HEADER MEMBRANE PROTEIN, HORMONE 28-MAY-10 3N96
TITLE CRYSTAL STRUCTURE OF HUMAN CRFR2 ALPHA EXTRACELLULAR DOMAIN IN COMPLEX
TITLE 2 WITH UROCORTIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALTOSE BINDING PROTEIN-CRFR2 ALPHA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: UROCORTIN;
COMPND 8 CHAIN: E, F, G, H;
COMPND 9 FRAGMENT: UNP RESIDUES 107-122;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CRFR2 ALPHA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-DUET1;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS CLASS B-GPCR, EXTRACELLULAR DOMAIN, CRFR2 ALPHA EXTRACELLULAR DOMAIN,
KEYWDS 2 NEUROPEPTIDE, SELECTIVITY, MEMBRANE PROTEIN, HORMONE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.PAL,K.SWAMINATHAN,A.A.PIOSZAK,H.E.XU
REVDAT 3 06-SEP-23 3N96 1 HETSYN
REVDAT 2 29-JUL-20 3N96 1 COMPND REMARK SEQADV HET
REVDAT 2 2 1 HETNAM FORMUL LINK SITE
REVDAT 2 3 1 ATOM
REVDAT 1 20-OCT-10 3N96 0
JRNL AUTH K.PAL,K.SWAMINATHAN,A.A.PIOSZAK,H.E.XU
JRNL TITL STRUCTURAL BASIS OF LIGAND SELECTIVITY IN HUMAN CRFR1 AND
JRNL TITL 2 CRFR2 ALPHA EXTRACELLULAR DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 58007
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) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2922
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) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4161
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.09
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 213
REMARK 3 BIN FREE R VALUE : 0.3530
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15054
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.52000
REMARK 3 B22 (A**2) : 0.38000
REMARK 3 B33 (A**2) : -0.80000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -3.90000
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): 0.408
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.317
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.316
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15530 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21122 ; 1.618 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1925 ; 6.385 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 697 ;33.456 ;25.581
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2528 ;17.725 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;21.595 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2306 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11846 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9641 ; 0.209 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15441 ; 0.323 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5885 ; 0.516 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5681 ; 0.793 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 11
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A -369 A -6 1
REMARK 3 1 B -369 B -6 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2826 ; 0.040 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 2826 ; 0.110 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B -369 B -6 1
REMARK 3 1 C -369 C -6 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 2826 ; 0.080 ; 0.050
REMARK 3 TIGHT THERMAL 2 B (A**2): 2826 ; 0.120 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C -369 C -6 1
REMARK 3 1 D -369 D -6 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 C (A): 2826 ; 0.040 ; 0.050
REMARK 3 TIGHT THERMAL 3 C (A**2): 2826 ; 0.080 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 4 A 101 2
REMARK 3 1 B 4 B 101 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 392 ; 0.050 ; 0.050
REMARK 3 MEDIUM POSITIONAL 4 A (A): 369 ; 0.060 ; 0.500
REMARK 3 TIGHT THERMAL 4 A (A**2): 392 ; 0.080 ; 0.500
REMARK 3 MEDIUM THERMAL 4 A (A**2): 369 ; 0.100 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 4 B 30 2
REMARK 3 1 C 4 C 30 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 B (A): 108 ; 0.100 ; 0.050
REMARK 3 MEDIUM POSITIONAL 5 B (A): 91 ; 0.140 ; 0.500
REMARK 3 TIGHT THERMAL 5 B (A**2): 108 ; 0.130 ; 0.500
REMARK 3 MEDIUM THERMAL 5 B (A**2): 91 ; 0.150 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 4 C 30 2
REMARK 3 1 D 4 D 30 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 C (A): 108 ; 0.050 ; 0.050
REMARK 3 MEDIUM POSITIONAL 6 C (A): 91 ; 0.080 ; 0.500
REMARK 3 TIGHT THERMAL 6 C (A**2): 108 ; 0.090 ; 0.500
REMARK 3 MEDIUM THERMAL 6 C (A**2): 91 ; 0.130 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 36 B 101 2
REMARK 3 1 C 36 C 101 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 7 B (A): 264 ; 0.080 ; 0.050
REMARK 3 MEDIUM POSITIONAL 7 B (A): 262 ; 0.120 ; 0.500
REMARK 3 TIGHT THERMAL 7 B (A**2): 264 ; 0.100 ; 0.500
REMARK 3 MEDIUM THERMAL 7 B (A**2): 262 ; 0.130 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 36 C 101 2
