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PDBsum entry 3mdy

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Transferase/isomerase PDB id
3mdy
Jmol
Contents
Protein chains
320 a.a.
109 a.a.
Ligands
LDN ×2
Waters ×687
HEADER    TRANSFERASE/ISOMERASE                   31-MAR-10   3MDY
TITLE     CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE BONE MORPHOGENETIC
TITLE    2 PROTEIN RECEPTOR TYPE-1B (BMPR1B) IN COMPLEX WITH FKBP12 AND LDN-
TITLE    3 193189
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE-1B;
COMPND   3 CHAIN: A, C;
COMPND   4 FRAGMENT: BMPR1B CYTOPLASMIC (GS AND KINASE) DOMAIN (RESIDUE 168-
COMPND   5 502);
COMPND   6 SYNONYM: BMPR1B, BMP TYPE-1B RECEPTOR, BMPR-1B;
COMPND   7 EC: 2.7.11.30;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP1A;
COMPND  11 CHAIN: B, D;
COMPND  12 FRAGMENT: FKBP12;
COMPND  13 SYNONYM: FKBP12, PPIASE FKBP1A, FK506-BINDING PROTEIN 1A, FKBP-1A,
COMPND  14 ROTAMASE, IMMUNOPHILIN FKBP12, 12 KDA FK506-BINDING PROTEIN, 12 KDA
COMPND  15 FKBP, FKBP-12;
COMPND  16 EC: 5.2.1.8;
COMPND  17 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: BMPR1B;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFB-LIC-BSE;
SOURCE  12 MOL_ID: 2;
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  14 ORGANISM_COMMON: HUMAN;
SOURCE  15 ORGANISM_TAXID: 9606;
SOURCE  16 GENE: FKBP12;
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS    COMPLEX (ISOMERASE-PROTEIN KINASE), RECEPTOR SERINE/THREONINE KINASE,
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC, ATP-BINDING, DISEASE MUTATION,
KEYWDS   3 KINASE, TRANSFERASE, ROTAMASE, TRANSFERASE-ISOMERASE COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.CHAIKUAD,C.SANVITALE,P.MAHAJAN,N.DAGA,C.COOPER,T.KROJER,I.ALFANO,
AUTHOR   2 S.KNAPP,F.VON DELFT,J.WEIGELT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,
AUTHOR   3 A.BULLOCK,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT   1   19-MAY-10 3MDY    0
JRNL        AUTH   A.CHAIKUAD,C.SANVITALE,P.MAHAJAN,N.DAGA,C.COOPER,T.KROJER,
JRNL        AUTH 2 I.ALFANO,S.KNAPP,F.VON DELFT,J.WEIGELT,C.H.ARROWSMITH,
JRNL        AUTH 3 A.M.EDWARDS,C.BOUNTRA,A.BULLOCK,
JRNL        AUTH 4 STRUCTURAL GENOMICS CONSORTIUM (SGC)
JRNL        TITL   CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE BONE
JRNL        TITL 2 MORPHOGENETIC PROTEIN RECEPTOR TYPE-1B (BMPR1B) IN COMPLEX
JRNL        TITL 3 WITH FKBP12 AND LDN-193189
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.65
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5
REMARK   3   NUMBER OF REFLECTIONS             : 57883
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) : 0.204
REMARK   3   R VALUE            (WORKING SET) : 0.201
REMARK   3   FREE R VALUE                     : 0.255
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3085
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) : 2.05
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4071
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.42
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3010
REMARK   3   BIN FREE R VALUE SET COUNT          : 234
REMARK   3   BIN FREE R VALUE                    : 0.3090
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 6727
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 62
REMARK   3   SOLVENT ATOMS            : 687
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 25.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.03
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.73000
REMARK   3    B22 (A**2) : 2.56000
REMARK   3    B33 (A**2) : -1.83000
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): 0.219
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.192
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.983
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7003 ; 0.015 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  4873 ; 0.002 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9471 ; 1.422 ; 1.973
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11820 ; 0.926 ; 3.001
