUP (A): 46.2061 39.5062 16.6555
REMARK 3 T TENSOR
REMARK 3 T11: -0.0142 T22: 0.3763
REMARK 3 T33: 0.0701 T12: -0.0125
REMARK 3 T13: -0.0228 T23: 0.1985
REMARK 3 L TENSOR
REMARK 3 L11: 19.0965 L22: 30.1460
REMARK 3 L33: 36.8150 L12: 4.0313
REMARK 3 L13: -5.3002 L23: 0.5626
REMARK 3 S TENSOR
REMARK 3 S11: 0.4131 S12: 1.1412 S13: 0.6484
REMARK 3 S21: -0.3665 S22: -0.8767 S23: -0.0085
REMARK 3 S31: -1.1489 S32: 2.0986 S33: 0.4636
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 69 B 76
REMARK 3 ORIGIN FOR THE GROUP (A): 37.9973 29.2374 14.2350
REMARK 3 T TENSOR
REMARK 3 T11: 0.1564 T22: 0.2204
REMARK 3 T33: 0.1927 T12: 0.2424
REMARK 3 T13: -0.1207 T23: 0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 4.8440 L22: 37.8123
REMARK 3 L33: 12.5919 L12: 8.5262
REMARK 3 L13: -3.4833 L23: 6.6617
REMARK 3 S TENSOR
REMARK 3 S11: -0.5080 S12: 1.1011 S13: -1.8543
REMARK 3 S21: -0.7518 S22: 0.1050 S23: -1.3061
REMARK 3 S31: 2.0672 S32: 1.1434 S33: 0.4029
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 77 B 90
REMARK 3 ORIGIN FOR THE GROUP (A): 32.3453 38.3147 20.1254
REMARK 3 T TENSOR
REMARK 3 T11: 0.1011 T22: 0.2613
REMARK 3 T33: 0.1328 T12: 0.0096
REMARK 3 T13: 0.0645 T23: 0.0882
REMARK 3 L TENSOR
REMARK 3 L11: 3.7185 L22: 7.5554
REMARK 3 L33: 13.7175 L12: 2.8189
REMARK 3 L13: 3.8104 L23: -3.8962
REMARK 3 S TENSOR
REMARK 3 S11: 0.1656 S12: -0.5523 S13: -0.0775
REMARK 3 S21: 0.4448 S22: -0.1226 S23: 0.6245
REMARK 3 S31: -0.6500 S32: -0.4737 S33: -0.0430
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3EAE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1000049076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97940
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12780
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.240
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.9470
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.64700
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRIES 2HTS AND 2NLU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M NH4SO4, 0.2 M K/NA TART, 0.1 M
REMARK 280 NA CITRATE PH 5.6., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 20.77750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.47100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.97500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.47100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.77750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.97500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 HIS B 3
REMARK 465 ALA B 4
REMARK 465 ILE B 28
REMARK 465 ALA B 29
REMARK 465 ASP B 30
REMARK 465 GLY B 31
REMARK 465 ALA B 32
REMARK 465 VAL B 33
REMARK 465 LYS B 34
REMARK 465 PRO B 35
REMARK 465 PRO B 36
REMARK 465 PRO B 37
REMARK 465 ASN B 38
REMARK 465 SER B 91
REMARK 465 TYR B 92
