HEADER LIGASE/PROTEIN BINDING 29-OCT-10 3PFV
TITLE CRYSTAL STRUCTURE OF CBL-B TKB DOMAIN IN COMPLEX WITH EGFR PY1069
TITLE 2 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE CBL-B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL TKB DOMAIN (UNP RESIDUES 38-344);
COMPND 5 SYNONYM: CASITAS B-LINEAGE LYMPHOMA PROTO-ONCOGENE B, RING FINGER
COMPND 6 PROTEIN 56, SH3-BINDING PROTEIN CBL-B, SIGNAL TRANSDUCTION PROTEIN
COMPND 7 CBL-B;
COMPND 8 EC: 6.3.2.-;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: 11-MERIC PEPTIDE FROM EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 12 CHAIN: C, D;
COMPND 13 FRAGMENT: UNP RESIDUES 1066-1076;
COMPND 14 SYNONYM: PROTO-ONCOGENE C-ERBB-1, RECEPTOR TYROSINE-PROTEIN KINASE
COMPND 15 ERBB-1;
COMPND 16 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: CBLB, NBLA00127, RNF56;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, SIGNAL
KEYWDS 2 TRANSDUCTION PROTEIN, CBL-B, SH3-BINDING PROTEIN, LIGASE-PROTEIN
KEYWDS 3 BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHAIKUAD,K.GUO,C.D.O.COOPER,V.AYINAMPUDI,T.KROJER,J.R.C.MUNIZ,
AUTHOR 2 M.VOLLMAR,P.CANNING,O.GILEADI,F.VON DELFT,C.H.ARROWSMITH,J.WEIGELT,
AUTHOR 3 A.M.EDWARDS,C.BOUNTRA,A.BULLOCK,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 06-DEC-23 3PFV 1 REMARK
REVDAT 3 06-SEP-23 3PFV 1 REMARK SEQADV LINK
REVDAT 2 02-APR-14 3PFV 1 VERSN
REVDAT 1 08-DEC-10 3PFV 0
JRNL AUTH A.CHAIKUAD,K.GUO,C.D.O.COOPER,V.AYINAMPUDI,T.KROJER,
JRNL AUTH 2 J.R.C.MUNIZ,M.VOLLMAR,P.CANNING,O.GILEADI,F.VON DELFT,
JRNL AUTH 3 C.H.ARROWSMITH,J.WEIGELT,A.M.EDWARDS,C.BOUNTRA,A.BULLOCK,
JRNL AUTH 4 STRUCTURAL GENOMICS CONSORTIUM (SGC)
JRNL TITL CRYSTAL STRUCTURE OF CBL-B TKB DOMAIN IN COMPLEX WITH EGFR
JRNL TITL 2 PY1069 PEPTIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.47
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 28661
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1524
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) : 2.27
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2150
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.2720
REMARK 3 BIN FREE R VALUE SET COUNT : 113
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5104
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.44000
REMARK 3 B22 (A**2) : 0.54000
REMARK 3 B33 (A**2) : -0.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.81000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.267
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.194
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.540
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.015 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; 0.005 ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.567 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; 1.198 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; 5.499 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ;33.703 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ;15.268 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ;16.486 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; 0.079 ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; 0.008 ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; 0.004 ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; 2.760 ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; 0.740 ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 4.514 ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; 7.110 ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 8.946 ; 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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 49 A 62 4
