HEADER SIGNALING PROTEIN 09-SEP-15 5DN2
TITLE HUMAN NRP2 B1 DOMAIN IN COMPLEX WITH THE PEPTIDE CORRESPONDING TO THE
TITLE 2 C-TERMINUS OF VEGF-A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROPILIN-2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: NEUROPILIN-2 DOMAIN B1 F5/8 TYPE C 1, UNP RESIDUES 275-429;
COMPND 5 SYNONYM: VASCULAR ENDOTHELIAL CELL GROWTH FACTOR 165 RECEPTOR 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR A;
COMPND 9 CHAIN: F, G, E;
COMPND 10 FRAGMENT: VEGF-A165-HBD, UNP RESIDUES 205-232;
COMPND 11 SYNONYM: VEGF-A,VASCULAR PERMEABILITY FACTOR,VPF;
COMPND 12 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: NRP2, VEGF165R2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: ROSETTA-GAMI 2(DE3)PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET15B-TEV;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: VEGFA, VEGF;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 20 EXPRESSION_SYSTEM_VARIANT: SHUFFLE;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS SIGNALING PROTEIN, NEUROPILIN-2, VEGFA, ANGIOGENESIS, HEPARIN,
KEYWDS 2 RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.C.I.TSAI,P.FRANKEL,C.FOTINOU,R.RANA,I.ZACHARY,S.DJORDJEVIC
REVDAT 2 10-JAN-24 5DN2 1 REMARK
REVDAT 1 20-JUL-16 5DN2 0
JRNL AUTH Y.C.TSAI,C.FOTINOU,R.RANA,T.YELLAND,P.FRANKEL,I.ZACHARY,
JRNL AUTH 2 S.DJORDJEVIC
JRNL TITL STRUCTURAL STUDIES OF NEUROPILIN-2 REVEAL A ZINC ION BINDING
JRNL TITL 2 SITE REMOTE FROM THE VASCULAR ENDOTHELIAL GROWTH FACTOR
JRNL TITL 3 BINDING POCKET.
JRNL REF FEBS J. V. 283 1921 2016
JRNL REFN ISSN 1742-464X
JRNL PMID 26991001
JRNL DOI 10.1111/FEBS.13711
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 56630
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3006
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4069
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 199
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5160
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 269
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.29000
REMARK 3 B22 (A**2) : -1.79000
REMARK 3 B33 (A**2) : -0.50000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.162
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.187
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5359 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5049 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7262 ; 1.463 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11550 ; 0.923 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 651 ; 7.298 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 277 ;37.852 ;23.213
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 922 ;13.207 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;16.589 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 774 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6159 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1367 ; 0.001 ; 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): 2571 ; 0.919 ; 1.849