REMARK 465 SER B 93
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 ILE A 28 CG1 CG2 CD1
REMARK 470 LYS A 34 CG CD CE NZ
REMARK 470 LYS A 73 CG CD CE NZ
REMARK 470 LYS A 75 CG CD CE NZ
REMARK 470 SER A 93 OG
REMARK 470 LYS B 6 CG CD CE NZ
REMARK 470 LYS B 16 CG CD CE NZ
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 LYS B 56 CG CD CE NZ
REMARK 470 LYS B 63 CG CD CE NZ
REMARK 470 ASP B 66 CG OD1 OD2
REMARK 470 LYS B 67 CG CD CE NZ
REMARK 470 LYS B 70 CG CD CE NZ
REMARK 470 LYS B 75 CG CD CE NZ
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 87 67.37 -154.36
REMARK 500 ASP B 26 -161.86 -104.18
REMARK 500 ASN B 87 59.17 -141.96
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3EAE A 1 93 UNP Q7Z4V5 HDGR2_HUMAN 1 93
DBREF 3EAE B 1 93 UNP Q7Z4V5 HDGR2_HUMAN 1 93
SEQRES 1 A 93 MET PRO HIS ALA PHE LYS PRO GLY ASP LEU VAL PHE ALA
SEQRES 2 A 93 LYS MET LYS GLY TYR PRO HIS TRP PRO ALA ARG ILE ASP
SEQRES 3 A 93 ASP ILE ALA ASP GLY ALA VAL LYS PRO PRO PRO ASN LYS
SEQRES 4 A 93 TYR PRO ILE PHE PHE PHE GLY THR HIS GLU THR ALA PHE
SEQRES 5 A 93 LEU GLY PRO LYS ASP LEU PHE PRO TYR ASP LYS CYS LYS
SEQRES 6 A 93 ASP LYS TYR GLY LYS PRO ASN LYS ARG LYS GLY PHE ASN
SEQRES 7 A 93 GLU GLY LEU TRP GLU ILE GLN ASN ASN PRO HIS ALA SER
SEQRES 8 A 93 TYR SER
SEQRES 1 B 93 MET PRO HIS ALA PHE LYS PRO GLY ASP LEU VAL PHE ALA
SEQRES 2 B 93 LYS MET LYS GLY TYR PRO HIS TRP PRO ALA ARG ILE ASP
SEQRES 3 B 93 ASP ILE ALA ASP GLY ALA VAL LYS PRO PRO PRO ASN LYS
SEQRES 4 B 93 TYR PRO ILE PHE PHE PHE GLY THR HIS GLU THR ALA PHE
SEQRES 5 B 93 LEU GLY PRO LYS ASP LEU PHE PRO TYR ASP LYS CYS LYS
SEQRES 6 B 93 ASP LYS TYR GLY LYS PRO ASN LYS ARG LYS GLY PHE ASN
SEQRES 7 B 93 GLU GLY LEU TRP GLU ILE GLN ASN ASN PRO HIS ALA SER
SEQRES 8 B 93 TYR SER
FORMUL 3 HOH *45(H2 O)
HELIX 1 1 GLY A 54 LYS A 56 5 3
HELIX 2 2 TYR A 61 GLY A 69 1 9
HELIX 3 3 GLY A 76 ASN A 87 1 12
HELIX 4 4 GLY B 54 LYS B 56 5 3
HELIX 5 5 TYR B 61 GLY B 69 1 9
HELIX 6 6 GLY B 76 ASN B 87 1 12
SHEET 1 A 5 THR A 50 LEU A 53 0
SHEET 2 A 5 TYR A 40 PHE A 44 -1 N ILE A 42 O ALA A 51
SHEET 3 A 5 TRP A 21 ILE A 25 -1 N ARG A 24 O PHE A 43
SHEET 4 A 5 LEU A 10 ALA A 13 -1 N ALA A 13 O TRP A 21
SHEET 5 A 5 LEU A 58 PRO A 60 -1 O PHE A 59 N PHE A 12
SHEET 1 B 5 THR B 50 LEU B 53 0
SHEET 2 B 5 TYR B 40 PHE B 44 -1 N ILE B 42 O ALA B 51
SHEET 3 B 5 TRP B 21 ILE B 25 -1 N ARG B 24 O PHE B 43
SHEET 4 B 5 LEU B 10 ALA B 13 -1 N VAL B 11 O ALA B 23
SHEET 5 B 5 LEU B 58 PRO B 60 -1 O PHE B 59 N PHE B 12
CRYST1 41.555 59.950 104.942 90.00 90.00 90.00 P 21 21 21 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 0.024064 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016681 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009529 0.00000
(ATOM LINES ARE NOT SHOWN.)
END