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   872 ; 6.079 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   290 ;32.449 ;23.379
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1250 ;14.462 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;19.707 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1031 ; 0.091 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7697 ; 0.006 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  1406 ; 0.002 ; 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):  4283 ; 3.706 ; 3.000
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1753 ; 0.894 ; 3.000
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6906 ; 5.486 ; 5.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2720 ; 7.434 ; 8.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2555 ; 9.839 ;11.000
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                    : D B
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     D      0       D     108      2
REMARK   3           1     B      0       B     108      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    D    (A):    633 ;  0.02 ;  0.05
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    796 ;  0.06 ;  0.50
REMARK   3   TIGHT THERMAL      1    D (A**2):    633 ;  0.15 ;  0.50
REMARK   3   MEDIUM THERMAL     1    B (A**2):    796 ;  0.11 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : A C
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A    174       A     175      4
REMARK   3           1     C    174       C     175      4
REMARK   3           2     A    177       A     178      4
REMARK   3           2     C    177       C     178      4
REMARK   3           3     A    180       A     189      4
REMARK   3           3     C    180       C     189      4
REMARK   3           4     A    190       A     204      2
REMARK   3           4     C    190       C     204      2
REMARK   3           5     A    206       A     222      2
REMARK   3           5     C    206       C     222      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   2    A    (A):    186 ;  0.04 ;  0.05
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    396 ;  0.04 ;  0.50
REMARK   3   TIGHT THERMAL      2    A (A**2):    186 ;  0.18 ;  0.50
REMARK   3   MEDIUM THERMAL     2    C (A**2):    396 ;  0.10 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 3
REMARK   3     CHAIN NAMES                    : C A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 6
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     C    226       C     253      2
REMARK   3           1     A    226       A     253      2
REMARK   3           2     C    255       C     268      2
REMARK   3           2     A    255       A     268      2
REMARK   3           3     C    269       C     273      6
REMARK   3           3     A    269       A     273      6
REMARK   3           4     C    274       C     356      2
REMARK   3           4     A    274       A     356      2
REMARK   3           5     C    370       C     388      4
REMARK   3           5     A    370       A     388      4
REMARK   3           6     C    390       C     500      2
REMARK   3           6     A    390       A     500      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   3    C    (A):   1396 ;  0.04 ;  0.05
REMARK   3   MEDIUM POSITIONAL  3    A    (A):   1987 ;  0.05 ;  0.50
REMARK   3   LOOSE POSITIONAL   3    C    (A):     61 ;  0.08 ;  5.00
REMARK   3   TIGHT THERMAL      3    C (A**2):   1396 ;  0.21 ;  0.50
REMARK   3   MEDIUM THERMAL     3    A (A**2):   1987 ;  0.16 ;  2.00
REMARK   3   LOOSE THERMAL      3    C (A**2):     61 ;  0.20 ; 10.00
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 12
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   174        A   202
REMARK   3    ORIGIN FOR THE GROUP (A):  24.9675   6.7593  55.9651
REMARK   3    T TENSOR
REMARK   3      T11:   0.0414 T22:   0.2287
REMARK   3      T33:   0.0579 T12:  -0.0101
REMARK   3      T13:   0.0236 T23:  -0.0691
REMARK   3    L TENSOR
REMARK   3      L11:   8.0398 L22:   2.0275
