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PDBsum entry 1zr4

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Recombination/DNA PDB id
1zr4
Jmol
Contents
Protein chains
183 a.a.
DNA/RNA
HEADER    RECOMBINATION/DNA                       19-MAY-05   1ZR4
TITLE     STRUCTURE OF A SYNAPTIC GAMMA-DELTA RESOLVASE TETRAMER COVALENTLY
TITLE    2 LINKED TO TWO CLEAVED DNAS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TCAGTGTCCGATAATTTAT;
COMPND   3 CHAIN: X, J, U, M;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: AAA;
COMPND   7 CHAIN: Z, I, W, O;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 3;
COMPND  10 MOLECULE: TTATCGGACACTG;
COMPND  11 CHAIN: Y, K, V, N;
COMPND  12 ENGINEERED: YES;
COMPND  13 MOL_ID: 4;
COMPND  14 MOLECULE: TRANSPOSON GAMMA-DELTA RESOLVASE;
COMPND  15 CHAIN: A, B, E, D;
COMPND  16 SYNONYM: TRANSPOSON TN1000 RESOLVASE;
COMPND  17 ENGINEERED: YES;
COMPND  18 MUTATION: YES;
COMPND  19 OTHER_DETAILS: ACTIVATED GAMMA-DELTA RESOLVASE MUTANT
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 OTHER_DETAILS: SYMMETRIZED RESOLVASE SITES;
SOURCE   4 MOL_ID: 2;
SOURCE   5 SYNTHETIC: YES;
SOURCE   6 OTHER_DETAILS: SYMMETRIZED RESOLVASE SITES;
SOURCE   7 MOL_ID: 3;
SOURCE   8 SYNTHETIC: YES;
SOURCE   9 OTHER_DETAILS: SYMMETRIZED RESOLVASE SITES;
SOURCE  10 MOL_ID: 4;
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE  12 ORGANISM_TAXID: 562;
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  17 EXPRESSION_SYSTEM_PLASMID: PSW26131
KEYWDS    RESOLVASE, SITE-SPECIFIC, RECOMBINATION, FLAT INTERFACE, CROSS-
KEYWDS   2 CRYSTAL AVERAGING, MULTI-CRYSTAL AVERAGING, RECOMBINATION-DNA
KEYWDS   3 COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    W.LI,S.KAMTEKAR,Y.XIONG,G.J.SARKIS,N.D.GRINDLEY,T.A.STEITZ
REVDAT   3   13-JUL-11 1ZR4    1       VERSN
REVDAT   2   24-FEB-09 1ZR4    1       VERSN
REVDAT   1   30-AUG-05 1ZR4    0
JRNL        AUTH   W.LI,S.KAMTEKAR,Y.XIONG,G.J.SARKIS,N.D.GRINDLEY,T.A.STEITZ
JRNL        TITL   STRUCTURE OF A SYNAPTIC GAMMA DELTA RESOLVASE TETRAMER
JRNL        TITL 2 COVALENTLY LINKED TO TWO CLEAVED DNAS.
JRNL        REF    SCIENCE                       V. 309  1210 2005
JRNL        REFN                   ISSN 0036-8075
JRNL        PMID   15994378
JRNL        DOI    10.1126/SCIENCE.1112064
REMARK   2
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
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) : 3.40
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 28441
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) : 0.266
REMARK   3   R VALUE            (WORKING SET) : 0.264
REMARK   3   FREE R VALUE                     : 0.295
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1510
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.40
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.58
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4089
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3640
REMARK   3   BIN FREE R VALUE SET COUNT          : 202
REMARK   3   BIN FREE R VALUE                    : 0.3790
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5672
REMARK   3   NUCLEIC ACID ATOMS       : 2844
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 0
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) : 111.26
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.10000
REMARK   3    B22 (A**2) : -1.99000
REMARK   3    B33 (A**2) : -0.11000
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): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.558
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.497
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 67.900
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.904
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.877
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8896 ; 0.009 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12532 ; 1.453 ; 2.367
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   726 ; 5.150 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   256 ;37.679 ;23.438
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1154 ;20.111 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    64 ;19.786 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1434 ; 0.078 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5552 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3129 ; 0.241 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5657 ; 0.305 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   172 ; 0.145 ; 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):    34 ; 0.308 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.130 ; 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):  3710 ; 2.006 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5748 ; 3.414 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6655 ; 1.850 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6784 ; 2.144 ; 4.500