REMARK 3 1 D 36 D 101 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 8 C (A): 264 ; 0.040 ; 0.050
REMARK 3 MEDIUM POSITIONAL 8 C (A): 262 ; 0.060 ; 0.500
REMARK 3 TIGHT THERMAL 8 C (A**2): 264 ; 0.100 ; 0.500
REMARK 3 MEDIUM THERMAL 8 C (A**2): 262 ; 0.130 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 E 31 E 41 2
REMARK 3 1 F 31 F 41 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 9 E (A): 44 ; 0.030 ; 0.050
REMARK 3 MEDIUM POSITIONAL 9 E (A): 46 ; 0.040 ; 0.500
REMARK 3 TIGHT THERMAL 9 E (A**2): 44 ; 0.060 ; 0.500
REMARK 3 MEDIUM THERMAL 9 E (A**2): 46 ; 0.060 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : F G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 F 31 F 41 2
REMARK 3 1 G 31 G 41 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 10 F (A): 44 ; 0.040 ; 0.050
REMARK 3 MEDIUM POSITIONAL 10 F (A): 46 ; 0.070 ; 0.500
REMARK 3 TIGHT THERMAL 10 F (A**2): 44 ; 0.070 ; 0.500
REMARK 3 MEDIUM THERMAL 10 F (A**2): 46 ; 0.080 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 G 33 G 41 2
REMARK 3 1 H 33 H 41 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 11 G (A): 36 ; 0.030 ; 0.050
REMARK 3 MEDIUM POSITIONAL 11 G (A): 40 ; 0.040 ; 0.500
REMARK 3 TIGHT THERMAL 11 G (A**2): 36 ; 0.030 ; 0.500
REMARK 3 MEDIUM THERMAL 11 G (A**2): 40 ; 0.030 ; 2.000
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 -369 A 2
REMARK 3 ORIGIN FOR THE GROUP (A): 2.9982 32.0987 31.0533
REMARK 3 T TENSOR
REMARK 3 T11: 0.0142 T22: 0.0129
REMARK 3 T33: 0.0319 T12: -0.0077
REMARK 3 T13: 0.0079 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.0239 L22: 1.6020
REMARK 3 L33: 3.0100 L12: -0.0677
REMARK 3 L13: -0.5327 L23: 1.0133
REMARK 3 S TENSOR
REMARK 3 S11: 0.1199 S12: -0.0695 S13: 0.0582
REMARK 3 S21: -0.0167 S22: -0.0601 S23: -0.1138
REMARK 3 S31: -0.0862 S32: -0.0501 S33: -0.0598
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 : B -369 B 2
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9389 71.7397 73.4496
REMARK 3 T TENSOR
REMARK 3 T11: 0.0306 T22: 0.0084
REMARK 3 T33: 0.0363 T12: -0.0029
REMARK 3 T13: 0.0149 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.0795 L22: 1.7271
REMARK 3 L33: 2.8896 L12: 0.0962
REMARK 3 L13: 0.5316 L23: 1.0234
REMARK 3 S TENSOR
REMARK 3 S11: 0.1275 S12: 0.0495 S13: -0.0458
REMARK 3 S21: 0.0478 S22: -0.0323 S23: -0.0604
REMARK 3 S31: 0.0916 S32: -0.0310 S33: -0.0953
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 : C -369 C 2
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7994 75.8335 15.2090
REMARK 3 T TENSOR
REMARK 3 T11: 0.1990 T22: 0.1279
REMARK 3 T33: 0.1231 T12: 0.0008
REMARK 3 T13: 0.0514 T23: 0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 1.4442 L22: 2.4742
REMARK 3 L33: 2.5869 L12: 0.5265
REMARK 3 L13: -0.3972 L23: 0.5052
REMARK 3 S TENSOR
REMARK 3 S11: 0.0353 S12: -0.2831 S13: -0.2177
REMARK 3 S21: 0.4215 S22: -0.0370 S23: 0.1549
REMARK 3 S31: 0.5036 S32: -0.0578 S33: 0.0018
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 : D -369 D 2
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4612 28.0382 89.2535
REMARK 3 T TENSOR
REMARK 3 T11: 0.2032 T22: 0.1273
REMARK 3 T33: 0.1068 T12: -0.0068
REMARK 3 T13: 0.0098 T23: 0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 1.4398 L22: 2.3732
REMARK 3 L33: 2.7646 L12: -0.4479
REMARK 3 L13: 0.3824 L23: 0.6339
REMARK 3 S TENSOR
REMARK 3 S11: 0.0139 S12: 0.2690 S13: 0.2073
REMARK 3 S21: -0.5059 S22: -0.0199 S23: 0.1453
REMARK 3 S31: -0.5122 S32: -0.0571 S33: 0.0060
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 3 A 103
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4642 8.1267 54.7621
REMARK 3 T TENSOR
REMARK 3 T11: 0.0848 T22: 0.2583
REMARK 3 T33: 0.1048 T12: -0.0399
REMARK 3 T13: -0.0063 T23: -0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 5.8645 L22: 3.7047
REMARK 3 L33: 0.6814 L12: 2.1063
REMARK 3 L13: -1.0690 L23: -1.0868
REMARK 3 S TENSOR
REMARK 3 S11: 0.0179 S12: -0.1435 S13: 0.1121
REMARK 3 S21: 0.0560 S22: -0.0203 S23: -0.1164
REMARK 3 S31: -0.1158 S32: 0.2808 S33: 0.0024
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 101
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7676 95.6865 49.1547
REMARK 3 T TENSOR
REMARK 3 T11: 0.0912 T22: 0.2024
REMARK 3 T33: 0.1483 T12: -0.0204
REMARK 3 T13: 0.0860 T23: -0.0309
REMARK 3 L TENSOR
REMARK 3 L11: 5.0704 L22: 3.0040
REMARK 3 L33: 1.5193 L12: -2.1757
REMARK 3 L13: 0.9149 L23: 0.0937
REMARK 3 S TENSOR
REMARK 3 S11: 0.0647 S12: 0.2311 S13: -0.1989
REMARK 3 S21: 0.0279 S22: 0.0040 S23: -0.1470
REMARK 3 S31: 0.1251 S32: 0.2260 S33: -0.0687
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3 C 102
REMARK 3 ORIGIN FOR THE GROUP (A): -40.4336 95.1794 50.7971
REMARK 3 T TENSOR
REMARK 3 T11: 0.0729 T22: 0.1188