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2570 ; 0.912 ; 1.848
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3206 ; 1.594 ; 2.753
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3207 ; 1.594 ; 2.754
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2788 ; 0.910 ; 2.027
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2788 ; 0.908 ; 2.027
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4047 ; 1.549 ; 2.981
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5806 ; 4.245 ;14.871
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5807 ; 4.245 ;14.876
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 274 A 429 5
REMARK 3 1 B 274 B 429 5
REMARK 3 1 C 274 C 429 5
REMARK 3 1 D 274 D 429 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 907 ; 0.19 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 907 ; 0.17 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 907 ; 0.17 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 907 ; 0.14 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 1451 ; 0.50 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 1451 ; 0.60 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 1451 ; 0.54 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 1451 ; 0.53 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 907 ; 2.18 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 907 ; 1.63 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 907 ; 1.37 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 907 ; 2.37 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1451 ; 2.54 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 1451 ; 1.87 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 1451 ; 1.65 ; 10.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 1451 ; 2.64 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
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 274 A 429
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7913 43.0668 -3.7927
REMARK 3 T TENSOR
REMARK 3 T11: 0.0239 T22: 0.1380
REMARK 3 T33: 0.0544 T12: 0.0060
REMARK 3 T13: -0.0021 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.3164 L22: 1.1550
REMARK 3 L33: 0.7942 L12: -0.3823
REMARK 3 L13: 0.3992 L23: -0.1826
REMARK 3 S TENSOR
REMARK 3 S11: 0.0561 S12: -0.0260 S13: -0.0203
REMARK 3 S21: -0.1616 S22: -0.0468 S23: 0.0722
REMARK 3 S31: 0.0255 S32: 0.0752 S33: -0.0094
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 274 B 429
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3514 26.6766 -3.6816
REMARK 3 T TENSOR
REMARK 3 T11: 0.0219 T22: 0.1382
REMARK 3 T33: 0.0630 T12: 0.0082
REMARK 3 T13: 0.0270 T23: 0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.2048 L22: 1.2594
REMARK 3 L33: 0.6560 L12: -0.2311
REMARK 3 L13: -0.2657 L23: -0.0163
REMARK 3 S TENSOR
REMARK 3 S11: 0.0259 S12: -0.0338 S13: 0.0142
REMARK 3 S21: -0.1480 S22: -0.0647 S23: -0.0965
REMARK 3 S31: 0.0183 S32: -0.0753 S33: 0.0388
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 274 C 429