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 : 4
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A B E D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      3       A      15      1
REMARK   3           1     B      3       B      15      1
REMARK   3           1     E      3       E      15      1
REMARK   3           1     D      3       D      15      1
REMARK   3           2     A     16       A      99      6
REMARK   3           2     B     16       B      99      6
REMARK   3           2     E     16       E      99      6
REMARK   3           2     D     16       D      99      6
REMARK   3           3     A    100       A     126      6
REMARK   3           3     B    100       B     126      6
REMARK   3           3     E    100       E     126      6
REMARK   3           3     D    100       D     126      6
REMARK   3           4     A    144       A     183      6
REMARK   3           4     B    144       B     183      6
REMARK   3           4     E    144       E     183      6
REMARK   3           4     D    144       D     183      6
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   TIGHT POSITIONAL   1    A    (A):    101 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    B    (A):    101 ;  0.02 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    E    (A):    101 ;  0.03 ;  0.05
REMARK   3   TIGHT POSITIONAL   1    D    (A):    101 ;  0.03 ;  0.05
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1177 ;  2.06 ;  5.00
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1177 ;  1.04 ;  5.00
REMARK   3   LOOSE POSITIONAL   1    E    (A):   1177 ;  3.06 ;  5.00
REMARK   3   LOOSE POSITIONAL   1    D    (A):   1177 ;  0.87 ;  5.00
REMARK   3   TIGHT THERMAL      1    A (A**2):    101 ;  0.05 ;  0.50
REMARK   3   TIGHT THERMAL      1    B (A**2):    101 ;  0.05 ;  0.50
REMARK   3   TIGHT THERMAL      1    E (A**2):    101 ;  0.05 ;  0.50
REMARK   3   TIGHT THERMAL      1    D (A**2):    101 ;  0.03 ;  0.50
REMARK   3   LOOSE THERMAL      1    A (A**2):   1177 ;  2.65 ; 10.00
REMARK   3   LOOSE THERMAL      1    B (A**2):   1177 ;  2.75 ; 10.00
REMARK   3   LOOSE THERMAL      1    E (A**2):   1177 ;  2.08 ; 10.00
REMARK   3   LOOSE THERMAL      1    D (A**2):   1177 ;  2.52 ; 10.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : X J U M
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     X      3       X      17      6
REMARK   3           1     J      3       J      17      6
REMARK   3           1     U      3       U      17      6
REMARK   3           1     M      3       M      17      6
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   LOOSE POSITIONAL   2    X    (A):    308 ;  0.49 ;  5.00
REMARK   3   LOOSE POSITIONAL   2    J    (A):    308 ;  0.36 ;  5.00
REMARK   3   LOOSE POSITIONAL   2    U    (A):    308 ;  0.26 ;  5.00
REMARK   3   LOOSE POSITIONAL   2    M    (A):    308 ;  0.52 ;  5.00
REMARK   3   LOOSE THERMAL      2    X (A**2):    308 ;  6.87 ; 10.00
REMARK   3   LOOSE THERMAL      2    J (A**2):    308 ;  2.49 ; 10.00
REMARK   3   LOOSE THERMAL      2    U (A**2):    308 ;  2.89 ; 10.00
REMARK   3   LOOSE THERMAL      2    M (A**2):    308 ;  4.21 ; 10.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 3
REMARK   3     CHAIN NAMES                    : Z I W O
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     Z     20       Z      22      2
REMARK   3           1     I     20       I      22      2
REMARK   3           1     W     20       W      22      2
REMARK   3           1     O     20       O      22      2
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  3    Z    (A):     63 ;  0.18 ;  0.50
REMARK   3   MEDIUM POSITIONAL  3    I    (A):     63 ;  0.15 ;  0.50
REMARK   3   MEDIUM POSITIONAL  3    W    (A):     63 ;  0.24 ;  0.50
REMARK   3   MEDIUM POSITIONAL  3    O    (A):     63 ;  0.20 ;  0.50
REMARK   3   MEDIUM THERMAL     3    Z (A**2):     63 ;  0.28 ;  2.00
REMARK   3   MEDIUM THERMAL     3    I (A**2):     63 ;  0.26 ;  2.00
REMARK   3   MEDIUM THERMAL     3    W (A**2):     63 ;  0.22 ;  2.00
REMARK   3   MEDIUM THERMAL     3    O (A**2):     63 ;  0.27 ;  2.00
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 4
REMARK   3     CHAIN NAMES                    : Y K V N
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     Y     23       Y      33      6
REMARK   3           1     K     23       K      33      6
REMARK   3           1     V     23       V      33      6
REMARK   3           1     N     23       N      33      6
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   LOOSE POSITIONAL   4    Y    (A):    221 ;  0.33 ;  5.00
REMARK   3   LOOSE POSITIONAL   4    K    (A):    221 ;  0.34 ;  5.00
REMARK   3   LOOSE POSITIONAL   4    V    (A):    221 ;  0.27 ;  5.00
REMARK   3   LOOSE POSITIONAL   4    N    (A):    221 ;  0.42 ;  5.00
