HEADER PENICILLIN-BINDING PROTEIN 25-OCT-16 5TR7
TITLE CRYSTAL STRUCTURE OF A PUTATIVE D-ALANYL-D-ALANINE CARBOXYPEPTIDASE
TITLE 2 FROM VIBRIO CHOLERAE O1 BIOVAR ELTOR STR. N16961
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 32-372;
COMPND 5 EC: 3.4.16.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;
SOURCE 3 ORGANISM_TAXID: 243277;
SOURCE 4 STRAIN: O1 BIOVAR ELTOR STR. N16961;
SOURCE 5 GENE: VC0947;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG53
KEYWDS PBP5, PENICIL-BINDING PROTEIN, STRUCTURAL GENOMICS, CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, TRANSFERASE,
KEYWDS 3 PENICILLIN-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.V.FILIPPOVA,G.MINASOV,L.SHUVALOVA,O.KIRYUKHINA,I.DUBROVSKA,
AUTHOR 2 S.SHATSMAN,W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
AUTHOR 3 DISEASES (CSGID)
REVDAT 2 04-OCT-23 5TR7 1 REMARK
REVDAT 1 09-NOV-16 5TR7 0
JRNL AUTH E.V.FILIPPOVA,G.MINASOV,L.SHUVALOVA,O.KIRYUKHINA,
JRNL AUTH 2 I.DUBROVSKA,S.SHATSMAN,W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 4 (CSGID)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE D-ALANYL-D-ALANINE
JRNL TITL 2 CARBOXYPEPTIDASE FROM VIBRIO CHOLERAE O1 BIOVAR ELTOR STR.
JRNL TITL 3 N16961
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 44920
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) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2246
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) : 3271
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3660
REMARK 3 BIN FREE R VALUE SET COUNT : 180
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5772
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 81
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.77000
REMARK 3 B22 (A**2) : 2.77000
REMARK 3 B33 (A**2) : -8.98000
REMARK 3 B12 (A**2) : 1.38000
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): 0.209
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.180
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.198
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.210
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5919 ; 0.018 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5568 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7982 ; 2.028 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12827 ; 0.993 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 750 ; 3.324 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 262 ;33.259 ;25.305
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1017 ;12.942 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;18.573 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 884 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6769 ; 0.027 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1326 ; 0.021 ; 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): 3006 ; 3.844 ; 3.692
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3005 ; 3.841 ; 3.690
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3754 ; 4.927 ; 5.521
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3755 ; 4.927 ; 5.522
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2913 ; 4.789 ; 4.156
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2913 ; 4.784 ; 4.156
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4229 ; 6.440 ; 6.061
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6629 ; 8.086 ;44.163
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6629 ; 8.086 ;44.160
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 34 281 B 34 281 16068 0.08 0.05
REMARK 3 2 A 33 283 C 33 283 16224 0.08 0.05
REMARK 3 3 B 34 281 C 34 281 16066 0.08 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
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 34 A 52
REMARK 3 ORIGIN FOR THE GROUP (A): -37.6964 60.4256 16.2150
REMARK 3 T TENSOR
REMARK 3 T11: 0.1271 T22: 0.1928
REMARK 3 T33: 0.0232 T12: -0.1051