REMARK 3 T33: 0.1380 T12: 0.0273
REMARK 3 T13: -0.0147 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 4.6251 L22: 2.6287
REMARK 3 L33: 3.4046 L12: 0.8893
REMARK 3 L13: -0.7638 L23: -2.9622
REMARK 3 S TENSOR
REMARK 3 S11: -0.0467 S12: 0.0005 S13: 0.0926
REMARK 3 S21: 0.0646 S22: 0.1185 S23: 0.1313
REMARK 3 S31: -0.1157 S32: -0.1324 S33: -0.0718
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 : D 3 D 103
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4339 8.6407 54.0161
REMARK 3 T TENSOR
REMARK 3 T11: 0.0586 T22: 0.1262
REMARK 3 T33: 0.0900 T12: -0.0420
REMARK 3 T13: 0.0456 T23: -0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 4.5625 L22: 3.2163
REMARK 3 L33: 2.3416 L12: -0.5647
REMARK 3 L13: 0.8091 L23: -2.3995
REMARK 3 S TENSOR
REMARK 3 S11: -0.0650 S12: -0.0166 S13: -0.1260
REMARK 3 S21: 0.0170 S22: 0.0839 S23: 0.0620
REMARK 3 S31: 0.1327 S32: -0.1530 S33: -0.0189
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 : G 28 G 41
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7289 16.5271 36.4345
REMARK 3 T TENSOR
REMARK 3 T11: 0.8452 T22: 1.1005
REMARK 3 T33: 0.8619 T12: 0.0419
REMARK 3 T13: 0.1326 T23: 0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 1.1389 L22: 1.2469
REMARK 3 L33: 11.7828 L12: -1.1874
REMARK 3 L13: 3.6091 L23: -3.7994
REMARK 3 S TENSOR
REMARK 3 S11: 0.4284 S12: 0.0280 S13: -0.1210
REMARK 3 S21: -0.2656 S22: 0.1082 S23: 0.2095
REMARK 3 S31: 0.6854 S32: 0.5336 S33: -0.5367
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 : H 32 H 41
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1104 86.1159 65.0128
REMARK 3 T TENSOR
REMARK 3 T11: 1.0975 T22: 0.8888
REMARK 3 T33: 0.8042 T12: -0.0907
REMARK 3 T13: -0.2694 T23: -0.0367
REMARK 3 L TENSOR
REMARK 3 L11: 5.0010 L22: 1.2900
REMARK 3 L33: 45.5139 L12: 2.5389
REMARK 3 L13: -15.0763 L23: -7.6589
REMARK 3 S TENSOR
REMARK 3 S11: 0.5736 S12: -0.4253 S13: 0.1050
REMARK 3 S21: 0.2551 S22: -0.1364 S23: 0.0799
REMARK 3 S31: -1.3233 S32: 1.3434 S33: -0.4371
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 : E 26 E 41
REMARK 3 ORIGIN FOR THE GROUP (A): -43.5654 88.7844 32.0187
REMARK 3 T TENSOR
REMARK 3 T11: 0.3973 T22: 1.0107
REMARK 3 T33: 0.2756 T12: -0.2928
REMARK 3 T13: 0.0851 T23: -0.3400
REMARK 3 L TENSOR
REMARK 3 L11: 9.3121 L22: 13.9048
REMARK 3 L33: 28.8134 L12: -2.0621
REMARK 3 L13: -10.4954 L23: -12.6989
REMARK 3 S TENSOR
REMARK 3 S11: 0.2473 S12: 1.1217 S13: 0.1064
REMARK 3 S21: -1.5841 S22: 0.0494 S23: -0.0388
REMARK 3 S31: 1.2552 S32: -1.1993 S33: -0.2967
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 : F 26 F 41
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6242 15.2351 72.4985
REMARK 3 T TENSOR
REMARK 3 T11: 0.7470 T22: 0.7021
REMARK 3 T33: 0.3079 T12: 0.4545
REMARK 3 T13: -0.1108 T23: -0.3462
REMARK 3 L TENSOR
REMARK 3 L11: 5.7284 L22: 12.5675
REMARK 3 L33: 23.4462 L12: 6.7325
REMARK 3 L13: 0.1040 L23: -9.8489
REMARK 3 S TENSOR
REMARK 3 S11: 0.3817 S12: -0.6454 S13: -0.0909
REMARK 3 S21: 1.4515 S22: -0.1753 S23: -0.2498
REMARK 3 S31: -1.0820 S32: -0.3580 S33: -0.2064
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3N96 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059537.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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) : 1.07818
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59140
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.69000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 3N93
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 6000 0.1M SODIUM ACETATE(PH
REMARK 280 4.6) 0.1M MGCL2 14% GLYCEROL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 105.77550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, F, G, I, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, E, H, J, K
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 APPLY THE FOLLOWING TO CHAINS: A, I
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, J
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L
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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -371
REMARK 465 ALA A -370
REMARK 465 ASP A 104
REMARK 465 HIS A 105
REMARK 465 HIS A 106
REMARK 465 HIS A 107
REMARK 465 HIS A 108
REMARK 465 HIS A 109
REMARK 465 HIS A 110
REMARK 465 MET B -371
REMARK 465 ALA B -370
REMARK 465 LEU B 102
REMARK 465 ASP B 103
REMARK 465 ASP B 104
REMARK 465 HIS B 105
REMARK 465 HIS B 106
REMARK 465 HIS B 107
REMARK 465 HIS B 108
REMARK 465 HIS B 109
REMARK 465 HIS B 110
REMARK 465 MET C -371
REMARK 465 ALA C -370
REMARK 465 LEU C 31
REMARK 465 ASP C 32
REMARK 465 PRO C 33
REMARK 465 GLU C 34
REMARK 465 GLY C 35
REMARK 465 ASP C 103
REMARK 465 ASP C 104
REMARK 465 HIS C 105
REMARK 465 HIS C 106