REMARK   3   LOOSE THERMAL      4    Y (A**2):    221 ;  5.25 ; 10.00
REMARK   3   LOOSE THERMAL      4    K (A**2):    221 ;  1.93 ; 10.00
REMARK   3   LOOSE THERMAL      4    V (A**2):    221 ;  3.62 ; 10.00
REMARK   3   LOOSE THERMAL      4    N (A**2):    221 ;  2.84 ; 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     3        A    99
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5619   4.1004  15.5522
REMARK   3    T TENSOR
REMARK   3      T11:  -0.3512 T22:  -0.3822
REMARK   3      T33:  -0.3577 T12:  -0.0457
REMARK   3      T13:  -0.0207 T23:   0.0360
REMARK   3    L TENSOR
REMARK   3      L11:   1.5593 L22:   4.8684
REMARK   3      L33:   8.7844 L12:  -0.4214
REMARK   3      L13:   2.6179 L23:   2.7585
REMARK   3    S TENSOR
REMARK   3      S11:  -0.4153 S12:  -0.1203 S13:   0.6473
REMARK   3      S21:  -0.1585 S22:   0.0829 S23:   0.0785
REMARK   3      S31:  -1.0293 S32:  -0.3145 S33:   0.3325
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   100        A   143
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3450  21.6172  17.4676
REMARK   3    T TENSOR
REMARK   3      T11:  -0.2653 T22:  -0.2676
REMARK   3      T33:  -0.3433 T12:  -0.0437
REMARK   3      T13:  -0.2636 T23:   0.0043
REMARK   3    L TENSOR
REMARK   3      L11:   2.2579 L22:   7.8754
REMARK   3      L33:  15.1058 L12:  -3.0221
REMARK   3      L13:   2.4773 L23:  -7.3290
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1075 S12:   0.3705 S13:   0.3944
REMARK   3      S21:   0.4794 S22:  -0.8689 S23:  -0.5441
REMARK   3      S31:  -1.7126 S32:   1.2484 S33:   0.9765
REMARK   3
REMARK   3   TLS GROUP : 3
REMARK   3    NUMBER OF COMPONENTS GROUP : 4
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   A   144        A   183
REMARK   3    RESIDUE RANGE :   Z    20        Z    22
REMARK   3    RESIDUE RANGE :   X     2        X    19
REMARK   3    RESIDUE RANGE :   Y    23        Y    35
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9855  31.2223 -14.8901
REMARK   3    T TENSOR
REMARK   3      T11:  -0.6219 T22:  -0.2039
REMARK   3      T33:  -0.4666 T12:   0.3114
REMARK   3      T13:   0.2407 T23:   0.2249
REMARK   3    L TENSOR
REMARK   3      L11:   7.6141 L22:   4.6953
REMARK   3      L33:  15.0770 L12:  -1.1431
REMARK   3      L13:   5.2767 L23:  -3.2355
REMARK   3    S TENSOR
REMARK   3      S11:   0.5795 S12:   1.6107 S13:   0.7525
REMARK   3      S21:  -0.1927 S22:  -1.1748 S23:  -0.0853
REMARK   3      S31:   0.5368 S32:   1.4683 S33:   0.5953
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 :   B     3        B    99
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5994  28.4161  39.2018
REMARK   3    T TENSOR
REMARK   3      T11:  -0.3772 T22:  -0.4646
REMARK   3      T33:  -0.1393 T12:   0.1322
REMARK   3      T13:   0.0660 T23:  -0.0165
REMARK   3    L TENSOR
REMARK   3      L11:  10.3865 L22:   6.1539
REMARK   3      L33:   7.7323 L12:  -0.9743
REMARK   3      L13:  -3.7958 L23:   3.6554
REMARK   3    S TENSOR
REMARK   3      S11:   0.1367 S12:   0.3627 S13:  -0.2466
REMARK   3      S21:   0.5197 S22:  -0.1478 S23:   0.7110
REMARK   3      S31:  -0.1209 S32:  -0.7049 S33:   0.0111
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   100        B   143
REMARK   3    ORIGIN FOR THE GROUP (A):  15.3565   7.9938  44.3795
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1945 T22:  -0.2959
REMARK   3      T33:   0.0177 T12:   0.1431
REMARK   3      T13:   0.2544 T23:  -0.0859
REMARK   3    L TENSOR
REMARK   3      L11:  12.0221 L22:   6.7330
REMARK   3      L33:   6.4245 L12:   2.5903
REMARK   3      L13:  -0.8335 L23:  -0.2808
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0401 S12:  -1.5881 S13:  -1.4274
REMARK   3      S21:   1.0419 S22:  -0.3411 S23:   1.1040
REMARK   3      S31:   0.5088 S32:  -0.5933 S33:   0.3812
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   I    20        I    22
REMARK   3    RESIDUE RANGE :   J     2        J    19
REMARK   3    RESIDUE RANGE :   K    23        K    35
REMARK   3    ORIGIN FOR THE GROUP (A): -17.7358   5.0153  52.7936
REMARK   3    T TENSOR
REMARK   3      T11:   0.6207 T22:   1.9344
REMARK   3      T33:   2.3089 T12:  -0.1510
REMARK   3      T13:   0.6149 T23:  -0.0368
REMARK   3    L TENSOR
REMARK   3      L11:  17.7615 L22:   2.6422
REMARK   3      L33:   4.1610 L12:   2.3647
REMARK   3      L13:  -7.4321 L23:   0.2099
REMARK   3    S TENSOR
REMARK   3      S11:  -1.2756 S12:  -0.7557 S13:   0.2787
REMARK   3      S21:  -0.6851 S22:   0.3635 S23:   2.4314
REMARK   3      S31:   0.0783 S32:  -2.5180 S33:   0.9122
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 :   E     3        E    99
REMARK   3    ORIGIN FOR THE GROUP (A):  52.8863  22.7752  31.9996
REMARK   3    T TENSOR
REMARK   3      T11:  -0.3484 T22:  -0.2604
REMARK   3      T33:  -0.3634 T12:  -0.1105
REMARK   3      T13:  -0.0799 T23:   0.1668
REMARK   3    L TENSOR