REMARK 3 1 B 49 B 62 4
REMARK 3 2 A 69 A 91 3
REMARK 3 2 B 69 B 91 3
REMARK 3 3 A 99 A 122 4
REMARK 3 3 B 99 B 122 4
REMARK 3 4 A 137 A 164 3
REMARK 3 4 B 137 B 164 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 299 ; 0.030 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 511 ; 0.030 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 386 ; 0.110 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 299 ; 0.150 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 511 ; 0.100 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 386 ; 0.110 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1068 C 1074 4
REMARK 3 1 D 1068 D 1074 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 C (A): 104 ; 0.570 ; 0.500
REMARK 3 MEDIUM THERMAL 2 C (A**2): 104 ; 0.760 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 174 B 311 3
REMARK 3 1 A 174 A 311 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 B (A): 812 ; 0.040 ; 0.050
REMARK 3 LOOSE POSITIONAL 3 B (A): 1070 ; 0.130 ; 5.000
REMARK 3 TIGHT THERMAL 3 B (A**2): 812 ; 0.190 ; 0.500
REMARK 3 LOOSE THERMAL 3 B (A**2): 1070 ; 0.130 ;10.000
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 45 A 61
REMARK 3 ORIGIN FOR THE GROUP (A): 35.2336 16.0656 28.6796
REMARK 3 T TENSOR
REMARK 3 T11: 0.2752 T22: 1.0294
REMARK 3 T33: 0.4163 T12: 0.1523
REMARK 3 T13: -0.3039 T23: -0.2040
REMARK 3 L TENSOR
REMARK 3 L11: 8.0211 L22: 29.5846
REMARK 3 L33: 8.1218 L12: 2.7076
REMARK 3 L13: 1.2408 L23: 1.2668
REMARK 3 S TENSOR
REMARK 3 S11: 0.4301 S12: 0.3745 S13: -0.0560
REMARK 3 S21: 2.1306 S22: -0.0446 S23: -1.7045
REMARK 3 S31: 0.4681 S32: 2.6193 S33: -0.3855
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 62 A 82
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7144 24.3665 29.1080
REMARK 3 T TENSOR
REMARK 3 T11: 0.2252 T22: 0.3795
REMARK 3 T33: 0.5787 T12: -0.0302
REMARK 3 T13: -0.1831 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 1.3793 L22: 2.6587
REMARK 3 L33: 4.5096 L12: -0.2071
REMARK 3 L13: 2.4179 L23: 0.4699
REMARK 3 S TENSOR
REMARK 3 S11: -0.1811 S12: 0.1647 S13: -0.0083
REMARK 3 S21: 0.1959 S22: 0.4411 S23: -0.5751
REMARK 3 S31: -0.2334 S32: 0.4189 S33: -0.2600
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 83 A 109
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1050 0.0603 35.6667
REMARK 3 T TENSOR
REMARK 3 T11: 0.2672 T22: 0.4415
REMARK 3 T33: 0.2796 T12: 0.1787
REMARK 3 T13: -0.0921 T23: 0.0699
REMARK 3 L TENSOR
REMARK 3 L11: 6.8701 L22: 7.0827
REMARK 3 L33: 5.0047 L12: -3.3018
REMARK 3 L13: 5.8492 L23: -2.7127
REMARK 3 S TENSOR
REMARK 3 S11: 0.1213 S12: -0.0266 S13: -0.2875
REMARK 3 S21: 0.1498 S22: 0.0290 S23: 0.0291
REMARK 3 S31: 0.0690 S32: 0.0010 S33: -0.1503
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 110 A 128
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9539 13.4512 19.6091
REMARK 3 T TENSOR
REMARK 3 T11: 0.1615 T22: 0.6945
REMARK 3 T33: 0.4042 T12: 0.1429
REMARK 3 T13: -0.1609 T23: -0.0875
REMARK 3 L TENSOR
REMARK 3 L11: 4.8312 L22: 18.2633
REMARK 3 L33: 6.3398 L12: 4.4708
REMARK 3 L13: -1.5019 L23: -7.1923
REMARK 3 S TENSOR
REMARK 3 S11: -0.2443 S12: 0.3296 S13: -0.0337
REMARK 3 S21: 0.3923 S22: 0.3284 S23: -1.3523
REMARK 3 S31: 0.3084 S32: 0.8337 S33: -0.0841
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 129 A 161
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7597 19.2749 21.1047
REMARK 3 T TENSOR
REMARK 3 T11: 0.2630 T22: 0.4212
REMARK 3 T33: 0.4188 T12: -0.0455