REMARK 3 T13: -0.0327 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 2.2201 L22: 10.5160
REMARK 3 L33: 2.4226 L12: -2.1050
REMARK 3 L13: 0.9188 L23: 1.6973
REMARK 3 S TENSOR
REMARK 3 S11: 0.0437 S12: -0.2856 S13: -0.0940
REMARK 3 S21: 0.6065 S22: 0.1675 S23: -0.2101
REMARK 3 S31: 0.1637 S32: 0.1429 S33: -0.2112
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 53 A 99
REMARK 3 ORIGIN FOR THE GROUP (A): -33.0069 69.4326 -3.5990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1295 T22: 0.2819
REMARK 3 T33: 0.1590 T12: -0.1451
REMARK 3 T13: 0.0512 T23: -0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 0.3621 L22: 1.9092
REMARK 3 L33: 1.9121 L12: -0.2161
REMARK 3 L13: 0.6111 L23: -0.2754
REMARK 3 S TENSOR
REMARK 3 S11: 0.0634 S12: 0.0387 S13: 0.0544
REMARK 3 S21: -0.0584 S22: 0.0039 S23: -0.2124
REMARK 3 S31: -0.2031 S32: 0.5247 S33: -0.0673
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 100 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): -37.1100 65.8926 -17.7199
REMARK 3 T TENSOR
REMARK 3 T11: 0.4090 T22: 0.2604
REMARK 3 T33: 0.2405 T12: -0.0320
REMARK 3 T13: -0.0151 T23: -0.0775
REMARK 3 L TENSOR
REMARK 3 L11: 2.2538 L22: 1.7143
REMARK 3 L33: 3.2093 L12: 0.6742
REMARK 3 L13: -2.6471 L23: -0.7729
REMARK 3 S TENSOR
REMARK 3 S11: 0.0371 S12: 0.1624 S13: -0.1857
REMARK 3 S21: -0.4728 S22: -0.1327 S23: -0.0293
REMARK 3 S31: -0.0860 S32: -0.0736 S33: 0.0956
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 123 A 225
REMARK 3 ORIGIN FOR THE GROUP (A): -35.6945 67.3829 -2.6703
REMARK 3 T TENSOR
REMARK 3 T11: 0.0834 T22: 0.1562
REMARK 3 T33: 0.0631 T12: -0.0539
REMARK 3 T13: 0.0195 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 0.7558 L22: 1.7884
REMARK 3 L33: 3.1629 L12: -0.3955
REMARK 3 L13: 0.0209 L23: 0.2385
REMARK 3 S TENSOR
REMARK 3 S11: 0.1110 S12: -0.0102 S13: -0.0203
REMARK 3 S21: -0.2633 S22: 0.0043 S23: -0.0846
REMARK 3 S31: -0.0632 S32: 0.5632 S33: -0.1153
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 226 A 267
REMARK 3 ORIGIN FOR THE GROUP (A): -41.8519 59.2681 6.5494
REMARK 3 T TENSOR
REMARK 3 T11: 0.0894 T22: 0.0952
REMARK 3 T33: 0.0698 T12: -0.0514
REMARK 3 T13: -0.0180 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 2.8368 L22: 3.4023
REMARK 3 L33: 3.8599 L12: -0.9584
REMARK 3 L13: 0.2627 L23: 0.7310
REMARK 3 S TENSOR
REMARK 3 S11: 0.0282 S12: 0.1047 S13: -0.2669
REMARK 3 S21: 0.3904 S22: -0.0583 S23: -0.0944
REMARK 3 S31: 0.1573 S32: 0.1886 S33: 0.0301
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 268 A 282
REMARK 3 ORIGIN FOR THE GROUP (A): -46.0718 57.9359 15.7676
REMARK 3 T TENSOR
REMARK 3 T11: 0.2229 T22: 0.2008
REMARK 3 T33: 0.2507 T12: -0.0957
REMARK 3 T13: 0.0278 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 3.1630 L22: 7.7005
REMARK 3 L33: 7.7383 L12: 0.5245
REMARK 3 L13: -1.7962 L23: 5.7020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0064 S12: -0.2432 S13: -0.3546
REMARK 3 S21: 0.3551 S22: -0.1836 S23: 0.5643
REMARK 3 S31: 0.2118 S32: 0.2021 S33: 0.1899
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 : B 34 B 40
REMARK 3 ORIGIN FOR THE GROUP (A): -43.1510 52.6383 -38.8140
REMARK 3 T TENSOR
REMARK 3 T11: 0.4755 T22: 0.3338
REMARK 3 T33: 0.1075 T12: -0.0318
REMARK 3 T13: 0.0725 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 2.7246 L22: 11.3019
REMARK 3 L33: 10.2702 L12: 5.2611
REMARK 3 L13: 0.6275 L23: -2.0969
REMARK 3 S TENSOR
REMARK 3 S11: -0.2792 S12: -0.0588 S13: -0.1692
REMARK 3 S21: -0.5636 S22: 0.3185 S23: -0.3504
REMARK 3 S31: -0.3435 S32: -1.0252 S33: -0.0393
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 41 B 191
REMARK 3 ORIGIN FOR THE GROUP (A): -34.6092 36.6905 -19.6736
REMARK 3 T TENSOR
REMARK 3 T11: 0.1919 T22: 0.4306
REMARK 3 T33: 0.3525 T12: 0.0070
REMARK 3 T13: 0.0335 T23: -0.1011
REMARK 3 L TENSOR
REMARK 3 L11: 0.3586 L22: 2.1131