REMARK   3      L11:  15.5337 L22:   3.9384
REMARK   3      L33:   5.7340 L12:  -0.4968
REMARK   3      L13:  -4.6720 L23:  -0.6380
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1877 S12:  -0.4914 S13:  -0.2671
REMARK   3      S21:  -0.1582 S22:   0.0903 S23:   0.0796
REMARK   3      S31:   0.0081 S32:   0.6486 S33:   0.0974
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 :   E   100        E   143
REMARK   3    ORIGIN FOR THE GROUP (A):  44.1611   4.3260  25.1124
REMARK   3    T TENSOR
REMARK   3      T11:  -0.3846 T22:  -0.2411
REMARK   3      T33:  -0.1481 T12:   0.0466
REMARK   3      T13:   0.1312 T23:   0.1523
REMARK   3    L TENSOR
REMARK   3      L11:   9.1794 L22:   4.8967
REMARK   3      L33:   4.2262 L12:  -6.2884
REMARK   3      L13:  -1.5941 L23:  -0.4327
REMARK   3    S TENSOR
REMARK   3      S11:   0.7532 S12:   1.2513 S13:  -0.8933
REMARK   3      S21:  -1.1428 S22:  -1.3023 S23:  -0.1905
REMARK   3      S31:   0.4278 S32:  -0.2167 S33:   0.5491
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   W    20        W    22
REMARK   3    RESIDUE RANGE :   U     2        U    19
REMARK   3    RESIDUE RANGE :   V    23        V    35
REMARK   3    ORIGIN FOR THE GROUP (A):  73.9836 -11.3309  19.7378
REMARK   3    T TENSOR
REMARK   3      T11:  -0.1251 T22:  -0.0845
REMARK   3      T33:  -0.0974 T12:   0.3760
REMARK   3      T13:   0.2425 T23:  -0.0286
REMARK   3    L TENSOR
REMARK   3      L11:  17.2041 L22:   9.9514
REMARK   3      L33:   2.0204 L12: -10.3400
REMARK   3      L13:   0.1490 L23:   1.0178
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0196 S12:   1.4607 S13:   0.8272
REMARK   3      S21:   0.1551 S22:  -0.3365 S23:  -1.1618
REMARK   3      S31:   0.1337 S32:   0.1973 S33:   0.3561
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 :   D     3        D    99
REMARK   3    ORIGIN FOR THE GROUP (A):  36.9818  -1.3693  52.4899
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0760 T22:  -0.3200
REMARK   3      T33:  -0.3812 T12:   0.2015
REMARK   3      T13:  -0.0610 T23:  -0.0084
REMARK   3    L TENSOR
REMARK   3      L11:   2.3598 L22:  11.0711
REMARK   3      L33:  12.0247 L12:   2.2048
REMARK   3      L13:  -0.1547 L23:  -2.8790
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1046 S12:  -0.3031 S13:   0.2047
REMARK   3      S21:   1.1086 S22:  -0.0446 S23:  -0.5444
REMARK   3      S31:  -0.2745 S32:   0.5402 S33:   0.1492
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   100        D   143
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2871  19.3491  52.9812
REMARK   3    T TENSOR
REMARK   3      T11:  -0.2229 T22:  -0.4207
REMARK   3      T33:  -0.3707 T12:   0.0812
REMARK   3      T13:  -0.1059 T23:   0.1273
REMARK   3    L TENSOR
REMARK   3      L11:   2.3326 L22:   1.5158
REMARK   3      L33:  12.6980 L12:   1.6622
REMARK   3      L13:   2.1858 L23:   3.4360
REMARK   3    S TENSOR
REMARK   3      S11:  -0.4834 S12:  -0.4406 S13:   0.2197
REMARK   3      S21:   0.0250 S22:   0.2181 S23:  -0.1759
REMARK   3      S31:  -0.9367 S32:   0.4836 S33:   0.2653
REMARK   3
REMARK   3   TLS GROUP : 12
REMARK   3    NUMBER OF COMPONENTS GROUP : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   O    20        O    22
REMARK   3    RESIDUE RANGE :   M     2        M    19
REMARK   3    RESIDUE RANGE :   N    23        N    35
REMARK   3    ORIGIN FOR THE GROUP (A):  41.3419  23.0314  85.2616
REMARK   3    T TENSOR
REMARK   3      T11:  -0.6361 T22:  -0.5725
REMARK   3      T33:  -0.4942 T12:  -0.2919
REMARK   3      T13:   0.1285 T23:  -0.1873
REMARK   3    L TENSOR
REMARK   3      L11:   8.8533 L22:   7.0303
REMARK   3      L33:   9.8154 L12:  -1.7388
REMARK   3      L13:  -0.1728 L23:  -0.9252
REMARK   3    S TENSOR
REMARK   3      S11:   0.2196 S12:  -1.4946 S13:   1.1742
REMARK   3      S21:   0.2273 S22:  -0.1673 S23:  -0.7283
REMARK   3      S31:  -1.8244 S32:   0.2744 S33:  -0.0524
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL
REMARK   4
REMARK   4 1ZR4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUN-05.
REMARK 100 THE RCSB ID CODE IS RCSB033021.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5
REMARK 200  NUMBER OF CRYSTALS USED        : 2
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X25
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.990
REMARK 200  MONOCHROMATOR                  : DOUBLE FLAT SI CRYSTAL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33091
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8
REMARK 200  DATA REDUNDANCY                : 8.000
REMARK 200  R MERGE                    (I) : 0.04700
REMARK 200  R SYM                      (I) : 0.04700
REMARK 200   FOR THE DATA SET  : 25.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.55
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.01000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 68.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NACL, 0.1M MAGNESIUM FORMATE,