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2794 55.4990 -24.0966
REMARK 3 T TENSOR
REMARK 3 T11: 0.0756 T22: 0.0831
REMARK 3 T33: 0.0236 T12: -0.0068
REMARK 3 T13: -0.0166 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.6453 L22: 0.1865
REMARK 3 L33: 0.8729 L12: 0.0967
REMARK 3 L13: -0.0277 L23: -0.2607
REMARK 3 S TENSOR
REMARK 3 S11: -0.0149 S12: -0.0780 S13: 0.0170
REMARK 3 S21: -0.0025 S22: 0.0200 S23: 0.0222
REMARK 3 S31: 0.0284 S32: 0.0631 S33: -0.0050
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 274 D 429
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0978 55.4516 24.2083
REMARK 3 T TENSOR
REMARK 3 T11: 0.0794 T22: 0.0887
REMARK 3 T33: 0.0104 T12: 0.0228
REMARK 3 T13: -0.0042 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.6538 L22: 0.1356
REMARK 3 L33: 1.0199 L12: -0.0093
REMARK 3 L13: 0.0225 L23: 0.3191
REMARK 3 S TENSOR
REMARK 3 S11: 0.0060 S12: 0.0876 S13: 0.0515
REMARK 3 S21: 0.0189 S22: 0.0074 S23: -0.0069
REMARK 3 S31: 0.0852 S32: -0.0242 S33: -0.0133
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 0
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0000 0.0000 0.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0660 T22: 0.0660
REMARK 3 T33: 0.0660 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: -0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 5DN2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000212805.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59661
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 86.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.22300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2QQJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG20000, 0.1M BICINE, 2% V/V
REMARK 280 DIOXANE, PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.02000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.02000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 55.12500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 69.76000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 55.12500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.76000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.02000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 55.12500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.76000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.02000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 55.12500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 69.76000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER F 205
REMARK 465 CYS F 206
REMARK 465 LYS F 207
REMARK 465 ASN F 208
REMARK 465 THR F 209
REMARK 465 ASP F 210
REMARK 465 SER F 211
REMARK 465 ARG F 212
REMARK 465 CYS F 213
REMARK 465 LYS F 214
REMARK 465 ALA F 215
REMARK 465 ARG F 216
REMARK 465 GLN F 217
REMARK 465 LEU F 218
REMARK 465 GLU F 219
REMARK 465 LEU F 220
REMARK 465 ASN F 221
REMARK 465 GLU F 222
REMARK 465 ARG F 223
REMARK 465 THR F 224
REMARK 465 CYS F 225
REMARK 465 ARG F 226
REMARK 465 CYS F 227
REMARK 465 ASP F 228