REMARK 3 T13: -0.1297 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.8425 L22: 6.4135
REMARK 3 L33: 7.6978 L12: 1.3983
REMARK 3 L13: -1.9646 L23: -5.4390
REMARK 3 S TENSOR
REMARK 3 S11: 0.0608 S12: 0.0673 S13: 0.2550
REMARK 3 S21: 0.7622 S22: 0.1440 S23: -0.4641
REMARK 3 S31: -0.6313 S32: 0.5006 S33: -0.2048
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 162 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7241 1.1114 19.1672
REMARK 3 T TENSOR
REMARK 3 T11: 0.3801 T22: 0.2927
REMARK 3 T33: 0.2488 T12: -0.0083
REMARK 3 T13: 0.0030 T23: 0.0434
REMARK 3 L TENSOR
REMARK 3 L11: 1.1673 L22: 0.7760
REMARK 3 L33: 3.2922 L12: 0.0410
REMARK 3 L13: 0.5798 L23: 0.1501
REMARK 3 S TENSOR
REMARK 3 S11: 0.0301 S12: -0.0936 S13: -0.0966
REMARK 3 S21: 0.1721 S22: 0.0177 S23: 0.1240
REMARK 3 S31: 0.4721 S32: -0.0401 S33: -0.0478
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 251 A 345
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2244 23.6575 16.7899
REMARK 3 T TENSOR
REMARK 3 T11: 0.2868 T22: 0.3001
REMARK 3 T33: 0.2594 T12: 0.0404
REMARK 3 T13: -0.0144 T23: 0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 1.5848 L22: 2.4736
REMARK 3 L33: 0.7058 L12: -0.4443
REMARK 3 L13: -0.0113 L23: -0.1762
REMARK 3 S TENSOR
REMARK 3 S11: -0.0990 S12: -0.0502 S13: 0.0487
REMARK 3 S21: 0.1438 S22: 0.0267 S23: 0.1431
REMARK 3 S31: -0.0400 S32: -0.0765 S33: 0.0723
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 : B 40 B 71
REMARK 3 ORIGIN FOR THE GROUP (A): 43.2495 6.4615 0.3587
REMARK 3 T TENSOR
REMARK 3 T11: 0.0287 T22: 0.8491
REMARK 3 T33: 0.5543 T12: -0.0077
REMARK 3 T13: -0.0023 T23: -0.0955
REMARK 3 L TENSOR
REMARK 3 L11: 2.9894 L22: 12.9056
REMARK 3 L33: 0.2942 L12: 0.6346
REMARK 3 L13: 0.8967 L23: -0.2903
REMARK 3 S TENSOR
REMARK 3 S11: -0.1610 S12: 0.4127 S13: -1.0427
REMARK 3 S21: 0.4673 S22: 0.4054 S23: -1.7423
REMARK 3 S31: -0.0678 S32: 0.1867 S33: -0.2444
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 72 B 97
REMARK 3 ORIGIN FOR THE GROUP (A): 44.2106 13.6551 -9.5044
REMARK 3 T TENSOR
REMARK 3 T11: 0.1448 T22: 0.8078
REMARK 3 T33: 0.6915 T12: -0.1166
REMARK 3 T13: 0.1622 T23: -0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 1.3165 L22: 6.8849
REMARK 3 L33: 1.7953 L12: -0.6195
REMARK 3 L13: 1.2178 L23: 1.5204
REMARK 3 S TENSOR
REMARK 3 S11: 0.1143 S12: 0.6477 S13: 0.1415
REMARK 3 S21: -0.7632 S22: 0.1181 S23: -0.9972
REMARK 3 S31: -0.0733 S32: 0.7943 S33: -0.2325
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 98 B 138
REMARK 3 ORIGIN FOR THE GROUP (A): 36.5455 10.0196 4.0760
REMARK 3 T TENSOR
REMARK 3 T11: 0.1237 T22: 0.4564
REMARK 3 T33: 0.4567 T12: -0.0768
REMARK 3 T13: -0.1065 T23: -0.0641
REMARK 3 L TENSOR
REMARK 3 L11: 1.3976 L22: 10.9598
REMARK 3 L33: 4.6885 L12: 1.9580
REMARK 3 L13: -1.1704 L23: -5.2800
REMARK 3 S TENSOR
REMARK 3 S11: -0.0449 S12: -0.3502 S13: 0.0591
REMARK 3 S21: 0.2157 S22: 0.1710 S23: -0.6692
REMARK 3 S31: -0.0887 S32: 0.5913 S33: -0.1261
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 139 B 172
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7493 12.9319 -8.2098
REMARK 3 T TENSOR
REMARK 3 T11: 0.2262 T22: 0.4229
REMARK 3 T33: 0.4383 T12: -0.1090
REMARK 3 T13: 0.0146 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.7088 L22: 1.7562
REMARK 3 L33: 2.5286 L12: -0.3404
REMARK 3 L13: 0.0049 L23: -0.9785
REMARK 3 S TENSOR
REMARK 3 S11: 0.0479 S12: -0.0381 S13: 0.0700
REMARK 3 S21: -0.1253 S22: 0.1206 S23: -0.4481
REMARK 3 S31: -0.1145 S32: 0.4604 S33: -0.1685
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 173 B 264