REMARK 280  0.1M SODIUM ACETATE, PH 5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 303K
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       59.57900
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.20950
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.64500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.20950
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.57900
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.64500
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: BIOLOGICAL TETRAMER IN ASSYMETRIC UNIT
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Z, Y, J, I, K, U, W, V,
REMARK 350                    AND CHAINS: M, O, N, A, B, E, 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 B     1
REMARK 465     MET D     1
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     LEU D  66    O
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     DT X   1   C1' -  O4' -  C4' ANGL. DEV. =  -9.0 DEGREES
REMARK 500     DT X   1   C3' -  C2' -  C1' ANGL. DEV. = -10.0 DEGREES
REMARK 500     DT X   1   O4' -  C1' -  N1  ANGL. DEV. =   8.3 DEGREES
REMARK 500     DC X   2   C5' -  C4' -  O4' ANGL. DEV. =   8.2 DEGREES
REMARK 500     DC X   2   C1' -  O4' -  C4' ANGL. DEV. =  -7.9 DEGREES
REMARK 500     DC X   2   O4' -  C1' -  N1  ANGL. DEV. =  10.6 DEGREES
REMARK 500     DT X   1   C3' -  O3' -  P   ANGL. DEV. =   9.7 DEGREES
REMARK 500     DC X   9   O4' -  C1' -  N1  ANGL. DEV. =   3.9 DEGREES
REMARK 500     DG X  10   O5' -  C5' -  C4' ANGL. DEV. =  -4.8 DEGREES
REMARK 500     DA X  11   O4' -  C1' -  N9  ANGL. DEV. =   1.8 DEGREES
REMARK 500     DT X  12   O4' -  C1' -  N1  ANGL. DEV. =   3.5 DEGREES
REMARK 500     DA X  14   C3' -  C2' -  C1' ANGL. DEV. =  -7.3 DEGREES
REMARK 500     DA X  18   O4' -  C1' -  N9  ANGL. DEV. =   3.5 DEGREES
REMARK 500     DT Y  23   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES
REMARK 500     DT Y  24   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES
REMARK 500     DT Y  24   C6  -  C5  -  C7  ANGL. DEV. =  -5.9 DEGREES
REMARK 500     DG Y  28   O4' -  C1' -  N9  ANGL. DEV. =   1.8 DEGREES
REMARK 500     DC Y  31   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES
REMARK 500     DA Y  32   C3' -  C2' -  C1' ANGL. DEV. =  -5.1 DEGREES
REMARK 500     DA Y  32   O4' -  C1' -  N9  ANGL. DEV. =   3.8 DEGREES
REMARK 500     DC Y  33   O4' -  C1' -  N1  ANGL. DEV. =   4.8 DEGREES
REMARK 500     DT Y  34   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES
REMARK 500     DG Y  35   O4' -  C1' -  N9  ANGL. DEV. =   2.7 DEGREES
REMARK 500     DG Y  35   C8  -  N9  -  C4  ANGL. DEV. =  -2.7 DEGREES
REMARK 500     DC J   2   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES
REMARK 500     DT J   1   C3' -  O3' -  P   ANGL. DEV. =   9.1 DEGREES
REMARK 500     DA J   3   C3' -  O3' -  P   ANGL. DEV. =   8.4 DEGREES
REMARK 500     DC J   8   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES
REMARK 500     DT J  12   O4' -  C1' -  N1  ANGL. DEV. =   3.2 DEGREES
REMARK 500     DT J  15   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES
REMARK 500     DT J  17   O4' -  C1' -  N1  ANGL. DEV. =   3.6 DEGREES
REMARK 500     DT K  24   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES
REMARK 500     DT K  34   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES
REMARK 500     DT U   1   O4' -  C1' -  N1  ANGL. DEV. =   4.6 DEGREES
REMARK 500     DC U   2   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES
REMARK 500     DT U   5   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES
REMARK 500     DG U   6   O4' -  C1' -  N9  ANGL. DEV. =   2.6 DEGREES
REMARK 500     DC U   8   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES
REMARK 500     DC U   9   O4' -  C1' -  N1  ANGL. DEV. =   3.2 DEGREES
REMARK 500     DA U  11   O4' -  C1' -  N9  ANGL. DEV. =   3.6 DEGREES
REMARK 500     DT U  12   O4' -  C1' -  N1  ANGL. DEV. =   3.6 DEGREES
REMARK 500     DT U  17   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES
REMARK 500     DA U  18   O4' -  C1' -  N9  ANGL. DEV. =   2.5 DEGREES
REMARK 500     DT U  19   O4' -  C1' -  N1  ANGL. DEV. =   3.2 DEGREES
REMARK 500     DA W  21   O4' -  C1' -  N9  ANGL. DEV. =   2.2 DEGREES
REMARK 500     DT V  24   O4' -  C1' -  N1  ANGL. DEV. =   3.6 DEGREES
REMARK 500     DT V  26   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES
REMARK 500     DC V  27   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES
REMARK 500     DG V  28   O4' -  C1' -  N9  ANGL. DEV. =   4.3 DEGREES
REMARK 500     DC V  31   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      79 ANGLE DEVIATIONS.
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    GLN A  14       47.74    -77.67
REMARK 500    SER A  15       39.37    -74.42
REMARK 500    ASN A  31      -39.34    -27.61