REMARK 465 SER G 205
REMARK 465 CYS G 206
REMARK 465 LYS G 207
REMARK 465 ASN G 208
REMARK 465 THR G 209
REMARK 465 ASP G 210
REMARK 465 SER G 211
REMARK 465 ARG G 212
REMARK 465 CYS G 213
REMARK 465 LYS G 214
REMARK 465 ALA G 215
REMARK 465 ARG G 216
REMARK 465 GLN G 217
REMARK 465 LEU G 218
REMARK 465 GLU G 219
REMARK 465 LEU G 220
REMARK 465 ASN G 221
REMARK 465 GLU G 222
REMARK 465 ARG G 223
REMARK 465 THR G 224
REMARK 465 CYS G 225
REMARK 465 ARG G 226
REMARK 465 CYS G 227
REMARK 465 ASP G 228
REMARK 465 SER E 205
REMARK 465 CYS E 206
REMARK 465 LYS E 207
REMARK 465 ASN E 208
REMARK 465 THR E 209
REMARK 465 ASP E 210
REMARK 465 SER E 211
REMARK 465 ARG E 212
REMARK 465 CYS E 213
REMARK 465 LYS E 214
REMARK 465 ALA E 215
REMARK 465 ARG E 216
REMARK 465 GLN E 217
REMARK 465 LEU E 218
REMARK 465 GLU E 219
REMARK 465 LEU E 220
REMARK 465 ASN E 221
REMARK 465 GLU E 222
REMARK 465 ARG E 223
REMARK 465 THR E 224
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 LYS F 229 CG CD CE NZ
REMARK 470 LYS G 229 CG CD CE NZ
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 303 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 278 30.76 -147.91
REMARK 500 HIS A 312 17.42 59.91
REMARK 500 ASN A 316 -131.33 53.02
REMARK 500 ARG A 334 -28.57 74.14
REMARK 500 ALA A 386 -123.00 -117.95
REMARK 500 SER A 416 -45.59 69.03
REMARK 500 ASN B 278 31.11 -148.50
REMARK 500 ASN B 316 -135.82 54.33
REMARK 500 ARG B 334 -30.10 75.15
REMARK 500 ALA B 386 -126.64 -115.18
REMARK 500 SER B 416 -44.17 74.71
REMARK 500 ASN C 278 27.12 -144.26
REMARK 500 TRP C 304 47.97 -142.10
REMARK 500 ASN C 316 -136.23 50.16
REMARK 500 ARG C 334 -32.99 75.52
REMARK 500 ALA C 386 -123.13 -120.13
REMARK 500 SER C 416 -38.13 67.60
REMARK 500 ASN D 278 27.21 -146.08
REMARK 500 TRP D 304 50.75 -140.83
REMARK 500 ASN D 316 -137.77 50.52
REMARK 500 ARG D 334 -37.31 78.32
REMARK 500 GLN D 353 12.24 58.41
REMARK 500 ALA D 386 -123.46 -117.48
REMARK 500 SER D 416 -42.93 69.16
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 DIO B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DIO D 501
DBREF 5DN2 A 275 429 UNP O60462 NRP2_HUMAN 275 429
DBREF 5DN2 B 275 429 UNP O60462 NRP2_HUMAN 275 429
DBREF 5DN2 C 275 429 UNP O60462 NRP2_HUMAN 275 429
DBREF 5DN2 D 275 429 UNP O60462 NRP2_HUMAN 275 429
DBREF 5DN2 F 205 232 UNP P15692 VEGFA_HUMAN 205 232
DBREF 5DN2 G 205 232 UNP P15692 VEGFA_HUMAN 205 232
DBREF 5DN2 E 205 232 UNP P15692 VEGFA_HUMAN 205 232
SEQADV 5DN2 MET A 274 UNP O60462 INITIATING METHIONINE
SEQADV 5DN2 MET B 274 UNP O60462 INITIATING METHIONINE
SEQADV 5DN2 MET C 274 UNP O60462 INITIATING METHIONINE
SEQADV 5DN2 MET D 274 UNP O60462 INITIATING METHIONINE
SEQRES 1 A 156 MET PHE GLN CYS ASN VAL PRO LEU GLY MET GLU SER GLY
SEQRES 2 A 156 ARG ILE ALA ASN GLU GLN ILE SER ALA SER SER THR TYR
SEQRES 3 A 156 SER ASP GLY ARG TRP THR PRO GLN GLN SER ARG LEU HIS
SEQRES 4 A 156 GLY ASP ASP ASN GLY TRP THR PRO ASN LEU ASP SER ASN
SEQRES 5 A 156 LYS GLU TYR LEU GLN VAL ASP LEU ARG PHE LEU THR MET