REMARK 3 L33: 4.7114 L12: 0.3800
REMARK 3 L13: -0.8571 L23: 0.6264
REMARK 3 S TENSOR
REMARK 3 S11: -0.0722 S12: -0.0759 S13: -0.0044
REMARK 3 S21: -0.1301 S22: 0.5101 S23: -0.2711
REMARK 3 S31: -0.3805 S32: 0.6524 S33: -0.4379
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 192 B 216
REMARK 3 ORIGIN FOR THE GROUP (A): -47.1212 33.6176 -17.9311
REMARK 3 T TENSOR
REMARK 3 T11: 0.0640 T22: 0.3798
REMARK 3 T33: 0.2261 T12: 0.0537
REMARK 3 T13: 0.0062 T23: 0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 1.2533 L22: 2.3409
REMARK 3 L33: 6.4332 L12: 0.1084
REMARK 3 L13: -2.5649 L23: 1.3486
REMARK 3 S TENSOR
REMARK 3 S11: -0.0438 S12: 0.3437 S13: 0.0699
REMARK 3 S21: 0.0413 S22: 0.1374 S23: 0.1827
REMARK 3 S31: 0.0269 S32: -0.6626 S33: -0.0936
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 217 B 236
REMARK 3 ORIGIN FOR THE GROUP (A): -50.0973 41.6824 -25.8970
REMARK 3 T TENSOR
REMARK 3 T11: 0.2822 T22: 0.6852
REMARK 3 T33: 0.1786 T12: 0.0456
REMARK 3 T13: 0.0011 T23: 0.1098
REMARK 3 L TENSOR
REMARK 3 L11: 2.7003 L22: 2.5325
REMARK 3 L33: 6.2000 L12: -1.5323
REMARK 3 L13: 1.4040 L23: -0.0183
REMARK 3 S TENSOR
REMARK 3 S11: -0.3179 S12: -0.0464 S13: -0.1725
REMARK 3 S21: -0.2894 S22: 0.6504 S23: 0.2798
REMARK 3 S31: -0.9328 S32: -1.0117 S33: -0.3325
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 237 B 258
REMARK 3 ORIGIN FOR THE GROUP (A): -45.0267 41.0255 -32.6488
REMARK 3 T TENSOR
REMARK 3 T11: 0.3336 T22: 0.4905
REMARK 3 T33: 0.1848 T12: -0.0453
REMARK 3 T13: -0.0053 T23: 0.0178
REMARK 3 L TENSOR
REMARK 3 L11: 1.9474 L22: 6.4288
REMARK 3 L33: 6.4712 L12: 3.1044
REMARK 3 L13: 1.6179 L23: 3.7229
REMARK 3 S TENSOR
REMARK 3 S11: -0.3872 S12: -0.1965 S13: -0.1220
REMARK 3 S21: -1.1436 S22: 0.2877 S23: -0.1552
REMARK 3 S31: -1.2758 S32: -0.6749 S33: 0.0995
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 259 B 282
REMARK 3 ORIGIN FOR THE GROUP (A): -48.5637 46.7222 -35.3734
REMARK 3 T TENSOR
REMARK 3 T11: 0.4710 T22: 0.5194
REMARK 3 T33: 0.0775 T12: 0.1761
REMARK 3 T13: -0.0241 T23: 0.1261
REMARK 3 L TENSOR
REMARK 3 L11: 3.0031 L22: 8.6917
REMARK 3 L33: 5.4142 L12: -0.8571
REMARK 3 L13: 0.4456 L23: 4.9107
REMARK 3 S TENSOR
REMARK 3 S11: -0.1471 S12: -0.2359 S13: 0.1728
REMARK 3 S21: -0.2816 S22: 0.1885 S23: 0.3112
REMARK 3 S31: -0.7884 S32: -0.9909 S33: -0.0415
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 33 C 38
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7487 27.6012 -0.2541
REMARK 3 T TENSOR
REMARK 3 T11: 0.3134 T22: 0.1549
REMARK 3 T33: 0.3477 T12: 0.0989
REMARK 3 T13: -0.0275 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 9.6772 L22: 3.7137
REMARK 3 L33: 43.3549 L12: -2.0054
REMARK 3 L13: -20.4580 L23: 4.8009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0988 S12: -0.7103 S13: 0.2341
REMARK 3 S21: 0.6124 S22: 0.5888 S23: 0.1355
REMARK 3 S31: 0.3601 S32: 1.5896 S33: -0.4900
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 39 C 105
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6044 37.3649 -20.2604
REMARK 3 T TENSOR
REMARK 3 T11: 0.0580 T22: 0.1042
REMARK 3 T33: 0.6995 T12: 0.0499
REMARK 3 T13: 0.0282 T23: 0.0652
REMARK 3 L TENSOR
REMARK 3 L11: 0.7057 L22: 1.4752
REMARK 3 L33: 3.7185 L12: -0.1784
REMARK 3 L13: 0.1526 L23: -1.1597
REMARK 3 S TENSOR
REMARK 3 S11: -0.0776 S12: -0.0086 S13: 0.0509
REMARK 3 S21: 0.0219 S22: -0.2006 S23: -0.3817
REMARK 3 S31: 0.3251 S32: 0.4160 S33: 0.2782
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 106 C 223
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3175 39.1195 -24.5132
REMARK 3 T TENSOR
REMARK 3 T11: 0.0959 T22: 0.0907
REMARK 3 T33: 0.7079 T12: 0.0383
REMARK 3 T13: 0.0429 T23: 0.0625
REMARK 3 L TENSOR
REMARK 3 L11: 0.8619 L22: 1.3223
REMARK 3 L33: 3.2538 L12: -0.6133
REMARK 3 L13: 0.2538 L23: -0.3310
REMARK 3 S TENSOR
REMARK 3 S11: -0.1053 S12: 0.0311 S13: 0.2754