REMARK 500    ALA A  38       89.62    -60.19
REMARK 500    SER A  39       14.33    -61.03
REMARK 500    SER A  42      -62.45    -21.49
REMARK 500    SER A  43       73.46   -164.66
REMARK 500    ASP A  44       70.25   -100.00
REMARK 500    GLU A  57      124.62    -33.02
REMARK 500    ASP A  67       20.91    -66.37
REMARK 500    ARG A  68      -60.62   -103.55
REMARK 500    THR A  99       -9.91    -45.62
REMARK 500    ARG A 142      131.31    -32.56
REMARK 500    ASN A 169       79.21   -105.61
REMARK 500    GLN B  14       48.28    -77.55
REMARK 500    SER B  15       34.66    -75.88
REMARK 500    ASN B  31      -35.84    -24.44
REMARK 500    SER B  42      -75.76    -43.12
REMARK 500    SER B  43       51.84   -156.96
REMARK 500    ASP B  67        1.22    -66.26
REMARK 500    ARG B  68      -83.49    -75.74
REMARK 500    LEU B  69      -61.36    -26.28
REMARK 500    LYS B 145      -30.27   -132.79
REMARK 500    SER B 162       33.29    -98.36
REMARK 500    HIS B 163      -36.60   -142.83
REMARK 500    SER E  12      -34.99    -39.43
REMARK 500    GLN E  14       49.03    -77.53
REMARK 500    SER E  15       42.92    -75.67
REMARK 500    ASN E  31      -18.15    -48.71
REMARK 500    ARG E  32       22.63   -147.93
REMARK 500    SER E  42      -66.82     -2.92
REMARK 500    SER E  43      116.05   -178.27
REMARK 500    ARG E  71      -74.10    -78.97
REMARK 500    ALA E  85        5.98    -66.20
REMARK 500    ILE E  93      -74.07    -56.87
REMARK 500    THR E  99       -0.77    -56.95
REMARK 500    GLU E 132       19.15    -68.79
REMARK 500    ALA E 133      -31.04   -145.29
REMARK 500    ASP E 149       31.88    -77.73
REMARK 500    ALA E 150      -11.84   -145.13
REMARK 500    GLN D  14       48.51    -77.88
REMARK 500    SER D  15       37.03    -74.34
REMARK 500    SER D  42      -74.28    -25.57
REMARK 500    SER D  43       80.07   -164.46
REMARK 500    ASP D  44       65.63   -112.90
REMARK 500    ARG D  45       78.06   -105.63
REMARK 500    ASP D  67       26.76    -72.07
REMARK 500    ILE D  93      -75.13    -69.26
REMARK 500    LYS D 136      -98.43    -94.33
REMARK 500    THR D 167      -72.94    -59.35
REMARK 500
REMARK 500 THIS ENTRY HAS      51 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZR2   RELATED DB: PDB
REMARK 900 RELATED ID: 1GDT   RELATED DB: PDB
REMARK 900 RELATED ID: 2RSL   RELATED DB: PDB
REMARK 900 RELATED ID: 1GDR   RELATED DB: PDB
DBREF  1ZR4 A    1   183  UNP    P03012   TNR1_ECOLI       1    183
DBREF  1ZR4 B    1   183  UNP    P03012   TNR1_ECOLI       1    183
DBREF  1ZR4 E    1   183  UNP    P03012   TNR1_ECOLI       1    183
DBREF  1ZR4 D    1   183  UNP    P03012   TNR1_ECOLI       1    183
DBREF  1ZR4 X    1    19  PDB    1ZR4     1ZR4             1     19
DBREF  1ZR4 Z   20    22  PDB    1ZR4     1ZR4            20     22
DBREF  1ZR4 Y   23    35  PDB    1ZR4     1ZR4            23     35
DBREF  1ZR4 J    1    19  PDB    1ZR4     1ZR4             1     19
DBREF  1ZR4 I   20    22  PDB    1ZR4     1ZR4            20     22
DBREF  1ZR4 K   23    35  PDB    1ZR4     1ZR4            23     35
DBREF  1ZR4 U    1    19  PDB    1ZR4     1ZR4             1     19
DBREF  1ZR4 W   20    22  PDB    1ZR4     1ZR4            20     22
DBREF  1ZR4 V   23    35  PDB    1ZR4     1ZR4            23     35
DBREF  1ZR4 M    1    19  PDB    1ZR4     1ZR4             1     19
DBREF  1ZR4 O   20    22  PDB    1ZR4     1ZR4            20     22
DBREF  1ZR4 N   23    35  PDB    1ZR4     1ZR4            23     35
SEQADV 1ZR4 ALA A    2  UNP  P03012    ARG     2 ENGINEERED
SEQADV 1ZR4 LYS A   56  UNP  P03012    GLU    56 ENGINEERED
SEQADV 1ZR4 SER A  101  UNP  P03012    GLY   101 ENGINEERED
SEQADV 1ZR4 TYR A  102  UNP  P03012    GLU   102 ENGINEERED
SEQADV 1ZR4 ILE A  103  UNP  P03012    MET   103 ENGINEERED
SEQADV 1ZR4 GLN A  124  UNP  P03012    GLU   124 ENGINEERED
SEQADV 1ZR4 ALA B    2  UNP  P03012    ARG     2 ENGINEERED
SEQADV 1ZR4 LYS B   56  UNP  P03012    GLU    56 ENGINEERED
SEQADV 1ZR4 SER B  101  UNP  P03012    GLY   101 ENGINEERED
SEQADV 1ZR4 TYR B  102  UNP  P03012    GLU   102 ENGINEERED
SEQADV 1ZR4 ILE B  103  UNP  P03012    MET   103 ENGINEERED
SEQADV 1ZR4 GLN B  124  UNP  P03012    GLU   124 ENGINEERED
SEQADV 1ZR4 ALA E    2  UNP  P03012    ARG     2 ENGINEERED
SEQADV 1ZR4 LYS E   56  UNP  P03012    GLU    56 ENGINEERED
SEQADV 1ZR4 SER E  101  UNP  P03012    GLY   101 ENGINEERED
SEQADV 1ZR4 TYR E  102  UNP  P03012    GLU   102 ENGINEERED
SEQADV 1ZR4 ILE E  103  UNP  P03012    MET   103 ENGINEERED
SEQADV 1ZR4 GLN E  124  UNP  P03012    GLU   124 ENGINEERED
SEQADV 1ZR4 ALA D    2  UNP  P03012    ARG     2 ENGINEERED
SEQADV 1ZR4 LYS D   56  UNP  P03012    GLU    56 ENGINEERED
SEQADV 1ZR4 SER D  101  UNP  P03012    GLY   101 ENGINEERED
SEQADV 1ZR4 TYR D  102  UNP  P03012    GLU   102 ENGINEERED
SEQADV 1ZR4 ILE D  103  UNP  P03012    MET   103 ENGINEERED