SEQRES 6 A 156 LEU THR ALA ILE ALA THR GLN GLY ALA ILE SER ARG GLU
SEQRES 7 A 156 THR GLN ASN GLY TYR TYR VAL LYS SER TYR LYS LEU GLU
SEQRES 8 A 156 VAL SER THR ASN GLY GLU ASP TRP MET VAL TYR ARG HIS
SEQRES 9 A 156 GLY LYS ASN HIS LYS VAL PHE GLN ALA ASN ASN ASP ALA
SEQRES 10 A 156 THR GLU VAL VAL LEU ASN LYS LEU HIS ALA PRO LEU LEU
SEQRES 11 A 156 THR ARG PHE VAL ARG ILE ARG PRO GLN THR TRP HIS SER
SEQRES 12 A 156 GLY ILE ALA LEU ARG LEU GLU LEU PHE GLY CYS ARG VAL
SEQRES 1 B 156 MET PHE GLN CYS ASN VAL PRO LEU GLY MET GLU SER GLY
SEQRES 2 B 156 ARG ILE ALA ASN GLU GLN ILE SER ALA SER SER THR TYR
SEQRES 3 B 156 SER ASP GLY ARG TRP THR PRO GLN GLN SER ARG LEU HIS
SEQRES 4 B 156 GLY ASP ASP ASN GLY TRP THR PRO ASN LEU ASP SER ASN
SEQRES 5 B 156 LYS GLU TYR LEU GLN VAL ASP LEU ARG PHE LEU THR MET
SEQRES 6 B 156 LEU THR ALA ILE ALA THR GLN GLY ALA ILE SER ARG GLU
SEQRES 7 B 156 THR GLN ASN GLY TYR TYR VAL LYS SER TYR LYS LEU GLU
SEQRES 8 B 156 VAL SER THR ASN GLY GLU ASP TRP MET VAL TYR ARG HIS
SEQRES 9 B 156 GLY LYS ASN HIS LYS VAL PHE GLN ALA ASN ASN ASP ALA
SEQRES 10 B 156 THR GLU VAL VAL LEU ASN LYS LEU HIS ALA PRO LEU LEU
SEQRES 11 B 156 THR ARG PHE VAL ARG ILE ARG PRO GLN THR TRP HIS SER
SEQRES 12 B 156 GLY ILE ALA LEU ARG LEU GLU LEU PHE GLY CYS ARG VAL
SEQRES 1 C 156 MET PHE GLN CYS ASN VAL PRO LEU GLY MET GLU SER GLY
SEQRES 2 C 156 ARG ILE ALA ASN GLU GLN ILE SER ALA SER SER THR TYR
SEQRES 3 C 156 SER ASP GLY ARG TRP THR PRO GLN GLN SER ARG LEU HIS
SEQRES 4 C 156 GLY ASP ASP ASN GLY TRP THR PRO ASN LEU ASP SER ASN
SEQRES 5 C 156 LYS GLU TYR LEU GLN VAL ASP LEU ARG PHE LEU THR MET
SEQRES 6 C 156 LEU THR ALA ILE ALA THR GLN GLY ALA ILE SER ARG GLU
SEQRES 7 C 156 THR GLN ASN GLY TYR TYR VAL LYS SER TYR LYS LEU GLU
SEQRES 8 C 156 VAL SER THR ASN GLY GLU ASP TRP MET VAL TYR ARG HIS
SEQRES 9 C 156 GLY LYS ASN HIS LYS VAL PHE GLN ALA ASN ASN ASP ALA
SEQRES 10 C 156 THR GLU VAL VAL LEU ASN LYS LEU HIS ALA PRO LEU LEU
SEQRES 11 C 156 THR ARG PHE VAL ARG ILE ARG PRO GLN THR TRP HIS SER
SEQRES 12 C 156 GLY ILE ALA LEU ARG LEU GLU LEU PHE GLY CYS ARG VAL
SEQRES 1 D 156 MET PHE GLN CYS ASN VAL PRO LEU GLY MET GLU SER GLY
SEQRES 2 D 156 ARG ILE ALA ASN GLU GLN ILE SER ALA SER SER THR TYR
SEQRES 3 D 156 SER ASP GLY ARG TRP THR PRO GLN GLN SER ARG LEU HIS
SEQRES 4 D 156 GLY ASP ASP ASN GLY TRP THR PRO ASN LEU ASP SER ASN
SEQRES 5 D 156 LYS GLU TYR LEU GLN VAL ASP LEU ARG PHE LEU THR MET
SEQRES 6 D 156 LEU THR ALA ILE ALA THR GLN GLY ALA ILE SER ARG GLU
SEQRES 7 D 156 THR GLN ASN GLY TYR TYR VAL LYS SER TYR LYS LEU GLU
SEQRES 8 D 156 VAL SER THR ASN GLY GLU ASP TRP MET VAL TYR ARG HIS
SEQRES 9 D 156 GLY LYS ASN HIS LYS VAL PHE GLN ALA ASN ASN ASP ALA
SEQRES 10 D 156 THR GLU VAL VAL LEU ASN LYS LEU HIS ALA PRO LEU LEU
SEQRES 11 D 156 THR ARG PHE VAL ARG ILE ARG PRO GLN THR TRP HIS SER
SEQRES 12 D 156 GLY ILE ALA LEU ARG LEU GLU LEU PHE GLY CYS ARG VAL
SEQRES 1 F 28 SER CYS LYS ASN THR ASP SER ARG CYS LYS ALA ARG GLN