REMARK   3      L33:   4.9602 L12:   2.4462
REMARK   3      L13:  -0.2378 L23:  -1.0077
REMARK   3    S TENSOR
REMARK   3      S11:   0.1950 S12:  -0.8312 S13:   0.4860
REMARK   3      S21:   0.1428 S22:  -0.1303 S23:   0.2994
REMARK   3      S31:  -0.1144 S32:  -0.4082 S33:  -0.0647
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   203        A   273
REMARK   3    ORIGIN FOR THE GROUP (A):  38.1429   4.8401  51.1508
REMARK   3    T TENSOR
REMARK   3      T11:   0.0839 T22:   0.1212
REMARK   3      T33:   0.0883 T12:   0.0021
REMARK   3      T13:   0.0172 T23:   0.0243
REMARK   3    L TENSOR
REMARK   3      L11:   0.7616 L22:   0.1217
REMARK   3      L33:   1.5606 L12:   0.0209
REMARK   3      L13:   0.9559 L23:   0.2345
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0527 S12:   0.1472 S13:   0.0337
REMARK   3      S21:   0.0290 S22:  -0.0761 S23:   0.0435
REMARK   3      S31:  -0.0123 S32:   0.0576 S33:   0.1287
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   274        A   369
REMARK   3    ORIGIN FOR THE GROUP (A):  44.1638   2.7285  65.0923
REMARK   3    T TENSOR
REMARK   3      T11:   0.0982 T22:   0.0606
REMARK   3      T33:   0.0923 T12:   0.0023
REMARK   3      T13:   0.0104 T23:   0.0169
REMARK   3    L TENSOR
REMARK   3      L11:   0.5961 L22:   0.0618
REMARK   3      L33:   0.6427 L12:   0.0111
REMARK   3      L13:   0.4616 L23:   0.1407
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0504 S12:   0.0028 S13:   0.0480
REMARK   3      S21:   0.0244 S22:  -0.0182 S23:   0.0174
REMARK   3      S31:   0.0232 S32:  -0.0259 S33:   0.0686
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   370        A   502
REMARK   3    ORIGIN FOR THE GROUP (A):  58.1916  -2.4098  70.3249
REMARK   3    T TENSOR
REMARK   3      T11:   0.0929 T22:   0.0939
REMARK   3      T33:   0.0790 T12:   0.0505
REMARK   3      T13:   0.0248 T23:   0.0476
REMARK   3    L TENSOR
REMARK   3      L11:   0.8281 L22:   0.5765
REMARK   3      L33:   1.0699 L12:   0.5225
REMARK   3      L13:   0.6153 L23:   0.0334
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0129 S12:   0.0022 S13:   0.0195
REMARK   3      S21:   0.0083 S22:  -0.0693 S23:  -0.0081
REMARK   3      S31:   0.0725 S32:   0.1595 S33:   0.0822
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 :   B     0        B    67
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6752   4.0124  44.9094
REMARK   3    T TENSOR
REMARK   3      T11:   0.0124 T22:   0.2537
REMARK   3      T33:   0.1017 T12:  -0.0044
REMARK   3      T13:   0.0199 T23:   0.0878
REMARK   3    L TENSOR
REMARK   3      L11:   2.7838 L22:   0.7101
REMARK   3      L33:   1.6475 L12:  -0.3681
REMARK   3      L13:  -1.8042 L23:  -0.2326
REMARK   3    S TENSOR
REMARK   3      S11:   0.0926 S12:   0.3246 S13:   0.1331
REMARK   3      S21:  -0.0361 S22:   0.0723 S23:  -0.0850
REMARK   3      S31:  -0.0667 S32:  -0.4259 S33:  -0.1649
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 :   B    68        B   108
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2287  -1.2570  44.3658
REMARK   3    T TENSOR
REMARK   3      T11:   0.0143 T22:   0.2212
REMARK   3      T33:   0.0269 T12:  -0.0346
REMARK   3      T13:  -0.0032 T23:  -0.0029
REMARK   3    L TENSOR
REMARK   3      L11:   1.7971 L22:   1.3802
REMARK   3      L33:   1.7025 L12:  -0.6463
REMARK   3      L13:  -1.3888 L23:  -0.3501
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1441 S12:   0.1657 S13:  -0.0282
REMARK   3      S21:  -0.0065 S22:   0.1490 S23:   0.0287
REMARK   3      S31:   0.1451 S32:  -0.2937 S33:  -0.0049
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 :   C   174        C   201
REMARK   3    ORIGIN FOR THE GROUP (A):  40.6469   6.6888  13.0983
REMARK   3    T TENSOR
REMARK   3      T11:   0.0754 T22:   0.3070
REMARK   3      T33:   0.0853 T12:  -0.0164
REMARK   3      T13:   0.0272 T23:   0.0628
REMARK   3    L TENSOR
REMARK   3      L11:   4.9327 L22:   1.5684
REMARK   3      L33:   3.3397 L12:  -1.3411
REMARK   3      L13:   1.6687 L23:  -0.3333
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0262 S12:   0.8025 S13:   0.3704