SEQADV 1ZR4 GLN D  124  UNP  P03012    GLU   124 ENGINEERED
SEQRES   1 X   19   DT  DC  DA  DG  DT  DG  DT  DC  DC  DG  DA  DT  DA
SEQRES   2 X   19   DA  DT  DT  DT  DA  DT
SEQRES   1 Z    3   DA  DA  DA
SEQRES   1 Y   13   DT  DT  DA  DT  DC  DG  DG  DA  DC  DA  DC  DT  DG
SEQRES   1 J   19   DT  DC  DA  DG  DT  DG  DT  DC  DC  DG  DA  DT  DA
SEQRES   2 J   19   DA  DT  DT  DT  DA  DT
SEQRES   1 I    3   DA  DA  DA
SEQRES   1 K   13   DT  DT  DA  DT  DC  DG  DG  DA  DC  DA  DC  DT  DG
SEQRES   1 U   19   DT  DC  DA  DG  DT  DG  DT  DC  DC  DG  DA  DT  DA
SEQRES   2 U   19   DA  DT  DT  DT  DA  DT
SEQRES   1 W    3   DA  DA  DA
SEQRES   1 V   13   DT  DT  DA  DT  DC  DG  DG  DA  DC  DA  DC  DT  DG
SEQRES   1 M   19   DT  DC  DA  DG  DT  DG  DT  DC  DC  DG  DA  DT  DA
SEQRES   2 M   19   DA  DT  DT  DT  DA  DT
SEQRES   1 O    3   DA  DA  DA
SEQRES   1 N   13   DT  DT  DA  DT  DC  DG  DG  DA  DC  DA  DC  DT  DG
SEQRES   1 A  183  MET ALA LEU PHE GLY TYR ALA ARG VAL SER THR SER GLN
SEQRES   2 A  183  GLN SER LEU ASP ILE GLN VAL ARG ALA LEU LYS ASP ALA
SEQRES   3 A  183  GLY VAL LYS ALA ASN ARG ILE PHE THR ASP LYS ALA SER
SEQRES   4 A  183  GLY SER SER SER ASP ARG LYS GLY LEU ASP LEU LEU ARG
SEQRES   5 A  183  MET LYS VAL LYS GLU GLY ASP VAL ILE LEU VAL LYS LYS
SEQRES   6 A  183  LEU ASP ARG LEU GLY ARG ASP THR ALA ASP MET ILE GLN
SEQRES   7 A  183  LEU ILE LYS GLU PHE ASP ALA GLN GLY VAL SER ILE ARG
SEQRES   8 A  183  PHE ILE ASP ASP GLY ILE SER THR ASP SER TYR ILE GLY
SEQRES   9 A  183  LYS MET VAL VAL THR ILE LEU SER ALA VAL ALA GLN ALA
SEQRES  10 A  183  GLU ARG GLN ARG ILE LEU GLN ARG THR ASN GLU GLY ARG
SEQRES  11 A  183  GLN GLU ALA MET ALA LYS GLY VAL VAL PHE GLY ARG LYS
SEQRES  12 A  183  ARG LYS ILE ASP ARG ASP ALA VAL LEU ASN MET TRP GLN
SEQRES  13 A  183  GLN GLY LEU GLY ALA SER HIS ILE SER LYS THR MET ASN
SEQRES  14 A  183  ILE ALA ARG SER THR VAL TYR LYS VAL ILE ASN GLU SER
SEQRES  15 A  183  ASN
SEQRES   1 B  183  MET ALA LEU PHE GLY TYR ALA ARG VAL SER THR SER GLN
SEQRES   2 B  183  GLN SER LEU ASP ILE GLN VAL ARG ALA LEU LYS ASP ALA
SEQRES   3 B  183  GLY VAL LYS ALA ASN ARG ILE PHE THR ASP LYS ALA SER
SEQRES   4 B  183  GLY SER SER SER ASP ARG LYS GLY LEU ASP LEU LEU ARG
SEQRES   5 B  183  MET LYS VAL LYS GLU GLY ASP VAL ILE LEU VAL LYS LYS
SEQRES   6 B  183  LEU ASP ARG LEU GLY ARG ASP THR ALA ASP MET ILE GLN
SEQRES   7 B  183  LEU ILE LYS GLU PHE ASP ALA GLN GLY VAL SER ILE ARG
SEQRES   8 B  183  PHE ILE ASP ASP GLY ILE SER THR ASP SER TYR ILE GLY
SEQRES   9 B  183  LYS MET VAL VAL THR ILE LEU SER ALA VAL ALA GLN ALA
SEQRES  10 B  183  GLU ARG GLN ARG ILE LEU GLN ARG THR ASN GLU GLY ARG
SEQRES  11 B  183  GLN GLU ALA MET ALA LYS GLY VAL VAL PHE GLY ARG LYS
SEQRES  12 B  183  ARG LYS ILE ASP ARG ASP ALA VAL LEU ASN MET TRP GLN
SEQRES  13 B  183  GLN GLY LEU GLY ALA SER HIS ILE SER LYS THR MET ASN
SEQRES  14 B  183  ILE ALA ARG SER THR VAL TYR LYS VAL ILE ASN GLU SER
SEQRES  15 B  183  ASN
SEQRES   1 E  183  MET ALA LEU PHE GLY TYR ALA ARG VAL SER THR SER GLN
SEQRES   2 E  183  GLN SER LEU ASP ILE GLN VAL ARG ALA LEU LYS ASP ALA
SEQRES   3 E  183  GLY VAL LYS ALA ASN ARG ILE PHE THR ASP LYS ALA SER
SEQRES   4 E  183  GLY SER SER SER ASP ARG LYS GLY LEU ASP LEU LEU ARG
SEQRES   5 E  183  MET LYS VAL LYS GLU GLY ASP VAL ILE LEU VAL LYS LYS
SEQRES   6 E  183  LEU ASP ARG LEU GLY ARG ASP THR ALA ASP MET ILE GLN
SEQRES   7 E  183  LEU ILE LYS GLU PHE ASP ALA GLN GLY VAL SER ILE ARG
SEQRES   8 E  183  PHE ILE ASP ASP GLY ILE SER THR ASP SER TYR ILE GLY
SEQRES   9 E  183  LYS MET VAL VAL THR ILE LEU SER ALA VAL ALA GLN ALA
SEQRES  10 E  183  GLU ARG GLN ARG ILE LEU GLN ARG THR ASN GLU GLY ARG
SEQRES  11 E  183  GLN GLU ALA MET ALA LYS GLY VAL VAL PHE GLY ARG LYS
SEQRES  12 E  183  ARG LYS ILE ASP ARG ASP ALA VAL LEU ASN MET TRP GLN
SEQRES  13 E  183  GLN GLY LEU GLY ALA SER HIS ILE SER LYS THR MET ASN
SEQRES  14 E  183  ILE ALA ARG SER THR VAL TYR LYS VAL ILE ASN GLU SER
SEQRES  15 E  183  ASN
SEQRES   1 D  183  MET ALA LEU PHE GLY TYR ALA ARG VAL SER THR SER GLN
SEQRES   2 D  183  GLN SER LEU ASP ILE GLN VAL ARG ALA LEU LYS ASP ALA
SEQRES   3 D  183  GLY VAL LYS ALA ASN ARG ILE PHE THR ASP LYS ALA SER
SEQRES   4 D  183  GLY SER SER SER ASP ARG LYS GLY LEU ASP LEU LEU ARG
SEQRES   5 D  183  MET LYS VAL LYS GLU GLY ASP VAL ILE LEU VAL LYS LYS
SEQRES   6 D  183  LEU ASP ARG LEU GLY ARG ASP THR ALA ASP MET ILE GLN
SEQRES   7 D  183  LEU ILE LYS GLU PHE ASP ALA GLN GLY VAL SER ILE ARG
SEQRES   8 D  183  PHE ILE ASP ASP GLY ILE SER THR ASP SER TYR ILE GLY
SEQRES   9 D  183  LYS MET VAL VAL THR ILE LEU SER ALA VAL ALA GLN ALA
SEQRES  10 D  183  GLU ARG GLN ARG ILE LEU GLN ARG THR ASN GLU GLY ARG
SEQRES  11 D  183  GLN GLU ALA MET ALA LYS GLY VAL VAL PHE GLY ARG LYS
SEQRES  12 D  183  ARG LYS ILE ASP ARG ASP ALA VAL LEU ASN MET TRP GLN
SEQRES  13 D  183  GLN GLY LEU GLY ALA SER HIS ILE SER LYS THR MET ASN