REMARK 3 S21: -0.0600 S22: -0.1056 S23: -0.3297
REMARK 3 S31: 0.4127 S32: 0.3431 S33: 0.2109
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 224 C 235
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2712 39.5120 -15.4431
REMARK 3 T TENSOR
REMARK 3 T11: 0.2433 T22: 0.4288
REMARK 3 T33: 0.5093 T12: -0.0475
REMARK 3 T13: 0.0378 T23: -0.1343
REMARK 3 L TENSOR
REMARK 3 L11: 8.8396 L22: 4.3590
REMARK 3 L33: 3.0309 L12: -4.3947
REMARK 3 L13: -1.0528 L23: 2.8697
REMARK 3 S TENSOR
REMARK 3 S11: -0.2843 S12: 0.0401 S13: 0.5041
REMARK 3 S21: -0.2613 S22: -0.3131 S23: 0.1086
REMARK 3 S31: -0.2113 S32: -0.6377 S33: 0.5973
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 236 C 274
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9152 33.7120 -11.2867
REMARK 3 T TENSOR
REMARK 3 T11: 0.0502 T22: 0.1354
REMARK 3 T33: 0.6031 T12: 0.0296
REMARK 3 T13: -0.0128 T23: -0.0915
REMARK 3 L TENSOR
REMARK 3 L11: 0.2354 L22: 2.1004
REMARK 3 L33: 5.3408 L12: 0.5675
REMARK 3 L13: 0.4035 L23: -0.0085
REMARK 3 S TENSOR
REMARK 3 S11: -0.0238 S12: -0.1490 S13: -0.0618
REMARK 3 S21: -0.0145 S22: -0.3195 S23: 0.0353
REMARK 3 S31: 0.2210 S32: -0.4371 S33: 0.3433
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 275 C 283
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4840 39.5184 1.1193
REMARK 3 T TENSOR
REMARK 3 T11: 0.0753 T22: 0.2593
REMARK 3 T33: 0.3357 T12: -0.0200
REMARK 3 T13: 0.0234 T23: -0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 3.8002 L22: 8.2606
REMARK 3 L33: 3.1709 L12: 1.3257
REMARK 3 L13: -1.1539 L23: 4.2389
REMARK 3 S TENSOR
REMARK 3 S11: 0.1574 S12: -0.3186 S13: -0.0367
REMARK 3 S21: 0.2222 S22: -0.3205 S23: 0.2903
REMARK 3 S31: 0.0099 S32: -0.1080 S33: 0.1631
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 5TR7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224687.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : C(111)
REMARK 200 OPTICS : 3.0 UNDULATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47191
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.6000
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) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.75000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: 1NZO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM NITRATE, 0.1 M BIS-TRIS
REMARK 280 PROPANE, 20% PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.47500
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 56.95000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 PRO A 32
REMARK 465 THR A 284
REMARK 465 VAL A 285
REMARK 465 ALA A 286
REMARK 465 PRO A 287
REMARK 465 HIS A 288
REMARK 465 LYS A 289
REMARK 465 ALA A 290
REMARK 465 GLY A 291
REMARK 465 GLU A 292
REMARK 465 THR A 293
REMARK 465 PHE A 294
REMARK 465 VAL A 295
REMARK 465 ASN A 296
REMARK 465 GLU A 297
REMARK 465 THR A 298
REMARK 465 ILE A 299
REMARK 465 TRP A 300
REMARK 465 MET A 301
REMARK 465 GLY A 302
REMARK 465 ASP A 303
REMARK 465 LYS A 304
REMARK 465 ASP A 305
REMARK 465 THR A 306
REMARK 465 ILE A 307
REMARK 465 ALA A 308
REMARK 465 LEU A 309
REMARK 465 GLY A 310
REMARK 465 VAL A 311
REMARK 465 ASP A 312
REMARK 465 LYS A 313
REMARK 465 ASP A 314
REMARK 465 THR A 315
REMARK 465 TYR A 316
REMARK 465 VAL A 317
REMARK 465 THR A 318
REMARK 465 LEU A 319
REMARK 465 PRO A 320
REMARK 465 ARG A 321
REMARK 465 GLY A 322
REMARK 465 GLN A 323
REMARK 465 ALA A 324
REMARK 465 LYS A 325
REMARK 465 ASP A 326
REMARK 465 LEU A 327
REMARK 465 THR A 328
REMARK 465 ALA A 329
REMARK 465 SER A 330
REMARK 465 PHE A 331
REMARK 465 VAL A 332
REMARK 465 LEU A 333
REMARK 465 GLU A 334
REMARK 465 LYS A 335
REMARK 465 GLN A 336
REMARK 465 LEU A 337
REMARK 465 LYS A 338
REMARK 465 ALA A 339
REMARK 465 PRO A 340
REMARK 465 LEU A 341
REMARK 465 LYS A 342
REMARK 465 LYS A 343
REMARK 465 GLY A 344
REMARK 465 ASP A 345
REMARK 465 ILE A 346
REMARK 465 VAL A 347
REMARK 465 GLY A 348
REMARK 465 THR A 349