REMARK   3      S21:  -0.1715 S22:  -0.1098 S23:  -0.2800
REMARK   3      S31:  -0.1097 S32:   0.7010 S33:   0.1360
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 :   C   202        C   256
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0405   5.1500  17.8387
REMARK   3    T TENSOR
REMARK   3      T11:   0.0778 T22:   0.0561
REMARK   3      T33:   0.0728 T12:  -0.0158
REMARK   3      T13:   0.0200 T23:   0.0004
REMARK   3    L TENSOR
REMARK   3      L11:   0.4684 L22:   0.6200
REMARK   3      L33:   0.6231 L12:  -0.1885
REMARK   3      L13:   0.2268 L23:   0.0247
REMARK   3    S TENSOR
REMARK   3      S11:   0.0379 S12:  -0.0790 S13:   0.0200
REMARK   3      S21:   0.0141 S22:  -0.0290 S23:  -0.1144
REMARK   3      S31:  -0.0209 S32:   0.0749 S33:  -0.0090
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 :   C   257        C   373
REMARK   3    ORIGIN FOR THE GROUP (A):  22.3068   2.2488   7.5905
REMARK   3    T TENSOR
REMARK   3      T11:   0.0902 T22:   0.0796
REMARK   3      T33:   0.0836 T12:   0.0114
REMARK   3      T13:   0.0129 T23:   0.0071
REMARK   3    L TENSOR
REMARK   3      L11:   0.6879 L22:   0.0244
REMARK   3      L33:   0.9394 L12:   0.0916
REMARK   3      L13:   0.2544 L23:   0.0824
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0202 S12:  -0.0121 S13:   0.0145
REMARK   3      S21:  -0.0186 S22:  -0.0261 S23:  -0.0024
REMARK   3      S31:   0.0154 S32:   0.0569 S33:   0.0463
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 :   C   374        C   500
REMARK   3    ORIGIN FOR THE GROUP (A):   7.0158  -2.0467  -0.9074
REMARK   3    T TENSOR
REMARK   3      T11:   0.0742 T22:   0.2325
REMARK   3      T33:   0.0609 T12:  -0.0629
REMARK   3      T13:   0.0273 T23:  -0.0541
REMARK   3    L TENSOR
REMARK   3      L11:   0.5792 L22:   0.9163
REMARK   3      L33:   1.4119 L12:  -0.2291
REMARK   3      L13:   0.7061 L23:  -0.1012
REMARK   3    S TENSOR
REMARK   3      S11:   0.0126 S12:   0.0214 S13:   0.0120
REMARK   3      S21:  -0.0964 S22:  -0.1103 S23:   0.0180
REMARK   3      S31:   0.1366 S32:  -0.3256 S33:   0.0977
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 :   D     0        D    43
REMARK   3    ORIGIN FOR THE GROUP (A):  55.0632   2.2557  23.6425
REMARK   3    T TENSOR
REMARK   3      T11:   0.0468 T22:   0.3961
REMARK   3      T33:   0.0412 T12:   0.0417
REMARK   3      T13:  -0.0006 T23:  -0.0844
REMARK   3    L TENSOR
REMARK   3      L11:   4.7033 L22:   0.4019
REMARK   3      L33:   1.1736 L12:   0.1500
REMARK   3      L13:  -1.2469 L23:   0.5329
REMARK   3    S TENSOR
REMARK   3      S11:   0.0058 S12:  -0.4595 S13:   0.1822
REMARK   3      S21:   0.0459 S22:   0.1313 S23:  -0.0323
REMARK   3      S31:   0.0769 S32:   0.4194 S33:  -0.1371
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 :   D    44        D   108
REMARK   3    ORIGIN FOR THE GROUP (A):  49.7196   2.2712  25.8548
REMARK   3    T TENSOR
REMARK   3      T11:   0.0295 T22:   0.2306
REMARK   3      T33:   0.0737 T12:   0.0212
REMARK   3      T13:  -0.0016 T23:  -0.0518
REMARK   3    L TENSOR
REMARK   3      L11:   5.1347 L22:   0.8376
REMARK   3      L33:   1.6695 L12:   0.3814
REMARK   3      L13:  -1.9646 L23:   0.3430
REMARK   3    S TENSOR
REMARK   3      S11:   0.0126 S12:  -0.3185 S13:   0.1608
REMARK   3      S21:  -0.0052 S22:   0.1743 S23:   0.1118
REMARK   3      S31:   0.0226 S32:   0.5095 S33:  -0.1868
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 3MDY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058425.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-10
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : DIAMOND
REMARK 200  BEAMLINE                       : I02
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795
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                  : 3X3 CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60968
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.790
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9
REMARK 200  DATA REDUNDANCY                : 5.400