REMARK 465 HIS C 107
REMARK 465 HIS C 108
REMARK 465 HIS C 109
REMARK 465 HIS C 110
REMARK 465 MET D -371
REMARK 465 ALA D -370
REMARK 465 LEU D 31
REMARK 465 ASP D 32
REMARK 465 PRO D 33
REMARK 465 GLU D 34
REMARK 465 GLY D 35
REMARK 465 ASP D 104
REMARK 465 HIS D 105
REMARK 465 HIS D 106
REMARK 465 HIS D 107
REMARK 465 HIS D 108
REMARK 465 HIS D 109
REMARK 465 HIS D 110
REMARK 465 SER G 26
REMARK 465 GLN G 27
REMARK 465 SER H 26
REMARK 465 GLN H 27
REMARK 465 ARG H 28
REMARK 465 GLU H 29
REMARK 465 ARG H 30
REMARK 465 ALA H 31
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR B 37 OE1 GLN C -5 1.89
REMARK 500 O ARG E 28 O HOH E 50 1.95
REMARK 500 CG2 VAL C -77 O HOH C 125 2.02
REMARK 500 CE2 TYR B 37 O VAL C -189 2.06
REMARK 500 O ALA C -224 O HOH C 130 2.07
REMARK 500 OH TYR A 37 OE1 GLN D -5 2.08
REMARK 500 OH TYR C -87 O HOH C 133 2.11
REMARK 500 CZ TYR B 37 O VAL C -189 2.12
REMARK 500 N MET C -146 O HOH C 130 2.15
REMARK 500 CE2 TYR A 37 O VAL D -189 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A-217 CG GLU A-217 CD 0.091
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A -26 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B -26 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASN D 69 N - CA - C ANGL. DEV. = 18.1 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-202 -93.81 -65.82
REMARK 500 ASN A-129 96.90 -69.45
REMARK 500 TYR A -87 -58.46 -122.54
REMARK 500 ASP A -74 -65.11 -90.93
REMARK 500 LEU A 31 -179.28 -63.84
REMARK 500 PRO A 33 10.18 -55.60
REMARK 500 GLU A 34 54.35 -151.63
REMARK 500 LEU A 102 14.75 -144.65
REMARK 500 ALA B-202 -92.20 -67.52
REMARK 500 ASN B-129 98.11 -69.94
REMARK 500 ASP B -74 -63.41 -92.70
REMARK 500 PRO B 33 9.33 -53.60
REMARK 500 GLU B 34 60.01 -153.19
REMARK 500 ASN B 69 61.44 37.88
REMARK 500 ALA C-202 -96.50 -76.02
REMARK 500 ASN C-197 74.24 49.28
REMARK 500 LYS C-119 46.97 37.04
REMARK 500 TYR C -87 -54.22 -121.24
REMARK 500 ASP C -74 -62.04 -103.32
REMARK 500 ASP C 25 4.14 -56.47
REMARK 500 ASN C 69 67.03 33.37
REMARK 500 ASN C 74 99.50 -69.49
REMARK 500 ILE D-262 -51.02 -121.04
REMARK 500 ALA D-202 -99.03 -76.18
REMARK 500 ASN D-197 76.14 48.76
REMARK 500 LYS D-119 45.03 35.19
REMARK 500 TYR D -87 -52.06 -124.49
REMARK 500 ASP D 25 6.49 -57.50
REMARK 500 PRO D 29 154.39 -49.97
REMARK 500 ASN D 69 50.43 30.58
REMARK 500 LEU D 102 -85.41 -128.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR C 37 SER C 38 -149.29
REMARK 500 TYR D 37 SER D 38 -145.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3N93 RELATED DB: PDB
REMARK 900 RELATED ID: 3N95 RELATED DB: PDB
DBREF 3N96 E 26 41 UNP P55089 UCN1_HUMAN 107 122
DBREF 3N96 F 26 41 UNP P55089 UCN1_HUMAN 107 122
DBREF 3N96 G 26 41 UNP P55089 UCN1_HUMAN 107 122
DBREF 3N96 H 26 41 UNP P55089 UCN1_HUMAN 107 122
DBREF 3N96 A -371 110 PDB 3N96 3N96 -371 110
DBREF 3N96 B -371 110 PDB 3N96 3N96 -371 110
DBREF 3N96 C -371 110 PDB 3N96 3N96 -371 110
DBREF 3N96 D -371 110 PDB 3N96 3N96 -371 110
SEQADV 3N96 NH2 E 42 UNP P55089 AMIDATION
SEQADV 3N96 NH2 F 42 UNP P55089 AMIDATION
SEQADV 3N96 NH2 G 42 UNP P55089 AMIDATION
SEQADV 3N96 NH2 H 42 UNP P55089 AMIDATION
SEQRES 1 A 482 MET ALA LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE
SEQRES 2 A 482 ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY
SEQRES 3 A 482 LYS LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL
SEQRES 4 A 482 GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL
SEQRES 5 A 482 ALA ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA
SEQRES 6 A 482 HIS ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU
SEQRES 7 A 482 ALA GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU
SEQRES 8 A 482 TYR PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS
SEQRES 9 A 482 LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU
SEQRES 10 A 482 ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR
SEQRES 11 A 482 TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA
SEQRES 12 A 482 LYS GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO
SEQRES 13 A 482 TYR PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR
SEQRES 14 A 482 ALA PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP
SEQRES 15 A 482 VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR
SEQRES 16 A 482 PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA
SEQRES 17 A 482 ASP THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS
SEQRES 18 A 482 GLY GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP
SEQRES 19 A 482 SER ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR
SEQRES 20 A 482 VAL LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE
SEQRES 21 A 482 VAL GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO
SEQRES 22 A 482 ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU
SEQRES 23 A 482 LEU THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS
SEQRES 24 A 482 PRO LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU
SEQRES 25 A 482 LEU ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN
SEQRES 26 A 482 ALA GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET
SEQRES 27 A 482 SER ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN
SEQRES 28 A 482 ALA ALA SER GLY ARG GLN THR VAL ASP GLU ALA LEU LYS
SEQRES 29 A 482 ASP ALA GLN THR ASN ALA ALA ALA GLU PHE ALA ALA LEU
SEQRES 30 A 482 LEU HIS SER LEU LEU GLU ALA ASN CYS SER LEU ALA LEU
SEQRES 31 A 482 ALA GLU GLU LEU LEU LEU ASP GLY TRP GLY PRO PRO LEU
SEQRES 32 A 482 ASP PRO GLU GLY PRO TYR SER TYR CYS ASN THR THR LEU
SEQRES 33 A 482 ASP GLN ILE GLY THR CYS TRP PRO ARG SER ALA ALA GLY
SEQRES 34 A 482 ALA LEU VAL GLU ARG PRO CYS PRO GLU TYR PHE ASN GLY
SEQRES 35 A 482 VAL LYS TYR ASN THR THR ARG ASN ALA TYR ARG GLU CYS
SEQRES 36 A 482 LEU GLU ASN GLY THR TRP ALA SER LYS ILE ASN TYR SER
SEQRES 37 A 482 GLN CYS GLU PRO ILE LEU ASP ASP HIS HIS HIS HIS HIS
SEQRES 38 A 482 HIS
SEQRES 1 B 482 MET ALA LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE
SEQRES 2 B 482 ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY
SEQRES 3 B 482 LYS LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL
SEQRES 4 B 482 GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL
SEQRES 5 B 482 ALA ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA
SEQRES 6 B 482 HIS ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU
SEQRES 7 B 482 ALA GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU
SEQRES 8 B 482 TYR PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS
SEQRES 9 B 482 LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU
SEQRES 10 B 482 ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR
SEQRES 11 B 482 TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA
SEQRES 12 B 482 LYS GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO
SEQRES 13 B 482 TYR PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR
SEQRES 14 B 482 ALA PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP
SEQRES 15 B 482 VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR
SEQRES 16 B 482 PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA
SEQRES 17 B 482 ASP THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS
SEQRES 18 B 482 GLY GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP
SEQRES 19 B 482 SER ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR
SEQRES 20 B 482 VAL LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE
SEQRES 21 B 482 VAL GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO
SEQRES 22 B 482 ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU
SEQRES 23 B 482 LEU THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS
SEQRES 24 B 482 PRO LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU
SEQRES 25 B 482 LEU ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN
SEQRES 26 B 482 ALA GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET
SEQRES 27 B 482 SER ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN
SEQRES 28 B 482 ALA ALA SER GLY ARG GLN THR VAL ASP GLU ALA LEU LYS
SEQRES 29 B 482 ASP ALA GLN THR ASN ALA ALA ALA GLU PHE ALA ALA LEU
SEQRES 30 B 482 LEU HIS SER LEU LEU GLU ALA ASN CYS SER LEU ALA LEU
SEQRES 31 B 482 ALA GLU GLU LEU LEU LEU ASP GLY TRP GLY PRO PRO LEU
SEQRES 32 B 482 ASP PRO GLU GLY PRO TYR SER TYR CYS ASN THR THR LEU
SEQRES 33 B 482 ASP GLN ILE GLY THR CYS TRP PRO ARG SER ALA ALA GLY
SEQRES 34 B 482 ALA LEU VAL GLU ARG PRO CYS PRO GLU TYR PHE ASN GLY
SEQRES 35 B 482 VAL LYS TYR ASN THR THR ARG ASN ALA TYR ARG GLU CYS
SEQRES 36 B 482 LEU GLU ASN GLY THR TRP ALA SER LYS ILE ASN TYR SER
SEQRES 37 B 482 GLN CYS GLU PRO ILE LEU ASP ASP HIS HIS HIS HIS HIS
SEQRES 38 B 482 HIS
SEQRES 1 C 482 MET ALA LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE
SEQRES 2 C 482 ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY
SEQRES 3 C 482 LYS LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL
SEQRES 4 C 482 GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL
SEQRES 5 C 482 ALA ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA
SEQRES 6 C 482 HIS ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU
SEQRES 7 C 482 ALA GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU
SEQRES 8 C 482 TYR PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS
SEQRES 9 C 482 LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU
SEQRES 10 C 482 ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR
SEQRES 11 C 482 TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA
SEQRES 12 C 482 LYS GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO
SEQRES 13 C 482 TYR PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR
SEQRES 14 C 482 ALA PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP
SEQRES 15 C 482 VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR
SEQRES 16 C 482 PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA
SEQRES 17 C 482 ASP THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS
SEQRES 18 C 482 GLY GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP
SEQRES 19 C 482 SER ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR
SEQRES 20 C 482 VAL LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE
SEQRES 21 C 482 VAL GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO
SEQRES 22 C 482 ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU
SEQRES 23 C 482 LEU THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS
SEQRES 24 C 482 PRO LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU
SEQRES 25 C 482 LEU ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN
SEQRES 26 C 482 ALA GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET
SEQRES 27 C 482 SER ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN
SEQRES 28 C 482 ALA ALA SER GLY ARG GLN THR VAL ASP GLU ALA LEU LYS
SEQRES 29 C 482 ASP ALA GLN THR ASN ALA ALA ALA GLU PHE ALA ALA LEU
SEQRES 30 C 482 LEU HIS SER LEU LEU GLU ALA ASN CYS SER LEU ALA LEU
SEQRES 31 C 482 ALA GLU GLU LEU LEU LEU ASP GLY TRP GLY PRO PRO LEU
SEQRES 32 C 482 ASP PRO GLU GLY PRO TYR SER TYR CYS ASN THR THR LEU
SEQRES 33 C 482 ASP GLN ILE GLY THR CYS TRP PRO ARG SER ALA ALA GLY
SEQRES 34 C 482 ALA LEU VAL GLU ARG PRO CYS PRO GLU TYR PHE ASN GLY
SEQRES 35 C 482 VAL LYS TYR ASN THR THR ARG ASN ALA TYR ARG GLU CYS
SEQRES 36 C 482 LEU GLU ASN GLY THR TRP ALA SER LYS ILE ASN TYR SER
SEQRES 37 C 482 GLN CYS GLU PRO ILE LEU ASP ASP HIS HIS HIS HIS HIS
SEQRES 38 C 482 HIS
SEQRES 1 D 482 MET ALA LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE
SEQRES 2 D 482 ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY
SEQRES 3 D 482 LYS LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL
SEQRES 4 D 482 GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL
SEQRES 5 D 482 ALA ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA
SEQRES 6 D 482 HIS ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU
SEQRES 7 D 482 ALA GLU ILE THR PRO ASP LYS ALA PHE GLN ASP LYS LEU
SEQRES 8 D 482 TYR PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS
SEQRES 9 D 482 LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU
SEQRES 10 D 482 ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR
SEQRES 11 D 482 TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA
SEQRES 12 D 482 LYS GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO
SEQRES 13 D 482 TYR PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR
SEQRES 14 D 482 ALA PHE LYS TYR GLU ASN GLY LYS TYR ASP ILE LYS ASP
SEQRES 15 D 482 VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR
SEQRES 16 D 482 PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA
SEQRES 17 D 482 ASP THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS
SEQRES 18 D 482 GLY GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP
SEQRES 19 D 482 SER ASN ILE ASP THR SER LYS VAL ASN TYR GLY VAL THR
SEQRES 20 D 482 VAL LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE
SEQRES 21 D 482 VAL GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO
SEQRES 22 D 482 ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU
SEQRES 23 D 482 LEU THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS
SEQRES 24 D 482 PRO LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU
SEQRES 25 D 482 LEU ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN
SEQRES 26 D 482 ALA GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET
SEQRES 27 D 482 SER ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN
SEQRES 28 D 482 ALA ALA SER GLY ARG GLN THR VAL ASP GLU ALA LEU LYS
SEQRES 29 D 482 ASP ALA GLN THR ASN ALA ALA ALA GLU PHE ALA ALA LEU
SEQRES 30 D 482 LEU HIS SER LEU LEU GLU ALA ASN CYS SER LEU ALA LEU
SEQRES 31 D 482 ALA GLU GLU LEU LEU LEU ASP GLY TRP GLY PRO PRO LEU
SEQRES 32 D 482 ASP PRO GLU GLY PRO TYR SER TYR CYS ASN THR THR LEU
SEQRES 33 D 482 ASP GLN ILE GLY THR CYS TRP PRO ARG SER ALA ALA GLY
SEQRES 34 D 482 ALA LEU VAL GLU ARG PRO CYS PRO GLU TYR PHE ASN GLY
SEQRES 35 D 482 VAL LYS TYR ASN THR THR ARG ASN ALA TYR ARG GLU CYS
SEQRES 36 D 482 LEU GLU ASN GLY THR TRP ALA SER LYS ILE ASN TYR SER
SEQRES 37 D 482 GLN CYS GLU PRO ILE LEU ASP ASP HIS HIS HIS HIS HIS
SEQRES 38 D 482 HIS
SEQRES 1 E 17 SER GLN ARG GLU ARG ALA GLU GLN ASN ARG ILE ILE PHE
SEQRES 2 E 17 ASP SER VAL NH2
SEQRES 1 F 17 SER GLN ARG GLU ARG ALA GLU GLN ASN ARG ILE ILE PHE
SEQRES 2 F 17 ASP SER VAL NH2
SEQRES 1 G 17 SER GLN ARG GLU ARG ALA GLU GLN ASN ARG ILE ILE PHE
SEQRES 2 G 17 ASP SER VAL NH2