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6920 18.5387 -6.7589
REMARK 3 T TENSOR
REMARK 3 T11: 0.3078 T22: 0.3145
REMARK 3 T33: 0.2682 T12: -0.0460
REMARK 3 T13: 0.0099 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 1.1202 L22: 1.9849
REMARK 3 L33: 1.5779 L12: 0.0143
REMARK 3 L13: -0.6068 L23: -0.1150
REMARK 3 S TENSOR
REMARK 3 S11: 0.0531 S12: 0.0317 S13: 0.1325
REMARK 3 S21: -0.1642 S22: 0.0607 S23: -0.0621
REMARK 3 S31: -0.3298 S32: 0.0303 S33: -0.1138
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 265 B 323
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4815 -3.2456 -12.2585
REMARK 3 T TENSOR
REMARK 3 T11: 0.2804 T22: 0.3163
REMARK 3 T33: 0.2903 T12: -0.0301
REMARK 3 T13: 0.0104 T23: -0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 1.6194 L22: 2.7687
REMARK 3 L33: 1.3441 L12: 1.0357
REMARK 3 L13: -0.2239 L23: 0.4125
REMARK 3 S TENSOR
REMARK 3 S11: -0.0485 S12: 0.1753 S13: -0.1317
REMARK 3 S21: -0.2669 S22: 0.1357 S23: -0.2213
REMARK 3 S31: 0.0254 S32: 0.1219 S33: -0.0872
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 324 B 349
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6403 0.2530 -12.5775
REMARK 3 T TENSOR
REMARK 3 T11: 0.2600 T22: 0.3857
REMARK 3 T33: 0.2869 T12: -0.0620
REMARK 3 T13: -0.0599 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 2.2699 L22: 4.0778
REMARK 3 L33: 2.0810 L12: -0.7052
REMARK 3 L13: 1.5775 L23: -1.3958
REMARK 3 S TENSOR
REMARK 3 S11: -0.1947 S12: 0.1172 S13: 0.1205
REMARK 3 S21: -0.1953 S22: 0.1331 S23: 0.2134
REMARK 3 S31: -0.0019 S32: -0.2110 S33: 0.0616
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 : C 1066 C 1075
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4309 26.9756 28.1450
REMARK 3 T TENSOR
REMARK 3 T11: 0.4513 T22: 0.5040
REMARK 3 T33: 0.2745 T12: -0.0023
REMARK 3 T13: 0.0264 T23: -0.1634
REMARK 3 L TENSOR
REMARK 3 L11: 3.6699 L22: 6.5608
REMARK 3 L33: 4.1010 L12: -2.1761
REMARK 3 L13: 0.8377 L23: -5.0132
REMARK 3 S TENSOR
REMARK 3 S11: -0.3482 S12: -0.0105 S13: 0.1466
REMARK 3 S21: 0.9210 S22: 0.1920 S23: -0.1649
REMARK 3 S31: -0.5970 S32: -0.2402 S33: 0.1562
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 : D 1066 D 1075
REMARK 3 ORIGIN FOR THE GROUP (A): 20.5654 -4.5740 -19.8928
REMARK 3 T TENSOR
REMARK 3 T11: 0.4284 T22: 0.7302
REMARK 3 T33: 0.3164 T12: -0.2330
REMARK 3 T13: 0.1563 T23: -0.1855
REMARK 3 L TENSOR
REMARK 3 L11: 4.2286 L22: 6.8082
REMARK 3 L33: 14.8323 L12: -2.6730
REMARK 3 L13: -6.3859 L23: -1.0635
REMARK 3 S TENSOR
REMARK 3 S11: 0.1015 S12: -0.4492 S13: 0.0895
REMARK 3 S21: -0.8396 S22: 0.2259 S23: -0.0024
REMARK 3 S31: 0.4339 S32: 0.9632 S33: -0.3275
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 3PFV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : KIRKPATRICK BAEZ BIMORPH MIRROR
REMARK 200 PAIR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30186
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
REMARK 200 RESOLUTION RANGE LOW (A) : 49.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.60400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ID 3BUO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, 0.3M AMMONIUM SULFATE,
REMARK 280 0.1M BIS-TRIS, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293.15K
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 49.46700
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
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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 37
REMARK 465 GLN A 38
REMARK 465 ALA A 39
REMARK 465 ALA A 40
REMARK 465 ALA A 41