REMARK 200  R MERGE                    (I) : 0.12000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70
REMARK 200  R MERGE FOR SHELL          (I) : 0.52100
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   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 ENTRY: 3H9R CHAIN A, AND CHAIN B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M NA MALONATE, PH
REMARK 280  7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
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       32.70500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       91.66500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.00500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       91.66500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.70500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.00500
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 300 REMARK: AUTHOR STATES THAT THE BIOLOGICAL ASSEMBLY IS UNKNOWN.
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: 1790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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     SER A   166
REMARK 465     MET A   167
REMARK 465     THR A   168
REMARK 465     TYR A   169
REMARK 465     ILE A   170
REMARK 465     PRO A   171
REMARK 465     PRO A   172
REMARK 465     GLY A   173
REMARK 465     SER A   359
REMARK 465     ASP A   360
REMARK 465     THR A   361
REMARK 465     ASN A   362
REMARK 465     GLU A   363
REMARK 465     VAL A   364
REMARK 465     ASP A   365
REMARK 465     ILE A   366
REMARK 465     PRO A   367
REMARK 465     SER C   166
REMARK 465     MET C   167
REMARK 465     THR C   168
REMARK 465     TYR C   169
REMARK 465     ILE C   170
REMARK 465     PRO C   171
REMARK 465     PRO C   172
REMARK 465     GLY C   173
REMARK 465     SER C   359
REMARK 465     ASP C   360
REMARK 465     THR C   361
REMARK 465     ASN C   362
REMARK 465     GLU C   363
REMARK 465     VAL C   364
REMARK 465     ASP C   365
REMARK 465     LYS C   501
REMARK 465     LEU C   502
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     GLU A 174    CG   CD   OE1  OE2
REMARK 470     ARG A 177    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 323    CG   CD   OE1  NE2
REMARK 470     LYS A 342    CE   NZ
REMARK 470     ILE A 358    CG1  CG2  CD1
REMARK 470     GLU A 496    CD   OE1  OE2
REMARK 470     LYS A 501    CG   CD   CE   NZ
REMARK 470     GLU C 174    CG   CD   OE1  OE2
REMARK 470     ARG C 177    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLU C 181    CD   OE1  OE2
REMARK 470     LYS C 299    CE   NZ
REMARK 470     GLN C 323    CG   CD   OE1  NE2
REMARK 470     ILE C 366    CG1  CG2  CD1
REMARK 470     LYS C 493    CD   CE   NZ
REMARK 470     GLU C 496    CD   OE1  OE2
REMARK 470     GLN C 498    CG   CD   OE1  NE2
REMARK 470     ILE C 500    CG1  CG2  CD1
REMARK 470     MET B   1    CG   SD   CE
REMARK 470     ARG B  14    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B  53    CE   NZ
REMARK 470     MET D   1    CG   SD   CE
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 A   617     O    HOH A   670              2.05
REMARK 500   O    HOH A   513     O    HOH A   683              2.15
REMARK 500   OE1  GLU A   318     O    HOH A   670              2.16
REMARK 500   O    HOH D   593     O    HOH D   594              2.16
REMARK 500   O    HOH B   120     O    HOH B   125              2.16
REMARK 500   O    HOH C   533     O    HOH C   637              2.19
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    ASP C 399   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP C 499   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 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    SER A 175       98.54    -62.82
REMARK 500    SER A 186      -72.95    -57.81
REMARK 500    SER A 188      -67.78     78.65
REMARK 500    HIS A 255      141.84   -170.19
REMARK 500    ASP A 332       42.72   -147.82
REMARK 500    ASP A 350       77.58     66.98
REMARK 500    ILE A 446      -64.35    -91.17
REMARK 500    GLN A 498       11.70   -140.16