REMARK 465 LEU A 350
REMARK 465 TYR A 351
REMARK 465 TYR A 352
REMARK 465 GLN A 353
REMARK 465 LEU A 354
REMARK 465 ALA A 355
REMARK 465 GLY A 356
REMARK 465 ASN A 357
REMARK 465 ASP A 358
REMARK 465 ILE A 359
REMARK 465 ALA A 360
REMARK 465 GLN A 361
REMARK 465 TYR A 362
REMARK 465 PRO A 363
REMARK 465 LEU A 364
REMARK 465 LEU A 365
REMARK 465 ALA A 366
REMARK 465 LEU A 367
REMARK 465 GLU A 368
REMARK 465 ASP A 369
REMARK 465 VAL A 370
REMARK 465 GLN A 371
REMARK 465 GLU A 372
REMARK 465 PRO B 32
REMARK 465 ASP B 33
REMARK 465 GLU B 283
REMARK 465 THR B 284
REMARK 465 VAL B 285
REMARK 465 ALA B 286
REMARK 465 PRO B 287
REMARK 465 HIS B 288
REMARK 465 LYS B 289
REMARK 465 ALA B 290
REMARK 465 GLY B 291
REMARK 465 GLU B 292
REMARK 465 THR B 293
REMARK 465 PHE B 294
REMARK 465 VAL B 295
REMARK 465 ASN B 296
REMARK 465 GLU B 297
REMARK 465 THR B 298
REMARK 465 ILE B 299
REMARK 465 TRP B 300
REMARK 465 MET B 301
REMARK 465 GLY B 302
REMARK 465 ASP B 303
REMARK 465 LYS B 304
REMARK 465 ASP B 305
REMARK 465 THR B 306
REMARK 465 ILE B 307
REMARK 465 ALA B 308
REMARK 465 LEU B 309
REMARK 465 GLY B 310
REMARK 465 VAL B 311
REMARK 465 ASP B 312
REMARK 465 LYS B 313
REMARK 465 ASP B 314
REMARK 465 THR B 315
REMARK 465 TYR B 316
REMARK 465 VAL B 317
REMARK 465 THR B 318
REMARK 465 LEU B 319
REMARK 465 PRO B 320
REMARK 465 ARG B 321
REMARK 465 GLY B 322
REMARK 465 GLN B 323
REMARK 465 ALA B 324
REMARK 465 LYS B 325
REMARK 465 ASP B 326
REMARK 465 LEU B 327
REMARK 465 THR B 328
REMARK 465 ALA B 329
REMARK 465 SER B 330
REMARK 465 PHE B 331
REMARK 465 VAL B 332
REMARK 465 LEU B 333
REMARK 465 GLU B 334
REMARK 465 LYS B 335
REMARK 465 GLN B 336
REMARK 465 LEU B 337
REMARK 465 LYS B 338
REMARK 465 ALA B 339
REMARK 465 PRO B 340
REMARK 465 LEU B 341
REMARK 465 LYS B 342
REMARK 465 LYS B 343
REMARK 465 GLY B 344
REMARK 465 ASP B 345
REMARK 465 ILE B 346
REMARK 465 VAL B 347
REMARK 465 GLY B 348
REMARK 465 THR B 349
REMARK 465 LEU B 350
REMARK 465 TYR B 351
REMARK 465 TYR B 352
REMARK 465 GLN B 353
REMARK 465 LEU B 354
REMARK 465 ALA B 355
REMARK 465 GLY B 356
REMARK 465 ASN B 357
REMARK 465 ASP B 358
REMARK 465 ILE B 359
REMARK 465 ALA B 360
REMARK 465 GLN B 361
REMARK 465 TYR B 362
REMARK 465 PRO B 363
REMARK 465 LEU B 364
REMARK 465 LEU B 365
REMARK 465 ALA B 366
REMARK 465 LEU B 367
REMARK 465 GLU B 368
REMARK 465 ASP B 369
REMARK 465 VAL B 370
REMARK 465 GLN B 371
REMARK 465 GLU B 372
REMARK 465 PRO C 32
REMARK 465 THR C 284
REMARK 465 VAL C 285
REMARK 465 ALA C 286
REMARK 465 PRO C 287
REMARK 465 HIS C 288
REMARK 465 LYS C 289
REMARK 465 ALA C 290
REMARK 465 GLY C 291
REMARK 465 GLU C 292
REMARK 465 THR C 293
REMARK 465 PHE C 294
REMARK 465 VAL C 295
REMARK 465 ASN C 296
REMARK 465 GLU C 297
REMARK 465 THR C 298
REMARK 465 ILE C 299
REMARK 465 TRP C 300
REMARK 465 MET C 301
REMARK 465 GLY C 302
REMARK 465 ASP C 303
REMARK 465 LYS C 304
REMARK 465 ASP C 305
REMARK 465 THR C 306
REMARK 465 ILE C 307
REMARK 465 ALA C 308
REMARK 465 LEU C 309
REMARK 465 GLY C 310
REMARK 465 VAL C 311
REMARK 465 ASP C 312
REMARK 465 LYS C 313
REMARK 465 ASP C 314
REMARK 465 THR C 315
REMARK 465 TYR C 316
REMARK 465 VAL C 317
REMARK 465 THR C 318
REMARK 465 LEU C 319
REMARK 465 PRO C 320
REMARK 465 ARG C 321
REMARK 465 GLY C 322
REMARK 465 GLN C 323
REMARK 465 ALA C 324
REMARK 465 LYS C 325
REMARK 465 ASP C 326
REMARK 465 LEU C 327
REMARK 465 THR C 328
REMARK 465 ALA C 329
REMARK 465 SER C 330
REMARK 465 PHE C 331
REMARK 465 VAL C 332
REMARK 465 LEU C 333
REMARK 465 GLU C 334
REMARK 465 LYS C 335
REMARK 465 GLN C 336
REMARK 465 LEU C 337
REMARK 465 LYS C 338
REMARK 465 ALA C 339
REMARK 465 PRO C 340
REMARK 465 LEU C 341
REMARK 465 LYS C 342
REMARK 465 LYS C 343
REMARK 465 GLY C 344
REMARK 465 ASP C 345
REMARK 465 ILE C 346
REMARK 465 VAL C 347
REMARK 465 GLY C 348
REMARK 465 THR C 349
REMARK 465 LEU C 350
REMARK 465 TYR C 351