SEQRES 2 F 28 LEU GLU LEU ASN GLU ARG THR CYS ARG CYS ASP LYS PRO
SEQRES 3 F 28 ARG ARG
SEQRES 1 G 28 SER CYS LYS ASN THR ASP SER ARG CYS LYS ALA ARG GLN
SEQRES 2 G 28 LEU GLU LEU ASN GLU ARG THR CYS ARG CYS ASP LYS PRO
SEQRES 3 G 28 ARG ARG
SEQRES 1 E 28 SER CYS LYS ASN THR ASP SER ARG CYS LYS ALA ARG GLN
SEQRES 2 E 28 LEU GLU LEU ASN GLU ARG THR CYS ARG CYS ASP LYS PRO
SEQRES 3 E 28 ARG ARG
HET DIO B 501 6
HET GOL B 502 6
HET DIO D 501 6
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 8 DIO 2(C4 H8 O2)
FORMUL 9 GOL C3 H8 O3
FORMUL 11 HOH *269(H2 O)
HELIX 1 AA1 ALA A 289 GLU A 291 5 3
HELIX 2 AA2 THR A 305 SER A 309 5 5
HELIX 3 AA3 ALA B 289 GLU B 291 5 3
HELIX 4 AA4 THR B 305 SER B 309 5 5
HELIX 5 AA5 ALA C 289 GLU C 291 5 3
HELIX 6 AA6 THR C 305 SER C 309 5 5
HELIX 7 AA7 ALA D 289 GLU D 291 5 3
HELIX 8 AA8 THR D 305 SER D 309 5 5
SHEET 1 A 4 ILE A 293 ALA A 295 0
SHEET 2 A 4 LEU A 329 ASP A 332 -1
SHEET 3 A 4 PHE A 406 PRO A 411 -1
SHEET 4 A 4 TYR A 361 SER A 366 -1
SHEET 1 B 3 LEU A 402 THR A 404 0
SHEET 2 B 3 THR A 337 GLN A 345 -1
SHEET 3 B 3 ARG A 421 ARG A 428 -1
SHEET 1 C 2 ALA A 341 THR A 344 0
SHEET 2 C 2 VAL A 394 LYS A 397 -1
SHEET 1 D 2 TYR A 357 SER A 360 0
SHEET 2 D 2 THR A 413 HIS A 415 -1
SHEET 1 E 4 ILE B 293 ALA B 295 0
SHEET 2 E 4 LEU B 329 ASP B 332 -1
SHEET 3 E 4 PHE B 406 PRO B 411 -1
SHEET 4 E 4 TYR B 361 SER B 366 -1
SHEET 1 F 3 LEU B 402 THR B 404 0
SHEET 2 F 3 THR B 337 GLN B 345 -1
SHEET 3 F 3 ARG B 421 ARG B 428 -1
SHEET 1 G 2 ALA B 341 THR B 344 0
SHEET 2 G 2 VAL B 394 LYS B 397 -1
SHEET 1 H 2 TYR B 357 SER B 360 0
SHEET 2 H 2 THR B 413 HIS B 415 -1
SHEET 1 I 5 ILE C 293 ALA C 295 0
SHEET 2 I 5 LEU C 329 ASP C 332 -1
SHEET 3 I 5 PHE C 406 PRO C 411 -1
SHEET 4 I 5 SER C 360 SER C 366 -1
SHEET 5 I 5 VAL C 383 GLN C 385 -1
SHEET 1 J 3 LEU C 402 THR C 404 0
SHEET 2 J 3 THR C 337 GLN C 345 -1
SHEET 3 J 3 ARG C 421 CYS C 427 -1
SHEET 1 K 2 ALA C 341 THR C 344 0
SHEET 2 K 2 VAL C 394 LYS C 397 -1
SHEET 1 L 2 TYR C 357 SER C 360 0
SHEET 2 L 2 THR C 413 HIS C 415 -1
SHEET 1 M 4 ILE D 293 ALA D 295 0
SHEET 2 M 4 LEU D 329 ASP D 332 -1
SHEET 3 M 4 PHE D 406 PRO D 411 -1
SHEET 4 M 4 TYR D 361 SER D 366 -1
SHEET 1 N 3 LEU D 402 THR D 404 0
SHEET 2 N 3 THR D 337 GLN D 345 -1
SHEET 3 N 3 ARG D 421 CYS D 427 -1
SHEET 1 O 2 ALA D 341 THR D 344 0
SHEET 2 O 2 VAL D 394 LYS D 397 -1
SHEET 1 P 2 TYR D 357 SER D 360 0
SHEET 2 P 2 THR D 413 HIS D 415 -1
SSBOND 1 CYS A 277 CYS A 427 1555 1555 2.05
SSBOND 2 CYS B 277 CYS B 427 1555 1555 2.05
SSBOND 3 CYS C 277 CYS C 427 1555 1555 2.07
SSBOND 4 CYS D 277 CYS D 427 1555 1555 2.06
SITE 1 AC1 4 MET B 274 VAL C 374 TYR C 375 ARG C 376
SITE 1 AC2 2 ARG B 428 VAL B 429
SITE 1 AC3 4 MET A 274 VAL D 374 TYR D 375 ARG D 376
CRYST1 110.250 139.520 106.040 90.00 90.00 90.00 C 2 2 21 32
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 0.009070 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007167 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009430 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