REMARK 500    SER C 186      -75.11    -57.90
REMARK 500    SER C 188      -67.26     79.07
REMARK 500    HIS C 255      142.47   -172.74
REMARK 500    ARG C 331        4.36     81.21
REMARK 500    ASP C 332       41.12   -149.37
REMARK 500    ASP C 350       73.16     70.60
REMARK 500    ILE C 446      -64.73    -94.38
REMARK 500    ARG B  14      -33.99   -139.13
REMARK 500    ALA B  82     -121.87   -129.48
REMARK 500    ILE B  91      -53.00   -122.49
REMARK 500    ARG D  14      -31.09   -140.19
REMARK 500    ALA D  82     -123.58   -130.21
REMARK 500    ILE D  91      -55.03   -121.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LDN C 1
DBREF  3MDY A  168   502  UNP    O00238   BMR1B_HUMAN    168    502
DBREF  3MDY C  168   502  UNP    O00238   BMR1B_HUMAN    168    502
DBREF  3MDY B    1   108  UNP    P62942   FKB1A_HUMAN      1    108
DBREF  3MDY D    1   108  UNP    P62942   FKB1A_HUMAN      1    108
SEQADV 3MDY SER A  166  UNP  O00238              EXPRESSION TAG
SEQADV 3MDY MET A  167  UNP  O00238              EXPRESSION TAG
SEQADV 3MDY SER C  166  UNP  O00238              EXPRESSION TAG
SEQADV 3MDY MET C  167  UNP  O00238              EXPRESSION TAG
SEQADV 3MDY SER B    0  UNP  P62942              EXPRESSION TAG
SEQADV 3MDY SER D    0  UNP  P62942              EXPRESSION TAG
SEQRES   1 A  337  SER MET THR TYR ILE PRO PRO GLY GLU SER LEU ARG ASP
SEQRES   2 A  337  LEU ILE GLU GLN SER GLN SER SER GLY SER GLY SER GLY
SEQRES   3 A  337  LEU PRO LEU LEU VAL GLN ARG THR ILE ALA LYS GLN ILE
SEQRES   4 A  337  GLN MET VAL LYS GLN ILE GLY LYS GLY ARG TYR GLY GLU
SEQRES   5 A  337  VAL TRP MET GLY LYS TRP ARG GLY GLU LYS VAL ALA VAL
SEQRES   6 A  337  LYS VAL PHE PHE THR THR GLU GLU ALA SER TRP PHE ARG
SEQRES   7 A  337  GLU THR GLU ILE TYR GLN THR VAL LEU MET ARG HIS GLU
SEQRES   8 A  337  ASN ILE LEU GLY PHE ILE ALA ALA ASP ILE LYS GLY THR
SEQRES   9 A  337  GLY SER TRP THR GLN LEU TYR LEU ILE THR ASP TYR HIS
SEQRES  10 A  337  GLU ASN GLY SER LEU TYR ASP TYR LEU LYS SER THR THR
SEQRES  11 A  337  LEU ASP ALA LYS SER MET LEU LYS LEU ALA TYR SER SER
SEQRES  12 A  337  VAL SER GLY LEU CYS HIS LEU HIS THR GLU ILE PHE SER
SEQRES  13 A  337  THR GLN GLY LYS PRO ALA ILE ALA HIS ARG ASP LEU LYS
SEQRES  14 A  337  SER LYS ASN ILE LEU VAL LYS LYS ASN GLY THR CYS CYS
SEQRES  15 A  337  ILE ALA ASP LEU GLY LEU ALA VAL LYS PHE ILE SER ASP
SEQRES  16 A  337  THR ASN GLU VAL ASP ILE PRO PRO ASN THR ARG VAL GLY
SEQRES  17 A  337  THR LYS ARG TYR MET PRO PRO GLU VAL LEU ASP GLU SER
SEQRES  18 A  337  LEU ASN ARG ASN HIS PHE GLN SER TYR ILE MET ALA ASP
SEQRES  19 A  337  MET TYR SER PHE GLY LEU ILE LEU TRP GLU VAL ALA ARG
SEQRES  20 A  337  ARG CYS VAL SER GLY GLY ILE VAL GLU GLU TYR GLN LEU
SEQRES  21 A  337  PRO TYR HIS ASP LEU VAL PRO SER ASP PRO SER TYR GLU
SEQRES  22 A  337  ASP MET ARG GLU ILE VAL CYS ILE LYS LYS LEU ARG PRO
SEQRES  23 A  337  SER PHE PRO ASN ARG TRP SER SER ASP GLU CYS LEU ARG
SEQRES  24 A  337  GLN MET GLY LYS LEU MET THR GLU CYS TRP ALA HIS ASN
SEQRES  25 A  337  PRO ALA SER ARG LEU THR ALA LEU ARG VAL LYS LYS THR
SEQRES  26 A  337  LEU ALA LYS MET SER GLU SER GLN ASP ILE LYS LEU
SEQRES   1 C  337  SER MET THR TYR ILE PRO PRO GLY GLU SER LEU ARG ASP
SEQRES   2 C  337  LEU ILE GLU GLN SER GLN SER SER GLY SER GLY SER GLY
SEQRES   3 C  337  LEU PRO LEU LEU VAL GLN ARG THR ILE ALA LYS GLN ILE
SEQRES   4 C  337  GLN MET VAL LYS GLN ILE GLY LYS GLY ARG TYR GLY GLU
SEQRES   5 C  337  VAL TRP MET GLY LYS TRP ARG GLY GLU LYS VAL ALA VAL
SEQRES   6 C  337  LYS VAL PHE PHE THR THR GLU GLU ALA SER TRP PHE ARG
SEQRES   7 C  337  GLU THR GLU ILE TYR GLN THR VAL LEU MET ARG HIS GLU
SEQRES   8 C  337  ASN ILE LEU GLY PHE ILE ALA ALA ASP ILE LYS GLY THR
SEQRES   9 C  337  GLY SER TRP THR GLN LEU TYR LEU ILE THR ASP TYR HIS
SEQRES  10 C  337  GLU ASN GLY SER LEU TYR ASP TYR LEU LYS SER THR THR
SEQRES  11 C  337  LEU ASP ALA LYS SER MET LEU LYS LEU ALA TYR SER SER
SEQRES  12 C  337  VAL SER GLY LEU CYS HIS LEU HIS THR GLU ILE PHE SER
SEQRES  13 C  337  THR GLN GLY LYS PRO ALA ILE ALA HIS ARG ASP LEU LYS