REMARK 465 ASP A 42
REMARK 465 ARG A 43
REMARK 465 GLU A 346
REMARK 465 ASN A 347
REMARK 465 LEU A 348
REMARK 465 TYR A 349
REMARK 465 PHE A 350
REMARK 465 GLN A 351
REMARK 465 MET B 37
REMARK 465 GLN B 38
REMARK 465 ALA B 39
REMARK 465 PHE B 350
REMARK 465 GLN B 351
REMARK 465 ALA C 1076
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 ARG A 44 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 46 CG1 CG2
REMARK 470 GLU A 47 CG CD OE1 OE2
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 LYS A 91 CG CD CE NZ
REMARK 470 GLN A 96 CG CD OE1 NE2
REMARK 470 LYS A 129 CG CD CE NZ
REMARK 470 GLU A 130 CG CD OE1 OE2
REMARK 470 LYS A 279 CG CD CE NZ
REMARK 470 ARG B 43 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 54 CG OD1 OD2
REMARK 470 GLN B 61 CG CD OE1 NE2
REMARK 470 LYS B 64 CG CD CE NZ
REMARK 470 GLN B 66 CG CD OE1 NE2
REMARK 470 LEU B 89 CG CD1 CD2
REMARK 470 LYS B 91 CG CD CE NZ
REMARK 470 ASN B 95 CG OD1 ND2
REMARK 470 GLN B 96 CG CD OE1 NE2
REMARK 470 LEU B 98 CG CD1 CD2
REMARK 470 GLN B 100 CG CD OE1 NE2
REMARK 470 GLU B 103 CG CD OE1 OE2
REMARK 470 ARG B 120 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 131 NE CZ NH1 NH2
REMARK 470 GLN B 136 CG CD OE1 NE2
REMARK 470 GLN B 165 CG CD OE1 NE2
REMARK 470 LYS B 195 CG CD CE NZ
REMARK 470 GLU B 346 CG CD OE1 OE2
REMARK 470 LEU B 348 CG CD1 CD2
REMARK 470 LEU C1066 CG CD1 CD2
REMARK 470 GLN C1067 CG CD OE1 NE2
REMARK 470 LEU D1066 CG CD1 CD2
REMARK 470 GLN D1067 CG CD OE1 NE2
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 O4 SO4 B 3 O HOH B 406 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 140 CZ ARG A 140 NH1 -0.132
REMARK 500 ARG A 286 CZ ARG A 286 NH1 -0.130
REMARK 500 ARG A 286 CZ ARG A 286 NH2 -0.128
REMARK 500 ARG B 140 CZ ARG B 140 NH1 -0.130
REMARK 500 ARG B 140 CZ ARG B 140 NH2 -0.094
REMARK 500 ARG B 286 CZ ARG B 286 NH1 -0.111
REMARK 500 ARG B 286 CZ ARG B 286 NH2 -0.149
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 ARG A 140 NH1 - CZ - NH2 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ARG A 140 NE - CZ - NH2 ANGL. DEV. = 12.1 DEGREES
REMARK 500 ARG A 183 CD - NE - CZ ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 183 NE - CZ - NH1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG A 183 NE - CZ - NH2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG A 198 CD - NE - CZ ANGL. DEV. = 13.7 DEGREES
REMARK 500 ARG A 198 NE - CZ - NH1 ANGL. DEV. = -11.6 DEGREES
REMARK 500 ARG A 198 NE - CZ - NH2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG A 286 NH1 - CZ - NH2 ANGL. DEV. = -14.0 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG B 140 CG - CD - NE ANGL. DEV. = -22.0 DEGREES
REMARK 500 ARG B 140 NH1 - CZ - NH2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG B 140 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 140 NE - CZ - NH2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 183 CD - NE - CZ ANGL. DEV. = 11.9 DEGREES
REMARK 500 ARG B 183 NE - CZ - NH1 ANGL. DEV. = -10.7 DEGREES
REMARK 500 ARG B 183 NE - CZ - NH2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ARG B 198 CD - NE - CZ ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG B 198 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG B 198 NE - CZ - NH2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 ARG B 286 NH1 - CZ - NH2 ANGL. DEV. = -13.8 DEGREES
REMARK 500 ARG B 286 NE - CZ - NH1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG B 286 NE - CZ - NH2 ANGL. DEV. = 4.2 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 ASN A 62 104.07 -54.34