REMARK 465 TYR C 352
REMARK 465 GLN C 353
REMARK 465 LEU C 354
REMARK 465 ALA C 355
REMARK 465 GLY C 356
REMARK 465 ASN C 357
REMARK 465 ASP C 358
REMARK 465 ILE C 359
REMARK 465 ALA C 360
REMARK 465 GLN C 361
REMARK 465 TYR C 362
REMARK 465 PRO C 363
REMARK 465 LEU C 364
REMARK 465 LEU C 365
REMARK 465 ALA C 366
REMARK 465 LEU C 367
REMARK 465 GLU C 368
REMARK 465 ASP C 369
REMARK 465 VAL C 370
REMARK 465 GLN C 371
REMARK 465 GLU C 372
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 THR B 144 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 198 CD GLU A 198 OE1 0.092
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 MET A 71 CG - SD - CE ANGL. DEV. = -10.1 DEGREES
REMARK 500 ASP A 173 CB - CA - C ANGL. DEV. = -18.7 DEGREES
REMARK 500 ARG A 193 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG A 193 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLU A 198 CG - CD - OE2 ANGL. DEV. = -16.4 DEGREES
REMARK 500 ARG A 217 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 MET C 71 CG - SD - CE ANGL. DEV. = -9.6 DEGREES
REMARK 500 ARG C 82 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 193 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG C 193 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG C 253 NE - CZ - NH1 ANGL. DEV. = -3.1 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 ALA A 65 -131.29 54.15
REMARK 500 ASP A 104 -4.48 76.31
REMARK 500 PHE A 109 52.51 79.19
REMARK 500 ASP A 173 138.60 -38.99
REMARK 500 ASN A 227 75.34 -106.58
REMARK 500 ILE A 231 -72.14 -123.46
REMARK 500 GLU A 249 115.15 -162.09
REMARK 500 ALA B 65 -127.74 51.34
REMARK 500 PHE B 109 44.88 82.16
REMARK 500 ASP B 173 153.08 -49.77
REMARK 500 ASP B 174 138.07 -171.45
REMARK 500 ASN B 227 76.75 -107.90
REMARK 500 ILE B 231 -71.20 -124.96
REMARK 500 GLU B 249 116.74 -162.08
REMARK 500 ALA C 65 -126.68 51.59
REMARK 500 PHE C 109 55.40 72.10
REMARK 500 ASP C 173 151.89 -40.88
REMARK 500 ASP C 174 140.07 -171.99
REMARK 500 ASN C 227 75.44 -106.86
REMARK 500 ILE C 231 -72.25 -126.01
REMARK 500 GLU C 249 115.56 -161.01
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 PEG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO2 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO2 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO2 C 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP01407 RELATED DB: TARGETTRACK
DBREF1 5TR7 A 32 372 UNP A0A0H7A7Y4_VIBCL
DBREF2 5TR7 A A0A0H7A7Y4 32 372
DBREF1 5TR7 B 32 372 UNP A0A0H7A7Y4_VIBCL
DBREF2 5TR7 B A0A0H7A7Y4 32 372
DBREF1 5TR7 C 32 372 UNP A0A0H7A7Y4_VIBCL
DBREF2 5TR7 C A0A0H7A7Y4 32 372
SEQRES 1 A 341 PRO ASP ALA PRO GLN ILE ALA ALA LYS GLY TYR VAL LEU
SEQRES 2 A 341 MET ASP TYR HIS SER GLY LYS VAL LEU ALA GLU LYS GLU
SEQRES 3 A 341 MET ASP THR LYS LEU SER PRO ALA SER LEU THR LYS MET
SEQRES 4 A 341 MET THR SER TYR VAL ILE GLY GLN GLU VAL LYS ARG GLY
SEQRES 5 A 341 ASN ILE SER LEU ASN ASP ASP VAL VAL ILE SER LYS ASN
SEQRES 6 A 341 ALA TRP ALA LYS ASN PHE PRO ASP SER SER LYS MET PHE
SEQRES 7 A 341 VAL GLU VAL GLY THR THR VAL LYS VAL SER ASP LEU ASN
SEQRES 8 A 341 ARG GLY ILE ILE ILE GLN SER GLY ASN ASP ALA CYS VAL
SEQRES 9 A 341 ALA MET ALA GLU HIS VAL ALA GLY THR GLU ASP ALA PHE
SEQRES 10 A 341 VAL ASP LEU MET ASN ALA TRP ALA SER SER LEU GLY MET
SEQRES 11 A 341 LYS ASN SER HIS PHE THR ASN SER HIS GLY LEU ASP ASP
SEQRES 12 A 341 PRO ASN LEU TYR SER THR PRO TYR ASP LEU ALA LEU LEU
SEQRES 13 A 341 GLY GLN ALA LEU ILE ARG ASP VAL PRO GLU GLU TYR ALA
SEQRES 14 A 341 ILE TYR SER GLU GLN LYS PHE THR TYR ASN GLY ILE THR
SEQRES 15 A 341 GLN TYR ASN ARG ASN GLY LEU LEU TRP ASP LYS SER MET
SEQRES 16 A 341 ASN VAL ASP GLY ILE LYS THR GLY HIS THR SER GLY ALA
SEQRES 17 A 341 GLY TYR ASN LEU VAL SER SER ALA THR GLU GLY ASN MET
SEQRES 18 A 341 ARG LEU VAL ALA VAL VAL MET GLY THR ASP ASN GLU ASN
SEQRES 19 A 341 ALA ARG LYS ALA GLU SER LYS LYS LEU LEU SER TYR GLY