SEQRES  14 C  337  SER LYS ASN ILE LEU VAL LYS LYS ASN GLY THR CYS CYS
SEQRES  15 C  337  ILE ALA ASP LEU GLY LEU ALA VAL LYS PHE ILE SER ASP
SEQRES  16 C  337  THR ASN GLU VAL ASP ILE PRO PRO ASN THR ARG VAL GLY
SEQRES  17 C  337  THR LYS ARG TYR MET PRO PRO GLU VAL LEU ASP GLU SER
SEQRES  18 C  337  LEU ASN ARG ASN HIS PHE GLN SER TYR ILE MET ALA ASP
SEQRES  19 C  337  MET TYR SER PHE GLY LEU ILE LEU TRP GLU VAL ALA ARG
SEQRES  20 C  337  ARG CYS VAL SER GLY GLY ILE VAL GLU GLU TYR GLN LEU
SEQRES  21 C  337  PRO TYR HIS ASP LEU VAL PRO SER ASP PRO SER TYR GLU
SEQRES  22 C  337  ASP MET ARG GLU ILE VAL CYS ILE LYS LYS LEU ARG PRO
SEQRES  23 C  337  SER PHE PRO ASN ARG TRP SER SER ASP GLU CYS LEU ARG
SEQRES  24 C  337  GLN MET GLY LYS LEU MET THR GLU CYS TRP ALA HIS ASN
SEQRES  25 C  337  PRO ALA SER ARG LEU THR ALA LEU ARG VAL LYS LYS THR
SEQRES  26 C  337  LEU ALA LYS MET SER GLU SER GLN ASP ILE LYS LEU
SEQRES   1 B  109  SER MET GLY VAL GLN VAL GLU THR ILE SER PRO GLY ASP
SEQRES   2 B  109  GLY ARG THR PHE PRO LYS ARG GLY GLN THR CYS VAL VAL
SEQRES   3 B  109  HIS TYR THR GLY MET LEU GLU ASP GLY LYS LYS PHE ASP
SEQRES   4 B  109  SER SER ARG ASP ARG ASN LYS PRO PHE LYS PHE MET LEU
SEQRES   5 B  109  GLY LYS GLN GLU VAL ILE ARG GLY TRP GLU GLU GLY VAL
SEQRES   6 B  109  ALA GLN MET SER VAL GLY GLN ARG ALA LYS LEU THR ILE
SEQRES   7 B  109  SER PRO ASP TYR ALA TYR GLY ALA THR GLY HIS PRO GLY
SEQRES   8 B  109  ILE ILE PRO PRO HIS ALA THR LEU VAL PHE ASP VAL GLU
SEQRES   9 B  109  LEU LEU LYS LEU GLU
SEQRES   1 D  109  SER MET GLY VAL GLN VAL GLU THR ILE SER PRO GLY ASP
SEQRES   2 D  109  GLY ARG THR PHE PRO LYS ARG GLY GLN THR CYS VAL VAL
SEQRES   3 D  109  HIS TYR THR GLY MET LEU GLU ASP GLY LYS LYS PHE ASP
SEQRES   4 D  109  SER SER ARG ASP ARG ASN LYS PRO PHE LYS PHE MET LEU
SEQRES   5 D  109  GLY LYS GLN GLU VAL ILE ARG GLY TRP GLU GLU GLY VAL
SEQRES   6 D  109  ALA GLN MET SER VAL GLY GLN ARG ALA LYS LEU THR ILE
SEQRES   7 D  109  SER PRO ASP TYR ALA TYR GLY ALA THR GLY HIS PRO GLY
SEQRES   8 D  109  ILE ILE PRO PRO HIS ALA THR LEU VAL PHE ASP VAL GLU
SEQRES   9 D  109  LEU LEU LYS LEU GLU
HET    LDN  A   1      31
HET    LDN  C   1      31
HETNAM     LDN 4-[6-(4-PIPERAZIN-1-YLPHENYL)PYRAZOLO[1,5-A]PYRIMIDIN-
HETNAM   2 LDN  3-YL]QUINOLINE
FORMUL   5  LDN    2(C25 H22 N6)
FORMUL   7  HOH   *687(H2 O)
HELIX    1   1 SER A  175  GLY A  187  1                                  13
HELIX    2   2 PRO A  193  ARG A  198  1                                   6
HELIX    3   3 THR A  199  ILE A  204  1                                   6
HELIX    4   4 GLU A  237  GLN A  249  1                                  13
HELIX    5   5 THR A  269  TRP A  272  5                                   4
HELIX    6   6 SER A  286  THR A  294  1                                   9
HELIX    7   7 ASP A  297  THR A  317  1                                  21
HELIX    8   8 THR A  374  MET A  378  5                                   5
HELIX    9   9 PRO A  379  ASP A  384  1                                   6
HELIX   10  10 PHE A  392  ARG A  412  1                                  21
HELIX   11  11 SER A  436  CYS A  445  1                                  10
HELIX   12  12 PRO A  454  SER A  459  5                                   6
HELIX   13  13 ASP A  460  TRP A  474  1                                  15
HELIX   14  14 ASN A  477  ARG A  481  5                                   5
HELIX   15  15 THR A  483  SER A  497  1                                  15
HELIX   16  16 SER C  175  GLY C  187  1                                  13
HELIX   17  17 PRO C  193  ARG C  198  1                                   6
HELIX   18  18 THR C  199  ILE C  204  1                                   6
HELIX   19  19 GLU C  237  GLN C  249  1                                  13
HELIX   20  20 THR C  269  TRP C  272  5                                   4
HELIX   21  21 SER C  286  THR C  294  1                                   9
HELIX   22  22 ASP C  297  THR C  317  1                                  21