SEQRES 1 H 17 SER GLN ARG GLU ARG ALA GLU GLN ASN ARG ILE ILE PHE
SEQRES 2 H 17 ASP SER VAL NH2
HET NH2 E 42 1
HET NH2 F 42 1
HET NH2 G 42 1
HET NH2 H 42 1
HET GLC I 1 12
HET GLC I 2 11
HET GLC J 1 12
HET GLC J 2 11
HET GLC K 1 12
HET GLC K 2 11
HET GLC L 1 12
HET GLC L 2 11
HETNAM NH2 AMINO GROUP
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
FORMUL 5 NH2 4(H2 N)
FORMUL 9 GLC 8(C6 H12 O6)
FORMUL 13 HOH *103(H2 O)
HELIX 1 1 GLY A -354 GLY A -338 1 17
HELIX 2 2 LYS A -328 ALA A -318 1 11
HELIX 3 3 ARG A -304 SER A -297 1 8
HELIX 4 4 ASP A -288 ASP A -283 1 6
HELIX 5 5 TYR A -280 VAL A -273 1 8
HELIX 6 6 THR A -242 GLU A -240 5 3
HELIX 7 7 GLU A -239 ALA A -229 1 11
HELIX 8 8 GLU A -217 ALA A -208 1 10
HELIX 9 9 ASN A -185 ASN A -169 1 17
HELIX 10 10 ASP A -161 LYS A -151 1 11
HELIX 11 11 GLY A -142 TRP A -140 5 3
HELIX 12 12 ALA A -139 LYS A -131 1 9
HELIX 13 13 ASN A -98 TYR A -87 1 12
HELIX 14 14 THR A -84 LYS A -75 1 10
HELIX 15 15 LEU A -66 ALA A -58 1 9
HELIX 16 16 ASP A -56 GLY A -43 1 14
HELIX 17 17 GLN A -35 SER A -18 1 18
HELIX 18 18 THR A -14 ASN A -3 1 12
HELIX 19 19 ASN A -3 GLY A 28 1 32
HELIX 20 20 GLY B -354 GLY B -338 1 17
HELIX 21 21 LYS B -328 ALA B -318 1 11
HELIX 22 22 ARG B -304 SER B -297 1 8
HELIX 23 23 ASP B -288 ASP B -283 1 6
HELIX 24 24 TYR B -280 VAL B -273 1 8
HELIX 25 25 GLU B -239 ALA B -229 1 11
HELIX 26 26 GLU B -217 PHE B -214 5 4
HELIX 27 27 THR B -213 ALA B -208 1 6
HELIX 28 28 ASN B -185 ASN B -169 1 17
HELIX 29 29 ASP B -161 LYS B -151 1 11
HELIX 30 30 GLY B -142 TRP B -140 5 3
HELIX 31 31 ALA B -139 LYS B -131 1 9
HELIX 32 32 ASN B -98 TYR B -87 1 12
HELIX 33 33 THR B -84 LYS B -75 1 10
HELIX 34 34 LEU B -66 ALA B -58 1 9
HELIX 35 35 ASP B -56 GLY B -43 1 14
HELIX 36 36 GLN B -35 SER B -18 1 18
HELIX 37 37 THR B -14 ASN B -3 1 12
HELIX 38 38 ASN B -3 GLY B 28 1 32
HELIX 39 39 GLY C -354 GLY C -338 1 17
HELIX 40 40 LYS C -328 ALA C -318 1 11
HELIX 41 41 ARG C -304 SER C -297 1 8
HELIX 42 42 ASP C -288 ASP C -283 1 6
HELIX 43 43 TYR C -280 VAL C -273 1 8
HELIX 44 44 THR C -242 GLU C -240 5 3
HELIX 45 45 GLU C -239 LYS C -228 1 12
HELIX 46 46 GLU C -217 ALA C -208 1 10
HELIX 47 47 ASN C -185 ASN C -169 1 17
HELIX 48 48 ASP C -161 LYS C -151 1 11
HELIX 49 49 GLY C -142 TRP C -140 5 3
HELIX 50 50 ALA C -139 LYS C -131 1 9
HELIX 51 51 ASN C -98 TYR C -87 1 12
HELIX 52 52 THR C -84 LYS C -75 1 10
HELIX 53 53 LEU C -66 ALA C -58 1 9
HELIX 54 54 ASP C -56 GLY C -43 1 14
HELIX 55 55 GLN C -35 SER C -18 1 18
HELIX 56 56 THR C -14 ALA C -1 1 14
HELIX 57 57 ALA C 0 GLY C 28 1 29
HELIX 58 58 GLY D -354 GLY D -338 1 17
HELIX 59 59 LYS D -328 ALA D -318 1 11
HELIX 60 60 ARG D -304 SER D -297 1 8
HELIX 61 61 ASP D -288 ASP D -283 1 6
HELIX 62 62 TYR D -280 VAL D -273 1 8
HELIX 63 63 THR D -242 GLU D -240 5 3
HELIX 64 64 GLU D -239 LYS D -228 1 12
HELIX 65 65 GLU D -217 ASP D -206 1 12
HELIX 66 66 ASN D -185 ASN D -169 1 17
HELIX 67 67 ASP D -161 LYS D -151 1 11
HELIX 68 68 GLY D -142 TRP D -140 5 3
HELIX 69 69 ALA D -139 LYS D -131 1 9
HELIX 70 70 ASN D -98 TYR D -87 1 12
HELIX 71 71 THR D -84 LYS D -75 1 10
HELIX 72 72 LEU D -66 ALA D -58 1 9
HELIX 73 73 ASP D -56 GLY D -43 1 14
HELIX 74 74 GLN D -35 GLY D -17 1 19
HELIX 75 75 THR D -14 ALA D -1 1 14
HELIX 76 76 ALA D 0 GLY D 28 1 29
HELIX 77 77 SER E 26 VAL E 41 1 16
HELIX 78 78 SER F 26 VAL F 41 1 16
HELIX 79 79 ARG G 30 VAL G 41 1 12
HELIX 80 80 GLU H 32 VAL H 41 1 10
SHEET 1 A 6 VAL A-335 GLU A-332 0
SHEET 2 A 6 LEU A-363 TRP A-360 1 N LEU A-363 O THR A-334
SHEET 3 A 6 ILE A-311 ALA A-307 1 O ILE A-311 N TRP A-360
SHEET 4 A 6 PHE A-112 ILE A-104 -1 O SER A-107 N TRP A-308
SHEET 5 A 6 TYR A-264 GLU A-259 -1 N ILE A-262 O LEU A-108
SHEET 6 A 6 ALA A -69 VAL A -68 -1 O ALA A -69 N VAL A-260
SHEET 1 B 5 VAL A-335 GLU A-332 0
SHEET 2 B 5 LEU A-363 TRP A-360 1 N LEU A-363 O THR A-334
SHEET 3 B 5 ILE A-311 ALA A-307 1 O ILE A-311 N TRP A-360
SHEET 4 B 5 PHE A-112 ILE A-104 -1 O SER A-107 N TRP A-308
SHEET 5 B 5 GLU A -42 ILE A -41 1 O GLU A -42 N VAL A-111
SHEET 1 C 2 ARG A-272 TYR A-271 0
SHEET 2 C 2 LYS A-268 LEU A-267 -1 O LYS A-268 N TYR A-271
SHEET 1 D 4 SER A-225 LEU A-223 0
SHEET 2 D 4 THR A-148 ASN A-143 1 O ALA A-147 N SER A-225
SHEET 3 D 4 SER A-256 ASN A-252 -1 N ILE A-254 O THR A-145
SHEET 4 D 4 TYR A-128 THR A-125 -1 O GLY A-127 N TYR A-253
SHEET 1 E 2 TYR A-203 GLU A-198 0
SHEET 2 E 2 LYS A-195 GLY A-188 -1 O LYS A-195 N GLU A-198
SHEET 1 F 2 TYR A 39 CYS A 40 0
SHEET 2 F 2 SER A 54 ALA A 55 -1 O SER A 54 N CYS A 40
SHEET 1 G 2 THR A 43 LEU A 44 0
SHEET 2 G 2 CYS A 50 TRP A 51 -1 O TRP A 51 N THR A 43
SHEET 1 H 2 LEU A 59 PRO A 63 0
SHEET 2 H 2 ASN A 78 GLU A 82 -1 O ALA A 79 N ARG A 62
SHEET 1 I 2 TYR A 67 PHE A 68 0
SHEET 2 I 2 VAL A 71 LYS A 72 -1 O VAL A 71 N PHE A 68