SEQRES 20 A 341 PHE ARG PHE PHE GLU THR VAL ALA PRO HIS LYS ALA GLY
SEQRES 21 A 341 GLU THR PHE VAL ASN GLU THR ILE TRP MET GLY ASP LYS
SEQRES 22 A 341 ASP THR ILE ALA LEU GLY VAL ASP LYS ASP THR TYR VAL
SEQRES 23 A 341 THR LEU PRO ARG GLY GLN ALA LYS ASP LEU THR ALA SER
SEQRES 24 A 341 PHE VAL LEU GLU LYS GLN LEU LYS ALA PRO LEU LYS LYS
SEQRES 25 A 341 GLY ASP ILE VAL GLY THR LEU TYR TYR GLN LEU ALA GLY
SEQRES 26 A 341 ASN ASP ILE ALA GLN TYR PRO LEU LEU ALA LEU GLU ASP
SEQRES 27 A 341 VAL GLN GLU
SEQRES 1 B 341 PRO ASP ALA PRO GLN ILE ALA ALA LYS GLY TYR VAL LEU
SEQRES 2 B 341 MET ASP TYR HIS SER GLY LYS VAL LEU ALA GLU LYS GLU
SEQRES 3 B 341 MET ASP THR LYS LEU SER PRO ALA SER LEU THR LYS MET
SEQRES 4 B 341 MET THR SER TYR VAL ILE GLY GLN GLU VAL LYS ARG GLY
SEQRES 5 B 341 ASN ILE SER LEU ASN ASP ASP VAL VAL ILE SER LYS ASN
SEQRES 6 B 341 ALA TRP ALA LYS ASN PHE PRO ASP SER SER LYS MET PHE
SEQRES 7 B 341 VAL GLU VAL GLY THR THR VAL LYS VAL SER ASP LEU ASN
SEQRES 8 B 341 ARG GLY ILE ILE ILE GLN SER GLY ASN ASP ALA CYS VAL
SEQRES 9 B 341 ALA MET ALA GLU HIS VAL ALA GLY THR GLU ASP ALA PHE
SEQRES 10 B 341 VAL ASP LEU MET ASN ALA TRP ALA SER SER LEU GLY MET
SEQRES 11 B 341 LYS ASN SER HIS PHE THR ASN SER HIS GLY LEU ASP ASP
SEQRES 12 B 341 PRO ASN LEU TYR SER THR PRO TYR ASP LEU ALA LEU LEU
SEQRES 13 B 341 GLY GLN ALA LEU ILE ARG ASP VAL PRO GLU GLU TYR ALA
SEQRES 14 B 341 ILE TYR SER GLU GLN LYS PHE THR TYR ASN GLY ILE THR
SEQRES 15 B 341 GLN TYR ASN ARG ASN GLY LEU LEU TRP ASP LYS SER MET
SEQRES 16 B 341 ASN VAL ASP GLY ILE LYS THR GLY HIS THR SER GLY ALA
SEQRES 17 B 341 GLY TYR ASN LEU VAL SER SER ALA THR GLU GLY ASN MET
SEQRES 18 B 341 ARG LEU VAL ALA VAL VAL MET GLY THR ASP ASN GLU ASN
SEQRES 19 B 341 ALA ARG LYS ALA GLU SER LYS LYS LEU LEU SER TYR GLY
SEQRES 20 B 341 PHE ARG PHE PHE GLU THR VAL ALA PRO HIS LYS ALA GLY
SEQRES 21 B 341 GLU THR PHE VAL ASN GLU THR ILE TRP MET GLY ASP LYS
SEQRES 22 B 341 ASP THR ILE ALA LEU GLY VAL ASP LYS ASP THR TYR VAL
SEQRES 23 B 341 THR LEU PRO ARG GLY GLN ALA LYS ASP LEU THR ALA SER
SEQRES 24 B 341 PHE VAL LEU GLU LYS GLN LEU LYS ALA PRO LEU LYS LYS
SEQRES 25 B 341 GLY ASP ILE VAL GLY THR LEU TYR TYR GLN LEU ALA GLY
SEQRES 26 B 341 ASN ASP ILE ALA GLN TYR PRO LEU LEU ALA LEU GLU ASP
SEQRES 27 B 341 VAL GLN GLU
SEQRES 1 C 341 PRO ASP ALA PRO GLN ILE ALA ALA LYS GLY TYR VAL LEU
SEQRES 2 C 341 MET ASP TYR HIS SER GLY LYS VAL LEU ALA GLU LYS GLU
SEQRES 3 C 341 MET ASP THR LYS LEU SER PRO ALA SER LEU THR LYS MET
SEQRES 4 C 341 MET THR SER TYR VAL ILE GLY GLN GLU VAL LYS ARG GLY
SEQRES 5 C 341 ASN ILE SER LEU ASN ASP ASP VAL VAL ILE SER LYS ASN
SEQRES 6 C 341 ALA TRP ALA LYS ASN PHE PRO ASP SER SER LYS MET PHE
SEQRES 7 C 341 VAL GLU VAL GLY THR THR VAL LYS VAL SER ASP LEU ASN
SEQRES 8 C 341 ARG GLY ILE ILE ILE GLN SER GLY ASN ASP ALA CYS VAL
SEQRES 9 C 341 ALA MET ALA GLU HIS VAL ALA GLY THR GLU ASP ALA PHE
SEQRES 10 C 341 VAL ASP LEU MET ASN ALA TRP ALA SER SER LEU GLY MET
SEQRES 11 C 341 LYS ASN SER HIS PHE THR ASN SER HIS GLY LEU ASP ASP
SEQRES 12 C 341 PRO ASN LEU TYR SER THR PRO TYR ASP LEU ALA LEU LEU
SEQRES 13 C 341 GLY GLN ALA LEU ILE ARG ASP VAL PRO GLU GLU TYR ALA
SEQRES 14 C 341 ILE TYR SER GLU GLN LYS PHE THR TYR ASN GLY ILE THR
SEQRES 15 C 341 GLN TYR ASN ARG ASN GLY LEU LEU TRP ASP LYS SER MET
SEQRES 16 C 341 ASN VAL ASP GLY ILE LYS THR GLY HIS THR SER GLY ALA
SEQRES 17 C 341 GLY TYR ASN LEU VAL SER SER ALA THR GLU GLY ASN MET
SEQRES 18 C 341 ARG LEU VAL ALA VAL VAL MET GLY THR ASP ASN GLU ASN
SEQRES 19 C 341 ALA ARG LYS ALA GLU SER LYS LYS LEU LEU SER TYR GLY
SEQRES 20 C 341 PHE ARG PHE PHE GLU THR VAL ALA PRO HIS LYS ALA GLY
SEQRES 21 C 341 GLU THR PHE VAL ASN GLU THR ILE TRP MET GLY ASP LYS
SEQRES 22 C 341 ASP THR ILE ALA LEU GLY VAL ASP LYS ASP THR TYR VAL
SEQRES 23 C 341 THR LEU PRO ARG GLY GLN ALA LYS ASP LEU THR ALA SER