REMARK 500 ASN A 69 89.00 -67.12
REMARK 500 TYR A 92 79.54 -104.91
REMARK 500 LYS A 129 -112.44 47.89
REMARK 500 ASN A 163 13.96 59.51
REMARK 500 GLN A 167 24.18 -140.55
REMARK 500 ALA A 254 -58.77 -133.60
REMARK 500 PRO A 280 152.69 -49.49
REMARK 500 ALA B 41 46.87 -97.38
REMARK 500 ASN B 62 107.71 -55.15
REMARK 500 GLN B 66 63.55 67.51
REMARK 500 ASN B 69 87.56 -69.46
REMARK 500 TYR B 92 62.10 -111.50
REMARK 500 LYS B 129 -105.47 58.40
REMARK 500 GLN B 167 29.90 -140.03
REMARK 500 ALA B 254 -62.28 -136.02
REMARK 500 LYS B 314 140.81 -177.53
REMARK 500 GLU B 346 62.10 -66.50
REMARK 500 ASN B 347 31.44 -90.65
REMARK 500 GLN C1067 -139.11 -103.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 183 0.07 SIDE CHAIN
REMARK 500 ARG B 183 0.07 SIDE CHAIN
REMARK 500 ARG B 198 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 1 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 221 OD1
REMARK 620 2 THR A 223 OG1 101.2
REMARK 620 3 ASN A 225 OD1 81.1 86.0
REMARK 620 4 TYR A 227 O 90.0 160.0 79.4
REMARK 620 5 GLU A 232 OE1 128.8 99.0 147.1 86.4
REMARK 620 6 HOH A 432 O 163.8 63.6 91.9 103.1 62.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 2 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 221 OD1
REMARK 620 2 THR B 223 OG1 94.1
REMARK 620 3 ASN B 225 OD1 91.4 86.9
REMARK 620 4 TYR B 227 O 98.3 164.6 83.8
REMARK 620 5 GLU B 232 OE2 122.3 92.6 146.2 88.4
REMARK 620 6 HOH B 388 O 155.2 61.3 90.3 106.4 60.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 11
DBREF 3PFV A 38 344 UNP Q13191 CBLB_HUMAN 38 344
DBREF 3PFV B 38 344 UNP Q13191 CBLB_HUMAN 38 344
DBREF 3PFV C 1066 1076 UNP P00533 EGFR_HUMAN 1066 1076
DBREF 3PFV D 1066 1076 UNP P00533 EGFR_HUMAN 1066 1076
SEQADV 3PFV MET A 37 UNP Q13191 INITIATING METHIONINE
SEQADV 3PFV ALA A 345 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV GLU A 346 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV ASN A 347 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV LEU A 348 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV TYR A 349 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV PHE A 350 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV GLN A 351 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV MET B 37 UNP Q13191 INITIATING METHIONINE
SEQADV 3PFV ALA B 345 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV GLU B 346 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV ASN B 347 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV LEU B 348 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV TYR B 349 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV PHE B 350 UNP Q13191 EXPRESSION TAG
SEQADV 3PFV GLN B 351 UNP Q13191 EXPRESSION TAG
SEQRES 1 A 315 MET GLN ALA ALA ALA ASP ARG ARG THR VAL GLU LYS THR
SEQRES 2 A 315 TRP LYS LEU MET ASP LYS VAL VAL ARG LEU CYS GLN ASN
SEQRES 3 A 315 PRO LYS LEU GLN LEU LYS ASN SER PRO PRO TYR ILE LEU
SEQRES 4 A 315 ASP ILE LEU PRO ASP THR TYR GLN HIS LEU ARG LEU ILE
SEQRES 5 A 315 LEU SER LYS TYR ASP ASP ASN GLN LYS LEU ALA GLN LEU
SEQRES 6 A 315 SER GLU ASN GLU TYR PHE LYS ILE TYR ILE ASP SER LEU
SEQRES 7 A 315 MET LYS LYS SER LYS ARG ALA ILE ARG LEU PHE LYS GLU
SEQRES 8 A 315 GLY LYS GLU ARG MET TYR GLU GLU GLN SER GLN ASP ARG
SEQRES 9 A 315 ARG ASN LEU THR LYS LEU SER LEU ILE PHE SER HIS MET
SEQRES 10 A 315 LEU ALA GLU ILE LYS ALA ILE PHE PRO ASN GLY GLN PHE
SEQRES 11 A 315 GLN GLY ASP ASN PHE ARG ILE THR LYS ALA ASP ALA ALA
SEQRES 12 A 315 GLU PHE TRP ARG LYS PHE PHE GLY ASP LYS THR ILE VAL
SEQRES 13 A 315 PRO TRP LYS VAL PHE ARG GLN CYS LEU HIS GLU VAL HIS