SHEET 1 J 6 VAL B-335 GLU B-332 0
SHEET 2 J 6 LEU B-363 TRP B-360 1 N ILE B-361 O GLU B-332
SHEET 3 J 6 ILE B-311 ALA B-307 1 O PHE B-309 N TRP B-360
SHEET 4 J 6 PHE B-112 ILE B-104 -1 O SER B-107 N TRP B-308
SHEET 5 J 6 TYR B-264 GLU B-259 -1 N ILE B-262 O LEU B-108
SHEET 6 J 6 ALA B -69 VAL B -68 -1 O ALA B -69 N VAL B-260
SHEET 1 K 5 VAL B-335 GLU B-332 0
SHEET 2 K 5 LEU B-363 TRP B-360 1 N ILE B-361 O GLU B-332
SHEET 3 K 5 ILE B-311 ALA B-307 1 O PHE B-309 N TRP B-360
SHEET 4 K 5 PHE B-112 ILE B-104 -1 O SER B-107 N TRP B-308
SHEET 5 K 5 GLU B -42 ILE B -41 1 O GLU B -42 N VAL B-111
SHEET 1 L 2 ARG B-272 TYR B-271 0
SHEET 2 L 2 LYS B-268 LEU B-267 -1 O LYS B-268 N TYR B-271
SHEET 1 M 4 SER B-225 LEU B-223 0
SHEET 2 M 4 THR B-148 ASN B-143 1 O ALA B-147 N SER B-225
SHEET 3 M 4 SER B-256 ASN B-252 -1 N ILE B-254 O THR B-145
SHEET 4 M 4 TYR B-128 THR B-125 -1 O GLY B-127 N TYR B-253
SHEET 1 N 2 TYR B-203 GLU B-198 0
SHEET 2 N 2 LYS B-195 GLY B-188 -1 O LYS B-195 N GLU B-198
SHEET 1 O 2 TYR B 39 CYS B 40 0
SHEET 2 O 2 SER B 54 ALA B 55 -1 O SER B 54 N CYS B 40
SHEET 1 P 2 THR B 43 LEU B 44 0
SHEET 2 P 2 CYS B 50 TRP B 51 -1 O TRP B 51 N THR B 43
SHEET 1 Q 2 LEU B 59 PRO B 63 0
SHEET 2 Q 2 ASN B 78 GLU B 82 -1 O ALA B 79 N ARG B 62
SHEET 1 R 2 TYR B 67 PHE B 68 0
SHEET 2 R 2 VAL B 71 LYS B 72 -1 O VAL B 71 N PHE B 68
SHEET 1 S 6 VAL C-335 GLU C-332 0
SHEET 2 S 6 LEU C-363 TRP C-360 1 N ILE C-361 O GLU C-332
SHEET 3 S 6 ILE C-311 ALA C-307 1 O PHE C-309 N TRP C-360
SHEET 4 S 6 PHE C-112 ASN C-103 -1 O GLY C-105 N ILE C-310
SHEET 5 S 6 TYR C-264 GLU C-259 -1 N ALA C-261 O LEU C-108
SHEET 6 S 6 ALA C -69 VAL C -68 -1 O ALA C -69 N VAL C-260
SHEET 1 T 3 LEU C-294 ALA C-293 0
SHEET 2 T 3 PHE C-112 ASN C-103 -1 O ILE C-104 N ALA C-293
SHEET 3 T 3 GLU C -42 ILE C -41 1 O GLU C -42 N VAL C-111
SHEET 1 U 2 ARG C-272 TYR C-271 0
SHEET 2 U 2 LYS C-268 LEU C-267 -1 O LYS C-268 N TYR C-271
SHEET 1 V 4 SER C-225 LEU C-223 0
SHEET 2 V 4 THR C-148 ASN C-143 1 O ALA C-147 N SER C-225
SHEET 3 V 4 SER C-256 ASN C-252 -1 N ILE C-254 O THR C-145
SHEET 4 V 4 TYR C-128 THR C-125 -1 O THR C-125 N LEU C-255
SHEET 1 W 2 TYR C-203 GLU C-198 0
SHEET 2 W 2 LYS C-195 GLY C-188 -1 O LYS C-195 N GLU C-198
SHEET 1 X 2 TYR C 39 CYS C 40 0
SHEET 2 X 2 SER C 54 ALA C 55 -1 O SER C 54 N CYS C 40
SHEET 1 Y 2 THR C 43 LEU C 44 0
SHEET 2 Y 2 CYS C 50 TRP C 51 -1 O TRP C 51 N THR C 43
SHEET 1 Z 2 LEU C 59 PRO C 63 0
SHEET 2 Z 2 ASN C 78 GLU C 82 -1 O ALA C 79 N ARG C 62
SHEET 1 AA 2 TYR C 67 PHE C 68 0
SHEET 2 AA 2 VAL C 71 LYS C 72 -1 O VAL C 71 N PHE C 68
SHEET 1 AB 6 VAL D-335 GLU D-332 0
SHEET 2 AB 6 LEU D-363 TRP D-360 1 N ILE D-361 O GLU D-332
SHEET 3 AB 6 ILE D-311 ALA D-307 1 O PHE D-309 N TRP D-360
SHEET 4 AB 6 PHE D-112 ASN D-103 -1 O GLY D-105 N ILE D-310
SHEET 5 AB 6 TYR D-264 GLU D-259 -1 N ALA D-261 O LEU D-108
SHEET 6 AB 6 ALA D -69 VAL D -68 -1 O ALA D -69 N VAL D-260
SHEET 1 AC 3 LEU D-294 ALA D-293 0
SHEET 2 AC 3 PHE D-112 ASN D-103 -1 O ILE D-104 N ALA D-293
SHEET 3 AC 3 GLU D -42 ILE D -41 1 O GLU D -42 N VAL D-111
SHEET 1 AD 2 ARG D-272 TYR D-271 0
SHEET 2 AD 2 LYS D-268 LEU D-267 -1 O LYS D-268 N TYR D-271
SHEET 1 AE 4 SER D-225 LEU D-223 0
SHEET 2 AE 4 THR D-148 ASN D-143 1 O ALA D-147 N SER D-225
SHEET 3 AE 4 SER D-256 ASN D-252 -1 N ILE D-254 O THR D-145
SHEET 4 AE 4 TYR D-128 THR D-125 -1 O THR D-125 N LEU D-255
SHEET 1 AF 2 TYR D-203 GLU D-198 0
SHEET 2 AF 2 LYS D-195 GLY D-188 -1 O ASP D-193 N LYS D-200
SHEET 1 AG 2 TYR D 39 CYS D 40 0
SHEET 2 AG 2 SER D 54 ALA D 55 -1 O SER D 54 N CYS D 40
SHEET 1 AH 2 THR D 43 LEU D 44 0
SHEET 2 AH 2 CYS D 50 TRP D 51 -1 O TRP D 51 N THR D 43
SHEET 1 AI 2 LEU D 59 PRO D 63 0
SHEET 2 AI 2 ASN D 78 GLU D 82 -1 O ALA D 79 N ARG D 62
SHEET 1 AJ 2 TYR D 67 PHE D 68 0
SHEET 2 AJ 2 VAL D 71 LYS D 72 -1 O VAL D 71 N PHE D 68
SSBOND 1 CYS A 14 CYS A 50 1555 1555 2.17
SSBOND 2 CYS A 40 CYS A 83 1555 1555 2.05
SSBOND 3 CYS A 64 CYS A 98 1555 1555 2.06
SSBOND 4 CYS B 14 CYS B 50 1555 1555 2.18
SSBOND 5 CYS B 40 CYS B 83 1555 1555 2.05
SSBOND 6 CYS B 64 CYS B 98 1555 1555 2.06
SSBOND 7 CYS C 14 CYS C 50 1555 1555 2.11
SSBOND 8 CYS C 40 CYS C 83 1555 1555 2.09
SSBOND 9 CYS C 64 CYS C 98 1555 1555 2.08
SSBOND 10 CYS D 14 CYS D 50 1555 1555 2.13
SSBOND 11 CYS D 40 CYS D 83 1555 1555 2.05
SSBOND 12 CYS D 64 CYS D 98 1555 1555 2.06
LINK O4 GLC I 1 C1 GLC I 2 1555 1555 1.38
LINK O4 GLC J 1 C1 GLC J 2 1555 1555 1.39
LINK O4 GLC K 1 C1 GLC K 2 1555 1555 1.40
LINK O4 GLC L 1 C1 GLC L 2 1555 1555 1.41
CRYST1 54.063 211.551 107.839 90.00 104.37 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018497 0.000000 0.004738 0.00000
SCALE2 0.000000 0.004727 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009572 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