HELIX   23  23 THR C  374  MET C  378  5                                   5
HELIX   24  24 PRO C  379  ASP C  384  1                                   6
HELIX   25  25 PHE C  392  ARG C  412  1                                  21
HELIX   26  26 SER C  436  CYS C  445  1                                  10
HELIX   27  27 PRO C  454  SER C  459  5                                   6
HELIX   28  28 ASP C  460  TRP C  474  1                                  15
HELIX   29  29 ASN C  477  ARG C  481  5                                   5
HELIX   30  30 THR C  483  SER C  497  1                                  15
HELIX   31  31 ILE B   57  GLN B   66  1                                  10
HELIX   32  32 PRO B   79  ALA B   82  5                                   4
HELIX   33  33 ILE D   57  GLN D   66  1                                  10
HELIX   34  34 PRO D   79  ALA D   82  5                                   4
SHEET    1   A 5 GLN A 205  GLY A 213  0
SHEET    2   A 5 GLY A 216  TRP A 223 -1  O  VAL A 218   N  ILE A 210
SHEET    3   A 5 GLU A 226  PHE A 234 -1  O  VAL A 230   N  TRP A 219
SHEET    4   A 5 GLN A 274  THR A 279 -1  O  LEU A 277   N  LYS A 231
SHEET    5   A 5 PHE A 261  LYS A 267 -1  N  ALA A 263   O  ILE A 278
SHEET    1   B 2 ILE A 328  ALA A 329  0
SHEET    2   B 2 VAL A 355  LYS A 356 -1  O  VAL A 355   N  ALA A 329
SHEET    1   C 2 ILE A 338  VAL A 340  0
SHEET    2   C 2 CYS A 346  ILE A 348 -1  O  CYS A 347   N  LEU A 339
SHEET    1   D 5 GLN C 205  GLY C 213  0
SHEET    2   D 5 GLY C 216  TRP C 223 -1  O  VAL C 218   N  ILE C 210
SHEET    3   D 5 GLU C 226  PHE C 234 -1  O  VAL C 230   N  TRP C 219
SHEET    4   D 5 GLN C 274  THR C 279 -1  O  LEU C 275   N  PHE C 233
SHEET    5   D 5 PHE C 261  LYS C 267 -1  N  ALA C 263   O  ILE C 278
SHEET    1   E 2 ILE C 328  ALA C 329  0
SHEET    2   E 2 VAL C 355  LYS C 356 -1  O  VAL C 355   N  ALA C 329
SHEET    1   F 2 ILE C 338  VAL C 340  0
SHEET    2   F 2 CYS C 346  ILE C 348 -1  O  CYS C 347   N  LEU C 339
SHEET    1   G 5 VAL B   3  SER B   9  0
SHEET    2   G 5 ARG B  72  ILE B  77 -1  O  ARG B  72   N  ILE B   8
SHEET    3   G 5 LEU B  98  LEU B 107 -1  O  PHE B 100   N  LEU B  75
SHEET    4   G 5 THR B  22  LEU B  31 -1  N  MET B  30   O  VAL B  99
SHEET    5   G 5 LYS B  36  SER B  39 -1  O  ASP B  38   N  GLY B  29
SHEET    1   H 5 VAL B   3  SER B   9  0
SHEET    2   H 5 ARG B  72  ILE B  77 -1  O  ARG B  72   N  ILE B   8
SHEET    3   H 5 LEU B  98  LEU B 107 -1  O  PHE B 100   N  LEU B  75
SHEET    4   H 5 THR B  22  LEU B  31 -1  N  MET B  30   O  VAL B  99
SHEET    5   H 5 PHE B  47  MET B  50 -1  O  PHE B  47   N  VAL B  25
SHEET    1   I 5 VAL D   3  SER D   9  0
SHEET    2   I 5 ARG D  72  ILE D  77 -1  O  ARG D  72   N  ILE D   8
SHEET    3   I 5 LEU D  98  LEU D 107 -1  O  PHE D 100   N  LEU D  75
SHEET    4   I 5 THR D  22  LEU D  31 -1  N  MET D  30   O  VAL D  99
SHEET    5   I 5 LYS D  36  SER D  39 -1  O  ASP D  38   N  GLY D  29
SHEET    1   J 5 VAL D   3  SER D   9  0
SHEET    2   J 5 ARG D  72  ILE D  77 -1  O  ARG D  72   N  ILE D   8
SHEET    3   J 5 LEU D  98  LEU D 107 -1  O  PHE D 100   N  LEU D  75
SHEET    4   J 5 THR D  22  LEU D  31 -1  N  MET D  30   O  VAL D  99
SHEET    5   J 5 PHE D  47  MET D  50 -1  O  PHE D  49   N  CYS D  23
SITE     1 AC1 16 HOH A  65  ILE A 210  ALA A 229  LEU A 259
SITE     2 AC1 16 THR A 279  ASP A 280  HIS A 282  GLU A 283
SITE     3 AC1 16 GLY A 285  ASP A 289  LYS A 336  ASN A 337
SITE     4 AC1 16 LEU A 339  ASP A 350  HOH A 527  HOH A 715
SITE     1 AC2 17 HOH C  76  HOH C  93  ILE C 210  ALA C 229
SITE     2 AC2 17 LEU C 259  THR C 279  ASP C 280  HIS C 282
SITE     3 AC2 17 GLU C 283  GLY C 285  ASP C 289  LYS C 336
SITE     4 AC2 17 ASN C 337  LEU C 339  ASP C 350  HOH C 613
SITE     5 AC2 17 HOH C 681
CRYST1   65.410   80.010  183.330  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      0.015288  0.000000  0.000000        0.00000
SCALE2      0.000000  0.012498  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005455        0.00000
      
PROCHECK
Go to PROCHECK summary
 References