SEQRES 14 A 315 GLN ILE SER SER GLY LEU GLU ALA MET ALA LEU LYS SER
SEQRES 15 A 315 THR ILE ASP LEU THR CYS ASN ASP TYR ILE SER VAL PHE
SEQRES 16 A 315 GLU PHE ASP ILE PHE THR ARG LEU PHE GLN PRO TRP GLY
SEQRES 17 A 315 SER ILE LEU ARG ASN TRP ASN PHE LEU ALA VAL THR HIS
SEQRES 18 A 315 PRO GLY TYR MET ALA PHE LEU THR TYR ASP GLU VAL LYS
SEQRES 19 A 315 ALA ARG LEU GLN LYS TYR SER THR LYS PRO GLY SER TYR
SEQRES 20 A 315 ILE PHE ARG LEU SER CYS THR ARG LEU GLY GLN TRP ALA
SEQRES 21 A 315 ILE GLY TYR VAL THR GLY ASP GLY ASN ILE LEU GLN THR
SEQRES 22 A 315 ILE PRO HIS ASN LYS PRO LEU PHE GLN ALA LEU ILE ASP
SEQRES 23 A 315 GLY SER ARG GLU GLY PHE TYR LEU TYR PRO ASP GLY ARG
SEQRES 24 A 315 SER TYR ASN PRO ASP LEU THR GLY LEU ALA GLU ASN LEU
SEQRES 25 A 315 TYR PHE GLN
SEQRES 1 B 315 MET GLN ALA ALA ALA ASP ARG ARG THR VAL GLU LYS THR
SEQRES 2 B 315 TRP LYS LEU MET ASP LYS VAL VAL ARG LEU CYS GLN ASN
SEQRES 3 B 315 PRO LYS LEU GLN LEU LYS ASN SER PRO PRO TYR ILE LEU
SEQRES 4 B 315 ASP ILE LEU PRO ASP THR TYR GLN HIS LEU ARG LEU ILE
SEQRES 5 B 315 LEU SER LYS TYR ASP ASP ASN GLN LYS LEU ALA GLN LEU
SEQRES 6 B 315 SER GLU ASN GLU TYR PHE LYS ILE TYR ILE ASP SER LEU
SEQRES 7 B 315 MET LYS LYS SER LYS ARG ALA ILE ARG LEU PHE LYS GLU
SEQRES 8 B 315 GLY LYS GLU ARG MET TYR GLU GLU GLN SER GLN ASP ARG
SEQRES 9 B 315 ARG ASN LEU THR LYS LEU SER LEU ILE PHE SER HIS MET
SEQRES 10 B 315 LEU ALA GLU ILE LYS ALA ILE PHE PRO ASN GLY GLN PHE
SEQRES 11 B 315 GLN GLY ASP ASN PHE ARG ILE THR LYS ALA ASP ALA ALA
SEQRES 12 B 315 GLU PHE TRP ARG LYS PHE PHE GLY ASP LYS THR ILE VAL
SEQRES 13 B 315 PRO TRP LYS VAL PHE ARG GLN CYS LEU HIS GLU VAL HIS
SEQRES 14 B 315 GLN ILE SER SER GLY LEU GLU ALA MET ALA LEU LYS SER
SEQRES 15 B 315 THR ILE ASP LEU THR CYS ASN ASP TYR ILE SER VAL PHE
SEQRES 16 B 315 GLU PHE ASP ILE PHE THR ARG LEU PHE GLN PRO TRP GLY
SEQRES 17 B 315 SER ILE LEU ARG ASN TRP ASN PHE LEU ALA VAL THR HIS
SEQRES 18 B 315 PRO GLY TYR MET ALA PHE LEU THR TYR ASP GLU VAL LYS
SEQRES 19 B 315 ALA ARG LEU GLN LYS TYR SER THR LYS PRO GLY SER TYR
SEQRES 20 B 315 ILE PHE ARG LEU SER CYS THR ARG LEU GLY GLN TRP ALA
SEQRES 21 B 315 ILE GLY TYR VAL THR GLY ASP GLY ASN ILE LEU GLN THR
SEQRES 22 B 315 ILE PRO HIS ASN LYS PRO LEU PHE GLN ALA LEU ILE ASP
SEQRES 23 B 315 GLY SER ARG GLU GLY PHE TYR LEU TYR PRO ASP GLY ARG
SEQRES 24 B 315 SER TYR ASN PRO ASP LEU THR GLY LEU ALA GLU ASN LEU
SEQRES 25 B 315 TYR PHE GLN
SEQRES 1 C 11 LEU GLN ARG PTR SER SER ASP PRO THR GLY ALA
SEQRES 1 D 11 LEU GLN ARG PTR SER SER ASP PRO THR GLY ALA
MODRES 3PFV PTR C 1069 TYR O-PHOSPHOTYROSINE
MODRES 3PFV PTR D 1069 TYR O-PHOSPHOTYROSINE
HET PTR C1069 16
HET PTR D1069 16
HET NA A 1 1
HET CL A 3 1
HET CL A 4 1
HET SO4 A 2 5
HET SO4 A 352 5
HET SO4 A 6 5
HET SO4 A 7 5
HET EDO A 8 8
HET EDO A 9 4
HET EDO A 10 4
HET NA B 2 1
HET SO4 B 1 5
HET SO4 B 3 5
HET SO4 B 5 5
HET PG4 B 11 13
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN PTR PHOSPHONOTYROSINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 PTR 2(C9 H12 N O6 P)
FORMUL 5 NA 2(NA 1+)
FORMUL 6 CL 2(CL 1-)
FORMUL 8 SO4 7(O4 S 2-)
FORMUL 12 EDO 3(C2 H6 O2)
FORMUL 19 PG4 C8 H18 O5
FORMUL 20 HOH *220(H2 O)
HELIX 1 1 ARG A 44 GLN A 61 1 18
HELIX 2 2 ASN A 62 GLN A 66 5 5
HELIX 3 3 TYR A 73 TYR A 92 1 20
HELIX 4 4 ASP A 94 GLU A 103 1 10
HELIX 5 5 ASN A 104 LYS A 129 1 26
HELIX 6 6 GLU A 130 GLU A 134 5 5
HELIX 7 7 SER A 137 PHE A 161 1 25
HELIX 8 8 PRO A 162 GLN A 165 5 4
HELIX 9 9 GLN A 167 PHE A 171 5 5
HELIX 10 10 LYS A 175 GLY A 187 1 13
HELIX 11 11 TRP A 194 HIS A 205 1 12