SEQRES 24 C 341 PHE VAL LEU GLU LYS GLN LEU LYS ALA PRO LEU LYS LYS
SEQRES 25 C 341 GLY ASP ILE VAL GLY THR LEU TYR TYR GLN LEU ALA GLY
SEQRES 26 C 341 ASN ASP ILE ALA GLN TYR PRO LEU LEU ALA LEU GLU ASP
SEQRES 27 C 341 VAL GLN GLU
HET PEG A 401 7
HET NO2 A 402 3
HET NO2 A 403 3
HET PEG B 401 7
HET PEG B 402 7
HET GOL B 403 6
HET PEG C 401 7
HET NO2 C 402 3
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM NO2 NITRITE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 PEG 4(C4 H10 O3)
FORMUL 5 NO2 3(N O2 1-)
FORMUL 9 GOL C3 H8 O3
FORMUL 12 HOH *81(H2 O)
HELIX 1 AA1 PRO A 64 SER A 66 5 3
HELIX 2 AA2 LEU A 67 ARG A 82 1 16
HELIX 3 AA3 SER A 94 PHE A 102 5 9
HELIX 4 AA4 VAL A 118 ILE A 127 1 10
HELIX 5 AA5 GLY A 130 GLY A 143 1 14
HELIX 6 AA6 THR A 144 LEU A 159 1 16
HELIX 7 AA7 THR A 180 VAL A 195 1 16
HELIX 8 AA8 VAL A 195 ALA A 200 1 6
HELIX 9 AA9 ILE A 201 GLU A 204 5 4
HELIX 10 AB1 ASN A 218 ASP A 223 5 6
HELIX 11 AB2 ASN A 263 GLU A 283 1 21
HELIX 12 AB3 PRO B 64 SER B 66 5 3
HELIX 13 AB4 LEU B 67 ARG B 82 1 16
HELIX 14 AB5 TRP B 98 PHE B 102 5 5
HELIX 15 AB6 VAL B 118 ILE B 127 1 10
HELIX 16 AB7 GLY B 130 GLY B 143 1 14
HELIX 17 AB8 THR B 144 LEU B 159 1 16
HELIX 18 AB9 THR B 180 VAL B 195 1 16
HELIX 19 AC1 VAL B 195 ALA B 200 1 6
HELIX 20 AC2 ILE B 201 GLU B 204 5 4
HELIX 21 AC3 ASN B 218 ASP B 223 5 6
HELIX 22 AC4 ASN B 263 PHE B 282 1 20
HELIX 23 AC5 PRO C 64 SER C 66 5 3
HELIX 24 AC6 LEU C 67 ARG C 82 1 16
HELIX 25 AC7 TRP C 98 PHE C 102 5 5
HELIX 26 AC8 VAL C 118 ILE C 127 1 10
HELIX 27 AC9 GLY C 130 GLY C 143 1 14
HELIX 28 AD1 THR C 144 LEU C 159 1 16
HELIX 29 AD2 THR C 180 VAL C 195 1 16
HELIX 30 AD3 VAL C 195 ALA C 200 1 6
HELIX 31 AD4 ILE C 201 GLU C 204 5 4
HELIX 32 AD5 ASN C 218 ASP C 223 5 6
HELIX 33 AD6 ASN C 263 PHE C 282 1 20
SHEET 1 AA1 5 VAL A 52 LYS A 56 0
SHEET 2 AA1 5 GLY A 41 ASP A 46 -1 N TYR A 42 O LYS A 56
SHEET 3 AA1 5 MET A 252 THR A 261 -1 O VAL A 255 N MET A 45
SHEET 4 AA1 5 GLY A 240 GLU A 249 -1 N SER A 245 O ALA A 256
SHEET 5 AA1 5 ASN A 227 THR A 236 -1 N GLY A 234 O ASN A 242
SHEET 1 AA2 2 ASP A 90 VAL A 92 0
SHEET 2 AA2 2 THR A 115 LYS A 117 -1 O VAL A 116 N VAL A 91
SHEET 1 AA3 2 LYS A 206 TYR A 209 0
SHEET 2 AA3 2 ILE A 212 TYR A 215 -1 O GLN A 214 N PHE A 207
SHEET 1 AA4 5 VAL B 52 LYS B 56 0
SHEET 2 AA4 5 GLY B 41 ASP B 46 -1 N LEU B 44 O LEU B 53
SHEET 3 AA4 5 MET B 252 THR B 261 -1 O VAL B 255 N MET B 45
SHEET 4 AA4 5 GLY B 240 GLU B 249 -1 N SER B 245 O ALA B 256
SHEET 5 AA4 5 ASN B 227 THR B 236 -1 N GLY B 234 O ASN B 242
SHEET 1 AA5 2 ASP B 90 VAL B 92 0
SHEET 2 AA5 2 THR B 115 LYS B 117 -1 O VAL B 116 N VAL B 91
SHEET 1 AA6 2 LYS B 206 TYR B 209 0
SHEET 2 AA6 2 ILE B 212 TYR B 215 -1 O GLN B 214 N PHE B 207
SHEET 1 AA7 5 VAL C 52 LYS C 56 0
SHEET 2 AA7 5 GLY C 41 ASP C 46 -1 N LEU C 44 O LEU C 53
SHEET 3 AA7 5 MET C 252 THR C 261 -1 O VAL C 255 N MET C 45
SHEET 4 AA7 5 GLY C 240 GLU C 249 -1 N SER C 245 O ALA C 256
SHEET 5 AA7 5 ASN C 227 THR C 236 -1 N GLY C 234 O ASN C 242
SHEET 1 AA8 2 ASP C 90 VAL C 91 0
SHEET 2 AA8 2 VAL C 116 LYS C 117 -1 O VAL C 116 N VAL C 91
SHEET 1 AA9 2 LYS C 206 TYR C 209 0
SHEET 2 AA9 2 ILE C 212 TYR C 215 -1 O ILE C 212 N TYR C 209
CISPEP 1 GLY A 230 ILE A 231 0 1.65
CISPEP 2 GLY B 230 ILE B 231 0 0.89
CISPEP 3 GLY C 230 ILE C 231 0 1.67
SITE 1 AC1 2 TRP A 222 LYS A 268
SITE 1 AC2 3 ASN A 251 MET A 252 HOH A 507
SITE 1 AC3 5 ARG A 217 GLY A 219 GLU A 264 ARG A 267
SITE 2 AC3 5 LYS A 268
SITE 1 AC4 2 TRP B 155 SER B 158
SITE 1 AC5 3 HIS B 165 GLY C 219 NO2 C 402
SITE 1 AC6 2 SER C 158 GLY C 211
SITE 1 AC7 1 GOL B 403
CRYST1 88.749 88.749 85.425 90.00 90.00 120.00 P 31 9
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 0.011268 0.006505 0.000000 0.00000
SCALE2 0.000000 0.013011 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011706 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