SEQRES  14 D  183  ILE ALA ARG SER THR VAL TYR LYS VAL ILE ASN GLU SER
SEQRES  15 D  183  ASN
HELIX    1   1 SER A   15  ALA A   26  1                                  12
HELIX    2   2 LYS A   29  ASN A   31  5                                   3
HELIX    3   3 ARG A   45  ARG A   52  1                                   8
HELIX    4   4 LYS A   65  GLY A   70  1                                   6
HELIX    5   5 ASP A   72  GLY A   87  1                                  16
HELIX    6   6 SER A  101  ALA A  135  1                                  35
HELIX    7   7 ARG A  148  GLN A  156  1                                   9
HELIX    8   8 GLY A  160  MET A  168  1                                   9
HELIX    9   9 ALA A  171  SER A  182  1                                  12
HELIX   10  10 SER B   15  ALA B   26  1                                  12
HELIX   11  11 LYS B   29  ASN B   31  5                                   3
HELIX   12  12 ARG B   45  ARG B   52  1                                   8
HELIX   13  13 LYS B   65  GLY B   70  1                                   6
HELIX   14  14 ASP B   72  GLY B   87  1                                  16
HELIX   15  15 SER B  101  ALA B  135  1                                  35
HELIX   16  16 ASP B  147  GLN B  156  1                                  10
HELIX   17  17 HIS B  163  MET B  168  1                                   6
HELIX   18  18 ALA B  171  SER B  182  1                                  12
HELIX   19  19 SER E   15  GLY E   27  1                                  13
HELIX   20  20 LYS E   29  ASN E   31  5                                   3
HELIX   21  21 ARG E   45  ARG E   52  1                                   8
HELIX   22  22 LYS E   65  GLY E   70  1                                   6
HELIX   23  23 ASP E   72  ALA E   85  1                                  14
HELIX   24  24 SER E  101  ARG E  130  1                                  30
HELIX   25  25 ARG E  130  ALA E  135  1                                   6
HELIX   26  26 ASP E  147  VAL E  151  5                                   5
HELIX   27  27 GLY E  160  MET E  168  1                                   9
HELIX   28  28 ALA E  171  SER E  182  1                                  12
HELIX   29  29 SER D   15  ALA D   26  1                                  12
HELIX   30  30 LYS D   29  ASN D   31  5                                   3
HELIX   31  31 ARG D   45  ARG D   52  1                                   8
HELIX   32  32 ASP D   72  ALA D   85  1                                  14
HELIX   33  33 SER D  101  GLU D  132  1                                  32
HELIX   34  34 ASP D  147  ALA D  150  5                                   4
HELIX   35  35 VAL D  151  GLN D  156  1                                   6
HELIX   36  36 GLY D  160  MET D  168  1                                   9
HELIX   37  37 ALA D  171  GLU D  181  1                                  11
SHEET    1   A 5 ILE A  33  LYS A  37  0
SHEET    2   A 5 LEU A   3  VAL A   9  1  N  VAL A   9   O  ASP A  36
SHEET    3   A 5 VAL A  60  VAL A  63  1  O  VAL A  60   N  PHE A   4
SHEET    4   A 5 SER A  89  PHE A  92  1  O  ARG A  91   N  ILE A  61
SHEET    5   A 5 ILE A  97  SER A  98 -1  O  ILE A  97   N  PHE A  92
SHEET    1   B 5 ILE B  33  LYS B  37  0
SHEET    2   B 5 LEU B   3  VAL B   9  1  N  ALA B   7   O  PHE B  34
SHEET    3   B 5 VAL B  60  VAL B  63  1  O  LEU B  62   N  PHE B   4
SHEET    4   B 5 SER B  89  PHE B  92  1  O  SER B  89   N  ILE B  61
SHEET    5   B 5 ILE B  97  SER B  98 -1  O  ILE B  97   N  PHE B  92
SHEET    1   C 5 ILE E  33  LYS E  37  0
SHEET    2   C 5 LEU E   3  VAL E   9  1  N  ALA E   7   O  PHE E  34
SHEET    3   C 5 VAL E  60  VAL E  63  1  O  LEU E  62   N  PHE E   4
SHEET    4   C 5 SER E  89  PHE E  92  1  O  ARG E  91   N  ILE E  61
SHEET    5   C 5 ILE E  97  SER E  98 -1  O  ILE E  97   N  PHE E  92
SHEET    1   D 5 ILE D  33  LYS D  37  0
SHEET    2   D 5 LEU D   3  VAL D   9  1  N  GLY D   5   O  PHE D  34
SHEET    3   D 5 VAL D  60  VAL D  63  1  O  LEU D  62   N  PHE D   4
SHEET    4   D 5 SER D  89  PHE D  92  1  O  ARG D  91   N  ILE D  61
SHEET    5   D 5 ILE D  97  SER D  98 -1  O  ILE D  97   N  PHE D  92
LINK         OG  SER A  10                 P    DA Z  20     1555   1555  1.61
LINK         OG  SER B  10                 P    DA I  20     1555   1555  1.60
LINK         OG  SER E  10                 P    DA W  20     1555   1555  1.59
LINK         OG  SER D  10                 P    DA O  20     1555   1555  1.61
CISPEP   1 GLY D  137    VAL D  138          0       -28.61
CRYST1  119.158  127.290  140.419  90.00  90.00  90.00 P 21 21 21   16
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      0.008392  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007856  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007122        0.00000
      
PROCHECK
Go to PROCHECK summary
 References