HELIX 12 12 SER A 209 ASP A 221 1 13
HELIX 13 13 VAL A 230 PHE A 240 1 11
HELIX 14 14 PRO A 242 GLY A 244 5 3
HELIX 15 15 SER A 245 ALA A 254 1 10
HELIX 16 16 THR A 265 GLN A 274 1 10
HELIX 17 17 LYS A 275 SER A 277 5 3
HELIX 18 18 PRO A 315 GLU A 326 1 12
HELIX 19 19 LEU A 341 ALA A 345 5 5
HELIX 20 20 ASP B 42 GLN B 61 1 20
HELIX 21 21 ASN B 62 GLN B 66 5 5
HELIX 22 22 TYR B 73 TYR B 92 1 20
HELIX 23 23 ASP B 94 GLU B 103 1 10
HELIX 24 24 ASN B 104 LYS B 129 1 26
HELIX 25 25 GLU B 130 TYR B 133 5 4
HELIX 26 26 SER B 137 PHE B 161 1 25
HELIX 27 27 PRO B 162 GLN B 165 5 4
HELIX 28 28 GLN B 167 PHE B 171 5 5
HELIX 29 29 LYS B 175 GLY B 187 1 13
HELIX 30 30 TRP B 194 HIS B 205 1 12
HELIX 31 31 SER B 209 ASP B 221 1 13
HELIX 32 32 VAL B 230 PHE B 240 1 11
HELIX 33 33 PRO B 242 GLY B 244 5 3
HELIX 34 34 SER B 245 ALA B 254 1 10
HELIX 35 35 THR B 265 LYS B 275 1 11
HELIX 36 36 PRO B 315 GLU B 326 1 12
HELIX 37 37 LEU B 341 GLU B 346 1 6
SHEET 1 A 2 ILE A 191 PRO A 193 0
SHEET 2 A 2 TYR A 227 SER A 229 -1 O ILE A 228 N VAL A 192
SHEET 1 B 4 ILE A 306 THR A 309 0
SHEET 2 B 4 TRP A 295 VAL A 300 -1 N ILE A 297 O THR A 309
SHEET 3 B 4 SER A 282 LEU A 287 -1 N ARG A 286 O ALA A 296
SHEET 4 B 4 TYR A 331 PRO A 332 1 O TYR A 331 N TYR A 283
SHEET 1 C 2 ILE B 191 PRO B 193 0
SHEET 2 C 2 TYR B 227 SER B 229 -1 O ILE B 228 N VAL B 192
SHEET 1 D 4 ILE B 306 THR B 309 0
SHEET 2 D 4 TRP B 295 VAL B 300 -1 N ILE B 297 O THR B 309
SHEET 3 D 4 SER B 282 LEU B 287 -1 N ARG B 286 O ALA B 296
SHEET 4 D 4 TYR B 331 PRO B 332 1 O TYR B 331 N TYR B 283
LINK C ARG C1068 N PTR C1069 1555 1555 1.33
LINK C PTR C1069 N SER C1070 1555 1555 1.33
LINK C ARG D1068 N PTR D1069 1555 1555 1.33
LINK C PTR D1069 N SER D1070 1555 1555 1.33
LINK NA NA A 1 OD1 ASP A 221 1555 1555 2.49
LINK NA NA A 1 OG1 THR A 223 1555 1555 2.61
LINK NA NA A 1 OD1 ASN A 225 1555 1555 2.45
LINK NA NA A 1 O TYR A 227 1555 1555 2.35
LINK NA NA A 1 OE1 GLU A 232 1555 1555 2.37
LINK NA NA A 1 O HOH A 432 1555 1555 2.91
LINK NA NA B 2 OD1 ASP B 221 1555 1555 2.43
LINK NA NA B 2 OG1 THR B 223 1555 1555 2.68
LINK NA NA B 2 OD1 ASN B 225 1555 1555 2.38
LINK NA NA B 2 O TYR B 227 1555 1555 2.20
LINK NA NA B 2 OE2 GLU B 232 1555 1555 2.37
LINK NA NA B 2 O HOH B 388 1555 1555 2.89
CISPEP 1 PRO A 71 PRO A 72 0 1.90
CISPEP 2 GLN A 241 PRO A 242 0 4.16
CISPEP 3 PRO B 71 PRO B 72 0 1.50
CISPEP 4 GLN B 241 PRO B 242 0 4.10
SITE 1 AC1 6 ASP A 221 THR A 223 ASN A 225 TYR A 227
SITE 2 AC1 6 GLU A 232 HOH A 432
SITE 1 AC2 5 ASN A 104 GLU A 105 TYR A 106 HOH A 409
SITE 2 AC2 5 HOH A 410
SITE 1 AC3 2 HIS A 312 ASN A 313
SITE 1 AC4 5 THR A 174 LYS A 175 ARG A 238 GLN A 241
SITE 2 AC4 5 HOH A 444
SITE 1 AC5 3 ARG A 335 SER A 336 GLN B 206
SITE 1 AC6 4 ARG A 325 HOH A 393 ARG B 44 LYS B 48
SITE 1 AC7 5 ARG A 172 ARG B 291 LEU D1066 ARG D1068
SITE 2 AC7 5 PTR D1069
SITE 1 AC8 3 LYS A 195 ARG A 198 ARG B 272
SITE 1 AC9 1 HOH A 430
SITE 1 BC1 3 ARG A 272 HOH A 437 ARG B 198
SITE 1 BC2 6 ASP B 221 THR B 223 ASN B 225 TYR B 227
SITE 2 BC2 6 GLU B 232 HOH B 388
SITE 1 BC3 3 LYS B 175 ARG B 238 GLN B 241
SITE 1 BC4 6 GLN A 206 HOH B 25 ARG B 335 SER B 336
SITE 2 BC4 6 HOH B 392 HOH B 406
SITE 1 BC5 2 GLN B 138 ARG B 141
SITE 1 BC6 5 ARG A 141 HOH A 436 TRP B 194 MET B 214
SITE 2 BC6 5 HOH B 398
CRYST1 60.063 98.934 61.978 90.00 110.63 90.00 P 1 21 1 4
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 0.016649 0.000000 0.006269 0.00000
SCALE2 0.000000 0.010108 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017241 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
